|
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 ... |
43-147 |
7.83e-75 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 244.62 E-value: 7.83e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 43 DRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNI 122
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1988774682 123 RNDDIADGNPKLTLGLIWTIILHFQ 147
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
40-158 |
3.46e-72 |
|
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: 237.62 E-value: 3.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 40 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKL 119
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1988774682 120 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSE 158
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
35-156 |
2.94e-69 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 229.49 E-value: 2.94e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 35 MDGRKDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRH 114
Cdd:cd21236 7 LERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKR 86
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1988774682 115 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 156
Cdd:cd21236 87 RQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
160-265 |
3.48e-65 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 217.20 E-value: 3.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 160 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 239
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1988774682 240 PEDVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
161-265 |
6.50e-63 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 210.33 E-value: 6.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 240
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1988774682 241 EDVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
40-157 |
1.18e-60 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 204.50 E-value: 1.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 40 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKL 119
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1988774682 120 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 157
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
161-265 |
3.43e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 194.05 E-value: 3.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 240
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1988774682 241 EDVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
45-148 |
3.05e-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: 174.49 E-value: 3.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 45 VQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNIR 123
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1988774682 124 NDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
159-265 |
9.81e-49 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 170.22 E-value: 9.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 159 DMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLL 238
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1988774682 239 DPEDVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
40-144 |
4.80e-48 |
|
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: 168.31 E-value: 4.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 40 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLRHRQVK 118
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRVH 90
|
90 100
....*....|....*....|....*.
gi 1988774682 119 LVNIRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21246 91 LENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
161-261 |
1.26e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 163.74 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 240
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1988774682 241 EDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
41-148 |
1.25e-44 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 158.69 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 41 ERDRVQKKTFTKWVNKHLIKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLRHRQ 116
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1988774682 117 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
161-261 |
3.64e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 156.79 E-value: 3.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 240
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1988774682 241 EDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
39-144 |
4.07e-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: 4.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 39 KDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLrHRQV 117
Cdd:cd21193 10 QEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL-KTKV 88
|
90 100
....*....|....*....|....*..
gi 1988774682 118 KLVNIRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21193 89 RLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
40-144 |
2.98e-41 |
|
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: 149.79 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 40 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLRHRQVK 118
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQRVH 112
|
90 100
....*....|....*....|....*.
gi 1988774682 119 LVNIRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21318 113 LENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
41-148 |
3.36e-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: 148.87 E-value: 3.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 41 ERDRVQKKTFTKWVNKHLIKAQRH--VTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLRHRQ 116
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1988774682 117 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
44-261 |
5.61e-41 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 163.19 E-value: 5.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 44 RVQKKTFTKWVNKHLIKA-QRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 121 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQvngQSEDMTAKEKLLLWSQRMTDGYQ-GIRCDNFTTSWRDGKLFNAVI 199
Cdd:COG5069 88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 200 HKHYPRLINMGKVYQQTNLE--NLEQAFSVAEKDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLY 261
Cdd:COG5069 165 HDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
29-144 |
1.77e-40 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 147.51 E-value: 1.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 29 QGMLKAMdgrKDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQI 107
Cdd:cd21317 18 RSRIKAL---ADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDK 94
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774682 108 ALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21317 95 ALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
896-973 |
1.65e-39 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 142.36 E-value: 1.65e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774682 896 LSWQYLMRDFTQIRSWNITMLKTMKPEEYRLIMRNLELHYQDFMRDSQDSQLFGPDDRMQVEDDYTKSTQHFDNLLRS 973
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
148-263 |
2.37e-39 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 143.66 E-value: 2.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 148 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 227
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774682 228 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
157-261 |
5.05e-39 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 142.45 E-value: 5.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 157 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTR 236
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1988774682 237 LLDPEDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
160-265 |
7.99e-39 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 141.69 E-value: 7.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 160 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 239
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1988774682 240 PEDVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
41-148 |
6.30e-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: 139.20 E-value: 6.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 41 ERDRVQKKTFTKWVNKHLIKAQ--RHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVK 118
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1988774682 119 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
45-146 |
9.54e-38 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 138.69 E-value: 9.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 45 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLRHRQVKLVNI 122
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1988774682 123 RNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
43-144 |
9.94e-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: 138.68 E-value: 9.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 43 DRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLRHRQVKLVN 121
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1988774682 122 IRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
160-261 |
4.57e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 136.92 E-value: 4.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 160 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 239
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1988774682 240 PEDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1316-1895 |
1.50e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 152.78 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1316 QEYVTLRTRYSEL-MTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQlaeahakAIAKAEKEAQE 1394
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL-------ELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1395 LKLKMQEEVSKreiaavdAEKQKTNIQLELQELKNLSEQQIKDKSQqvdealhsRTKIEEEIRLIRIQLETTEKQKYTAE 1474
Cdd:COG1196 286 AQAEEYELLAE-------LARLEQDIARLEERRRELEERLEELEEE--------LAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1475 SELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQV 1554
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1555 KQAEIEKEKQIkvAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELE 1634
Cdd:COG1196 431 AELEEEEEEEE--EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1635 KWRQKANEALR------LRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQ 1708
Cdd:COG1196 509 GVKAALLLAGLrglagaVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1709 QKLTAEQELIRLRA-------DFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtm 1781
Cdd:COG1196 589 AAALARGAIGAAVDlvasdlrEADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS-- 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1782 snTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEK 1861
Cdd:COG1196 667 --RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
570 580 590
....*....|....*....|....*....|....
gi 1988774682 1862 EAENERLRRQAEDEAYQRKALEDQASQHKQEIEE 1895
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1340-2582 |
4.65e-36 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 151.90 E-value: 4.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1340 TDTQRRLDDEEKAAEKLKAEERKKMAEMQAELdkqkqlaeaHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEkqktn 1419
Cdd:NF041483 90 ADAERELRDARAQTQRILQEHAEHQARLQAEL---------HTEAVQRRQQLDQELAERRQTVESHVNENVAWAE----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1420 iqlelqELKNLSEQQIKdksQQVDEalhSRTKIEEEIRLIRIQLE--TTE-KQKYTAESELKQlrdraAEAEKLRKLAQD 1496
Cdd:NF041483 156 ------QLRARTESQAR---RLLDE---SRAEAEQALAAARAEAErlAEEaRQRLGSEAESAR-----AEAEAILRRARK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1497 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQaeEAERQVKQAEIEKEKQIKVAHEAAQKS- 1575
Cdd:NF041483 219 DAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAAAKQl 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1576 AAAELQSKHMSfaeKTSKLEeslkqehgaVLQLQQEAERlkkqqeDAENSREEAEKELEKWRQkanEALRLRLQAEDEAh 1655
Cdd:NF041483 297 ASAESANEQRT---RTAKEE---------IARLVGEATK------EAEALKAEAEQALADARA---EAEKLVAEAAEKA- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1656 kKTLAQEEAEKQKEEAEREAKK-RAKAEESALKQKEMAEEELERQRKIAESTAQqkltaeqeliRLRAD-FDNAEQQRSL 1733
Cdd:NF041483 355 -RTVAAEDTAAQLAKAARTAEEvLTKASEDAKATTRAAAEEAERIRREAEAEAD----------RLRGEaADQAEQLKGA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1734 LEDELYRLKNEVAAAQQQRKQLEDELAKVRSE-MDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEAsrlrais 1812
Cdd:NF041483 424 AKDDTKEYRAKTVELQEEARRLRGEAEQLRAEaVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADADEL------- 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1813 eeakhqRQIAEEEAARQRAEAerilkeklaaISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQE 1892
Cdd:NF041483 497 ------RSTATAESERVRTEA----------IERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1893 IEEKIVQLKKS----------------------------SEAEMERQKAiVDDTLKQRRVVEEEIRILKLNFEK------ 1938
Cdd:NF041483 561 ETERAIAARQAeaaeeltrlhteaeerltaaeealadarAEAERIRREA-AEETERLRTEAAERIRTLQAQAEQeaerlr 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1939 ------ASSGKLDLE-----------LELNKLKNIADETQQsKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEE 2001
Cdd:NF041483 640 teaaadASAARAEGEnvavrlrseaaAEAERLKSEAQESAD-RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEET 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2002 AARQRKAALEELERLRKKAEE----ARKQKDEADKEAEKQIVVA-QQAAQKCSAAEQQvqsvlAQQIEDSIT--QKKLKE 2074
Cdd:NF041483 719 LGSARAEADQERERAREQSEEllasARKRVEEAQAEAQRLVEEAdRRATELVSAAEQT-----AQQVRDSVAglQEQAEE 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2075 EYEKakklakeaeaakekaereaalLRQQAEE-AERQKTaaeeeaanqaKAQEDAERLRKEAeFEAAKRAQAEAAALMQK 2153
Cdd:NF041483 794 EIAG---------------------LRSAAEHaAERTRT----------EAQEEADRVRSDA-YAERERASEDANRLRRE 841
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2154 QQADTEMAkhKKLAEQTLKQKFQvEQEltkvKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVK----VQ 2229
Cdd:NF041483 842 AQEETEAA--KALAERTVSEAIA-EAE----RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQ 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2230 MEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMR-KLAEDAARLSVEAQ-EAARLRQIAEDDLNQQRALAEKMLKE 2307
Cdd:NF041483 915 ADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGSAQQHAERIRTE 994
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2308 KMQAIQEASrlkAEAEMLQKQkdlAQEQAQKLL-EDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSqls 2386
Cdd:NF041483 995 AERVKAEAA---AEAERLRTE---AREEADRTLdEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTT--- 1065
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2387 eaqARAEEEAKKFKKQADKVATRLHETeiATQEKMTVVERleferlnTSKEADDL-----RKAIA---DLENEKARLKKE 2458
Cdd:NF041483 1066 ---TEAEAQADTMVGAARKEAERIVAE--ATVEGNSLVEK-------ARTDADELlvgarRDATAireRAEELRDRITGE 1133
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2459 AEELQNKSK-EMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQE 2537
Cdd:NF041483 1134 IEELHERARrESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVRE 1213
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*
gi 1988774682 2538 KKTLQATMDAalskqkEAEEEMLRKQKEMQELERQRleqERILAE 2582
Cdd:NF041483 1214 AEKIKAEAEA------EAKRTVEEGKRELDVLVRRR---EDINAE 1249
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
157-261 |
1.21e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 133.26 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 157 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTR 236
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1988774682 237 LLDPEDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
40-148 |
3.09e-35 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 131.58 E-value: 3.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 40 DERDRVQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVK 118
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1988774682 119 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
164-265 |
9.23e-35 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 129.86 E-value: 9.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 164 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 242
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1988774682 243 VDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1401-1976 |
9.23e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 147.01 E-value: 9.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1401 EEVSKR----EIAAVDAEKQKTnIQLELQELK-NLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAES 1475
Cdd:COG1196 196 GELERQleplERQAEKAERYRE-LKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1476 ELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVK 1555
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1556 QAEIEKEKQIKVAHEAAQKSAAAE-----LQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAE 1630
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEeeleeLAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1631 KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 1710
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1711 LTAEQELIRLRAD---FDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKS 1787
Cdd:COG1196 515 LLAGLRGLAGAVAvliGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1788 KQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAE--EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAEn 1865
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAArlEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1866 ERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEkassgKLD 1945
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE-----ELL 748
|
570 580 590
....*....|....*....|....*....|.
gi 1988774682 1946 LELELNKLKNIADETQQskiraEEEAEKLRK 1976
Cdd:COG1196 749 EEEALEELPEPPDLEEL-----ERELERLER 774
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
145-261 |
1.68e-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: 130.17 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 145 HFQISDIQVNGQSEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQA 224
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774682 225 FSVAEKDLGVTRLLDPEDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1306-2061 |
4.35e-34 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 145.20 E-value: 4.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1306 KLDSASDNIIQEYVTLRTRYSELMTLTSQY---IKFitdtqRRLDDEEKAAEKL-----KAEERKKMAEMQAELDKQKQL 1377
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLERQAekaERY-----KELKAELRELELAllvlrLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1378 AEAHAKAIAKAEKEAQELKLKMQE------------EVSKREIAAVDAEKQKTNiqlelQELKNLsEQQIKDKSQQVDEA 1445
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSEleeeieelqkelYALANEISRLEQQKQILR-----ERLANL-ERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1446 LHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEA 1525
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1526 EKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHgav 1605
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA--- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1606 lQLQQEAERLKKQQEDAENsREEAEKELEKWRQKANEAL-----RLRLQAEDEAHKKTLAQEEAEKQKEeaerEAKKRAK 1680
Cdd:TIGR02168 486 -QLQARLDSLERLQENLEG-FSEGVKALLKNQSGLSGILgvlseLISVDEGYEAAIEAALGGRLQAVVV----ENLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1681 AEESALKQKE-----MAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLK--NEVAAAQQQRK 1753
Cdd:TIGR02168 560 KAIAFLKQNElgrvtFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvDDLDNALELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1754 QLEDELAKVRSEMDIL----IQLKtKAEKETMSNTEKSKQLLEAEaAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQ 1829
Cdd:TIGR02168 640 KLRPGYRIVTLDGDLVrpggVITG-GSAKTNSSILERRREIEELE-EKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1830 RAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEdQASQHKQEIEEKIVQLkkssEAEME 1909
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEEL----EAQIE 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1910 RQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAE 1989
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 1990 EKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQ 2061
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1341-1976 |
6.60e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 145.28 E-value: 6.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1341 DTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAiAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTni 1420
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-- 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1421 qlELQELKNLSEQQIKDKSQQVDEALHSRTKIEEeirliriqlettekqKYTAESELKQLRDRAAEAEKLRKLAqdEAEK 1500
Cdd:PTZ00121 1358 --EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE---------------KKKADEAKKKAEEDKKKADELKKAA--AAKK 1418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1501 LRKQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKALEdleklrmqAEEAERQVKQAEiEKEKQIKVAHEAAQKSAAAEL 1580
Cdd:PTZ00121 1419 KADEAKKKAEEKKKA-DEAKKKAEEAKKADEAKKKAEE--------AKKAEEAKKKAE-EAKKADEAKKKAEEAKKADEA 1488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1581 QSKhmsfAEKTSKLEESLKQEHGAvlqlQQEAERLKKQQE--DAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKT 1658
Cdd:PTZ00121 1489 KKK----AEEAKKKADEAKKAAEA----KKKADEAKKAEEakKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1659 LAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRaDFDNAEQQRSLLEDEL 1738
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLK 1639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1739 YRLKNEVAAAQQQRKqlEDELAKVRSEmdiliQLKTKAEKEtmsnTEKSKQLLEAEAAKMKdlAEEASRLRAisEEAKHQ 1818
Cdd:PTZ00121 1640 KKEAEEKKKAEELKK--AEEENKIKAA-----EEAKKAEED----KKKAEEAKKAEEDEKK--AAEALKKEA--EEAKKA 1704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1819 RQIAEEEAARQRaEAERILKEKLAAISEATRLKTEAEialkEKEAENERLRRQAEDeayqrkalEDQASQHKQEIEEKIV 1898
Cdd:PTZ00121 1705 EELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEAE----EDKKKAEEAKKDEEE--------KKKIAHLKKEEEKKAE 1771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1899 QLKKSSEAEMErqKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAD----ETQQSKIRAEEEAEKL 1974
Cdd:PTZ00121 1772 EIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDsaikEVADSKNMQLEEADAF 1849
|
..
gi 1988774682 1975 RK 1976
Cdd:PTZ00121 1850 EK 1851
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
161-261 |
2.89e-33 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 125.98 E-value: 2.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 240
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1988774682 241 EDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
40-144 |
7.50e-33 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 126.70 E-value: 7.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 40 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLRHRQVK 118
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 127
|
90 100
....*....|....*....|....*.
gi 1988774682 119 LVNIRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21316 128 LENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1771-2641 |
8.21e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 141.82 E-value: 8.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1771 QLKTKAEKETmsnTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAE---EEAARQRAEAERILKEKLAAISEA 1847
Cdd:PTZ00121 1083 AKEDNRADEA---TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEarkAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1848 TRLKTEAEIALKEKEAENERLRRQAEDeayQRKALEDQASQHKQEIE-----EKIVQLKKSSEAEMERQKAIVDDTLKQR 1922
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEaarkaEEERKAEEARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1923 RVVEEEIRIlklnfEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEA 2002
Cdd:PTZ00121 1237 KDAEEAKKA-----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2003 ARQRKA---------ALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSV--LAQQIEDSITQKK 2071
Cdd:PTZ00121 1312 EEAKKAdeakkkaeeAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2072 LKEEyekakklakeaeaakekaereaalLRQQAEEAERQktaaEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALM 2151
Cdd:PTZ00121 1392 KADE------------------------AKKKAEEDKKK----ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA 1443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2152 QKQQADTEMAKHKKLAEQtLKQKFQVEQELTKVKLKLDETDKQksvldEELQRLKDEVDDAVKQRGQVEEElfkvKVQME 2231
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEE-AKKKAEEAKKADEAKKKAEEAKKA-----DEAKKKAEEAKKKADEAKKAAEA----KKKAD 1513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2232 ELLKLKNKIEEENQRLIKKDKDSTQKLLAEE---AENMRKLAE----DAARLSVEAQEAARLRQIAEDDLNQQRALAEKM 2304
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEkkkADELKKAEElkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2305 LKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERkrqleimaEAERLRLQVSQ 2384
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK--------AEEENKIKAAE 1665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2385 LSEAQARAEEEAKKFKKqADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQN 2464
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKK-AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2465 KSKEMA--DAQQKKIEH---EKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfeeevKKAKALKDEQERQKQQMEQEKK 2539
Cdd:PTZ00121 1745 KAEEAKkdEEEKKKIAHlkkEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD-----KKIKDIFDNFANIIEGGKEGNL 1819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2540 TLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQK----LREKLQQLEDAQKDQHTRETDKVLHKDIi 2615
Cdd:PTZ00121 1820 VINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKeadfNKEKDLKEDDEEEIEEADEIEKIDKDDI- 1898
|
890 900
....*....|....*....|....*.
gi 1988774682 2616 hltTIETTKTVYNGQNVGDVVDGIDK 2641
Cdd:PTZ00121 1899 ---EREIPNNNMAGKNNDIIDDKLDK 1921
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
44-149 |
4.51e-32 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 122.95 E-value: 4.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 44 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLRHRQ-VKLV 120
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1988774682 121 NIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1494-2347 |
1.65e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 137.58 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1494 AQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRmQAEEAERQVKQAEIEKEKQIKVAHEAAQ 1573
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR-KAEDAKRVEIARKAEDARKAEEARKAED 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1574 -KSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDaenSREEAEKELEKWRQKANEALRLRLQAED 1652
Cdd:PTZ00121 1175 aKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA---KKAEAVKKAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1653 EAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEEL---ERQRKIAESTAQQKLTAEQELIRLRADFDNAEQ 1729
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1730 QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDiliQLKTKAEKEtmsntekskqllEAEAAKMKdlAEEASRLR 1809
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA---EKKKEEAKK------------KADAAKKK--AEEKKKAD 1394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1810 AISEEAKHQRQIAEE----EAARQRAEAeriLKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQ 1885
Cdd:PTZ00121 1395 EAKKKAEEDKKKADElkkaAAAKKKADE---AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1886 ASQHKQEIEEKIVQLKKSSEAEMERQKAivdDTLKQRrvveEEIRILKLNFEKASSGKLDLELELNKLKNIADETQqski 1965
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKA---DEAKKA----AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK---- 1540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1966 RAEE--EAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQ----RKAALEELERLRKKAEEARKQKDEADKEAEKQIV 2039
Cdd:PTZ00121 1541 KAEEkkKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2040 VAQQAAQkcsaaEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAA 2119
Cdd:PTZ00121 1621 KAEELKK-----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2120 NQAKAQEDAERLRKEAEFEAAkraqaeaaalmQKQQADTEMAKHKKLAEQTLKQKfqvEQELTKV-KLKLDETDKQKsvl 2198
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKK-----------KAEELKKAEEENKIKAEEAKKEA---EEDKKKAeEAKKDEEEKKK--- 1758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2199 deeLQRLKDEVDDAVKQRGQVEEELFKvkvqmEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSV 2278
Cdd:PTZ00121 1759 ---IAHLKKEEEKKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDS 1830
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774682 2279 EAQEAArlrqiaeDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQ 2347
Cdd:PTZ00121 1831 AIKEVA-------DSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEK 1892
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
45-148 |
2.18e-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: 120.47 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 45 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLRHRQVKLVNI 122
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1988774682 123 RNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
160-258 |
2.80e-31 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 120.22 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 160 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 239
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1988774682 240 PEDVDVPHPDEKSIITYVS 258
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
45-148 |
3.79e-31 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 119.73 E-value: 3.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 45 VQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNIR 123
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1988774682 124 NDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
148-263 |
1.33e-30 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 118.40 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 148 ISDIQvngqSEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 227
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774682 228 AEKDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLYDA 263
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
160-258 |
2.51e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 117.63 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 160 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 239
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1988774682 240 PEDVDVPHPDEKSIITYVS 258
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
164-266 |
3.42e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 117.34 E-value: 3.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 164 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLDPE 241
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1988774682 242 DVDVPHPDEKSIITYVSSLYDAMPR 266
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
41-150 |
3.44e-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: 117.30 E-value: 3.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 41 ERDRVQKKTFTKWVNKHLIKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLRHRQ 116
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1988774682 117 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 150
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
164-265 |
8.40e-30 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 115.83 E-value: 8.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 164 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 242
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1988774682 243 VDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
44-146 |
2.17e-29 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 114.89 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 44 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1988774682 121 NIRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
166-261 |
3.57e-29 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 113.98 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 166 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED-VD 244
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1988774682 245 VPHPDEKSIITYVSSLY 261
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1500-2110 |
6.49e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 128.13 E-value: 6.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1500 KLRKqvsEETQKK-RQAEEELKRKSEAEKEAAKQkqkaledLEKLRMQAEEAER--QVKQAEIEKEKQIKVAH------- 1569
Cdd:COG1196 171 KERK---EEAERKlEATEENLERLEDILGELERQ-------LEPLERQAEKAERyrELKEELKELEAELLLLKlreleae 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1570 EAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQ 1649
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1650 AEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQ 1729
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1730 QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLR 1809
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1810 AISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQH 1889
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1890 KQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEE 1969
Cdd:COG1196 561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1970 EAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCS 2049
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 2050 AAEQQVQSVLAQQIEdsITQKKLKEEYEKAKKLAKEAEAAKEKAEReaalLRQQAEEAERQ 2110
Cdd:COG1196 721 LEEEALEEQLEAERE--ELLEELLEEEELLEEEALEELPEPPDLEE----LERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1485-2341 |
4.06e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 125.55 E-value: 4.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1485 AEAEKLRKLAQDEAEKLR-KQVSEETQKK-RQAEEELKRKSEAEKEAAKQkqkaledLEKLRMQAEEAER------QVKQ 1556
Cdd:TIGR02168 152 AKPEERRAIFEEAAGISKyKERRKETERKlERTRENLDRLEDILNELERQ-------LKSLERQAEKAERykelkaELRE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1557 AEIE---KEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAEN--SREEAEK 1631
Cdd:TIGR02168 225 LELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeiSRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1632 ELEKWRQKANEALRLRLQAEDEAHKKTLAQEEaekqkeeaeREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKL 1711
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELA---------EELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1712 TAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDiliqlkTKAEKETMSNTEKSKQLL 1791
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE------EAELKELQAELEELEEEL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1792 EAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEaerilKEKLAAISEATRLKTEAEIALKEKEAE------- 1864
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR-----LDSLERLQENLEGFSEGVKALLKNQSGlsgilgv 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1865 -NERLRRQAEDE----AYQRKALEDQASQHKQEIEEKIVQLKKSS-------EAEMERQKAIVDDTLKQRRVVEEEIRIL 1932
Cdd:TIGR02168 525 lSELISVDEGYEaaieAALGGRLQAVVVENLNAAKKAIAFLKQNElgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1933 KLNFEKASSGKLDLELELNKL---KNIADETQQSKIRAEEE-------------------AEKLRKLALEEEKRRREAEE 1990
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYLLGGVlvvDDLDNALELAKKLRPGYrivtldgdlvrpggvitggSAKTNSSILERRREIEELEE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1991 KVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDeadkEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQiedSITQK 2070
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELE----ELSRQISALRKDLARLEAEVEQLEERIAQL---SKELT 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2071 KLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTaaeEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAAL 2150
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK---ALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2151 MQKQQADTEMAKHKKLAEQTLK---QKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVK 2227
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESlaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2228 vqmEELLKLKNKIEEENQRLikkdkdstQKLLAEEAENMRKLAEDAarlSVEAQEAARLRQIAEDDLNQQRALAEKmLKE 2307
Cdd:TIGR02168 915 ---RELEELREKLAQLELRL--------EGLEVRIDNLQERLSEEY---SLTLEEAEALENKIEDDEEEARRRLKR-LEN 979
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1988774682 2308 K--------MQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE 2341
Cdd:TIGR02168 980 KikelgpvnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
146-263 |
3.47e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 109.40 E-value: 3.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 146 FQISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAF 225
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1988774682 226 SVAEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
148-263 |
5.58e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 108.63 E-value: 5.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 148 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 227
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774682 228 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
44-146 |
7.77e-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: 107.57 E-value: 7.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 44 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1988774682 121 NIRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
39-148 |
2.75e-26 |
|
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: 106.77 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 39 KDERDRVQKKTFTKWVNKHLIKAQRHV--TDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLRHR 115
Cdd:cd21247 14 QEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKTK 93
|
90 100 110
....*....|....*....|....*....|....
gi 1988774682 116 -QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21247 94 vPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1343-1902 |
3.72e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 119.86 E-value: 3.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1343 QRRLDDEEKAAEKL--KAEERKKMAEMQAELDKQKQLAEAHAKAiAKAEKEAQELKlKMQEEVSKREIAAVDAEKQKTNI 1420
Cdd:PTZ00121 1370 EKKKEEAKKKADAAkkKAEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAK-KKAEEKKKADEAKKKAEEAKKAD 1447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1421 QLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAE----SELKQLRDRAAEAEKLRKL--A 1494
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkaAEAKKKADEAKKAEEAKKAdeA 1527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1495 QDEAEKLRKQVSEETQKKRQAEEELK----RKSEaEKEAAKQKQKALEDLEKLRMQAEEAeRQVKQAEIEK-----EKQI 1565
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKaeelKKAE-EKKKAEEAKKAEEDKNMALRKAEEA-KKAEEARIEEvmklyEEEK 1605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1566 KVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGavlQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALR 1645
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA---EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1646 lrlqAEDEAHKKtlaqeeaekqKEEAEREAKKRAKAEEsaLKQKEmaEEELERQRKIAESTAQQKLTAEQELIRLRADFD 1725
Cdd:PTZ00121 1683 ----AEEDEKKA----------AEALKKEAEEAKKAEE--LKKKE--AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1726 NAEQQRSLLEDelyrlKNEVaaaQQQRKQLEDELAKVRSEMDILIQ--LKTKAEKETMSNTEKSKQLL------------ 1791
Cdd:PTZ00121 1745 KAEEAKKDEEE-----KKKI---AHLKKEEEKKAEEIRKEKEAVIEeeLDEEDEKRRMEVDKKIKDIFdnfaniieggke 1816
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1792 ---------EAEAAKMKDLAEEASRLRAISEE-AKHQRQIAEEEAARQRAEA----ERILKEKLAAISEATRLKTEAEIA 1857
Cdd:PTZ00121 1817 gnlvindskEMEDSAIKEVADSKNMQLEEADAfEKHKFNKNNENGEDGNKEAdfnkEKDLKEDDEEEIEEADEIEKIDKD 1896
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1988774682 1858 LKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKK 1902
Cdd:PTZ00121 1897 DIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIKISK 1941
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
44-149 |
4.24e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 106.27 E-value: 4.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 44 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1988774682 121 NIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1674-2593 |
4.61e-26 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 118.92 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1674 EAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRadfDNAEQQRSLLEDELYRLKNEVAAAQQQRK 1753
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALE---YYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1754 QLEDELAKVRSEMDILIQLKTKAEKETmsntEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEA 1833
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKL----AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1834 ERILKEKLAAISEATRLKTEAEIALKEKEaENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKa 1913
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKELK-ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1914 ivddtlKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIaDETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVK 1993
Cdd:pfam02463 395 ------EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI-LEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1994 KIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVaqqaaqkcsaaeQQVQSVLAQQIEDSITQKKLK 2073
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA------------LIKDGVGGRIISAHGRLGDLG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2074 EEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQK 2153
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2154 QQADTEMAKHKKLAEQTLKQKFQveqelTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEEL 2233
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLK-----ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2234 lKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRklaedaarlsveaqeaARLRQIAEDDLNQQRALAEKMLKEKMQAIQ 2313
Cdd:pfam02463 691 -KEEILRRQLEIKKKEQREKEELKKLKLEAEELL----------------ADRVQEAQDKINEELKLLKQKIDEEEEEEE 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2314 EASRLKAEAEMLQKQkdlaQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAE 2393
Cdd:pfam02463 754 KSRLKKEEKEEEKSE----LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2394 EEAKKFKKQADKVATRLHETEIATQEKMTVverLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQ 2473
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERL---EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEES 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2474 QKKIEHEKTVLQQTFMTEKEmlLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTL------------ 2541
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEE--AEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELgkvnlmaieefe 984
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 1988774682 2542 --QATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQ 2593
Cdd:pfam02463 985 ekEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFF 1038
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1824-2607 |
1.25e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 117.46 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1824 EEAA------RQRAEAERilkeKLAAISEA-TRLkteaEIALKEKEAENERLRRQAEdEAYQRKALEDQASQHK------ 1890
Cdd:TIGR02168 162 EEAAgiskykERRKETER----KLERTRENlDRL----EDILNELERQLKSLERQAE-KAERYKELKAELRELElallvl 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1891 --QEIEEKIVQLKkSSEAEMERQKAIVDDTLKqrrVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAE 1968
Cdd:TIGR02168 233 rlEELREELEELQ-EELKEAEEELEELTAELQ---ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1969 EEAEKLRKlaleeekrrreaeeKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKC 2048
Cdd:TIGR02168 309 ERLANLER--------------QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2049 SAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDA 2128
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2129 ERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQE----LTKVKLKLD----------ETDKQ 2194
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkaLLKNQSGLSgilgvlseliSVDEG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2195 KS-----VLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKL 2269
Cdd:TIGR02168 535 YEaaieaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2270 A----------------EDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAI---QEASRLKAEAEMLQKQKD 2330
Cdd:TIGR02168 615 RkalsyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILerrREIEELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2331 LAQEQAQKLLEDkqlmQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRL 2410
Cdd:TIGR02168 695 ELEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2411 HETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKsKEMADAQQKKIEHEKTVLQQTFMT 2490
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2491 EKEMLLKKEKLIEDEKKRLEsQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQ--E 2568
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAqlE 928
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1988774682 2569 LERQRLEQEriLAEENQKLREKLQ-QLEDAQKDQHTRETD 2607
Cdd:TIGR02168 929 LRLEGLEVR--IDNLQERLSEEYSlTLEEAEALENKIEDD 966
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
164-263 |
1.72e-25 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 103.52 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 164 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED- 242
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1988774682 243 VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1626-2260 |
2.26e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 116.57 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1626 REEAEKELEKWRQKANEALR-LRLQAEDEAHKKTLAQEEAekqkeeaeREAKKRAKAEESALKQKEMAEEELERQRKIAE 1704
Cdd:COG1196 195 LGELERQLEPLERQAEKAERyRELKEELKELEAELLLLKL--------RELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1705 STAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNT 1784
Cdd:COG1196 267 AELEE---LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1785 EKSKQLLEAEAAKMKDLAEEASRL----RAISEEAKHQRQIAEEEAARQRAEAErILKEKLAAISEATRLKTEAEIALKE 1860
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALleaeAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1861 KEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRI-LKLNFEKA 1939
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLlLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1940 SSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKK 2019
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2020 AEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAqqiEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAAL 2099
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL---GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2100 LRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQ 2179
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2180 ELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQR---GQV----EEELFKVKVQMEELLKLKNKIEEENQRL---IK 2249
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIealGPVnllaIEEYEELEERYDFLSEQREDLEEARETLeeaIE 819
|
650
....*....|..
gi 1988774682 2250 K-DKDSTQKLLA 2260
Cdd:COG1196 820 EiDRETRERFLE 831
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1234-1903 |
2.72e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 116.31 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1234 KIQAVPITDSKTLKEQLAQEKK--LLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVspLKKTKLDSAS 1311
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1312 DNIIQEYVTLRTRYSELmtltSQYIKFITDTQRRLDDEEKAAEKLKAEERKK-------MAEMQAELDKQKQLAEAHAKA 1384
Cdd:TIGR02168 284 EELQKELYALANEISRL----EQQKQILRERLANLERQLEELEAQLEELESKldelaeeLAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1385 IAKAEKEAQELKLKM---QEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEE-EIRLIR 1460
Cdd:TIGR02168 360 LEELEAELEELESRLeelEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1461 IQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAE---EELKRKSEAEKEAAKQK---- 1533
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLErlqENLEGFSEGVKALLKNQsgls 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1534 ----------------QKALEDLEKLRMQA---EEAERQVKQAEIEKEKQI-KVAHEAAQKSAAAELQSKHM-------- 1585
Cdd:TIGR02168 520 gilgvlselisvdegyEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELgRVTFLPLDSIKGTEIQGNDReilknieg 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1586 ---------SFAEKTSKLEESL--------------------------------------------KQEHGAVLQLQQEA 1612
Cdd:TIGR02168 600 flgvakdlvKFDPKLRKALSYLlggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsAKTNSSILERRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1613 ERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMA 1692
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1693 EEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSL-------LEDELYRLKNEVAAAQQQRKQLEDELAKVRSE 1765
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealdeLRAELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1766 MDILIQlKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAIS 1845
Cdd:TIGR02168 840 LEDLEE-QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 1846 EATRLKTEAEIALKEKEAE----NERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKS 1903
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
148-263 |
4.66e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 103.27 E-value: 4.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 148 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 227
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774682 228 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
160-266 |
5.50e-25 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 102.36 E-value: 5.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 160 MTAKEKLLLWSQRMTDGY-QGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQT--NLENLEQAFSVAEKDLGVTR 236
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEfdKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1988774682 237 -LLDPEDVDvpHPDEKSIITYVSSLYDAMPR 266
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1343-2216 |
5.77e-25 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 115.45 E-value: 5.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1343 QRRLDDEEKAAE----KLKAEERKKMAEMQAELDKQ---KQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEK 1415
Cdd:pfam02463 153 ERRLEIEEEAAGsrlkRKKKEALKKLIEETENLAELiidLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1416 QKTNIQLELQELKNLSEQQIKDKSQQVDEalhsrtKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQ 1495
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIE------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1496 DEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKS 1575
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1576 AAA------ELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQ 1649
Cdd:pfam02463 387 SSAaklkeeELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1650 AEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQ-----KLTAEQELIRLRADF 1724
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISahgrlGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1725 DNAEQQRSLLEDELYRLKNEVAA-------AQQQRKQLEDELAKVRS----EMDILIQLKTKAEKETMSNTEKSKQLLEA 1793
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRAltelplgARKLRLLIPKLKLPLKSiavlEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1794 EAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKlaaiseaTRLKTEAEIALKEKEAENERLRRQAE 1873
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTK-------ELLEIQELQEKAESELAKEEILRRQL 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1874 DEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRilklnfEKASSGKLDLELELNKL 1953
Cdd:pfam02463 700 EIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR------LKKEEKEEEKSELSLKE 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1954 KNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKE 2033
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2034 AEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAErqkta 2113
Cdd:pfam02463 854 EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE----- 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2114 AEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMaKHKKLAEQTLKQKFQVEQELTKVKLKLDETDK 2193
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKV-NLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007
|
890 900
....*....|....*....|...
gi 1988774682 2194 QKSVLDEELQRLKDEVDDAVKQR 2216
Cdd:pfam02463 1008 IRAIIEETCQRLKEFLELFVSIN 1030
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
166-261 |
1.29e-24 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 101.07 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 166 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED-VD 244
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1988774682 245 VPHPDEKSIITYVSSLY 261
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1387-2317 |
2.39e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 113.23 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1387 KAEKEAQELKL-KMQEEVSKREIAAVDAEKQKTNIQL------ELQELKN-LSEQQIKDKSQQVDEALHSRTKIEEEIRL 1458
Cdd:TIGR02168 171 KERRKETERKLeRTRENLDRLEDILNELERQLKSLERqaekaeRYKELKAeLRELELALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1459 IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALE 1538
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1539 DLEKLrmQAEEAERQVKQAEIEKEKQikvaheaAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQ 1618
Cdd:TIGR02168 331 KLDEL--AEELAELEEKLEELKEELE-------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1619 QEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAqeeaekqkeeaereakKRAKAEESALKQKEMAEEELER 1698
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE----------------ELEEELEELQEELERLEEALEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1699 QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDeLYRLKNEVAAAQQQRKQLED---ELAKVRS--EMDILIQLK 1773
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEG-FSEGVKALLKNQSGLSGILGvlsELISVDEgyEAAIEAALG 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1774 TKAEKETMSNTEKSKQLLEA--EAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRA--------EAERILKEKLAA 1843
Cdd:TIGR02168 545 GRLQAVVVENLNAAKKAIAFlkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAkdlvkfdpKLRKALSYLLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1844 ISEATRLKTEAEIALKEKEAEN------ERLRRQAedeayqrkaledqasqhkqeieekiVQLKKSSEAEMERqkaivdd 1917
Cdd:TIGR02168 625 VLVVDDLDNALELAKKLRPGYRivtldgDLVRPGG-------------------------VITGGSAKTNSSI------- 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1918 tLKQRRvveeEIRILKLNFEKASSGKLDLELELNKLKNIADEtqqskirAEEEAEKLRKLALEEEKRRREAEEKVKKIAA 1997
Cdd:TIGR02168 673 -LERRR----EIEELEEKIEELEEKIAELEKALAELRKELEE-------LEEELEQLRKELEELSRQISALRKDLARLEA 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1998 AEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQqiedsitQKKLKEEYE 2077
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-------LDELRAELT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2078 KAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEaakraqaEAAALMQKQQAD 2157
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-------LEALLNERASLE 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2158 TEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDdavKQRGQVEEElfkVKVQMEELLKLK 2237
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID---NLQERLSEE---YSLTLEEAEALE 960
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2238 NKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEdaarlsveaqeaarLRQIAE--DDLNQQRALAEKMLKEKMQAIQEA 2315
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKELGPVNLAAIEE--------------YEELKEryDFLTAQKEDLTEAKETLEEAIEEI 1026
|
..
gi 1988774682 2316 SR 2317
Cdd:TIGR02168 1027 DR 1028
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
48-145 |
2.86e-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: 100.08 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 48 KTFTKWVNKHLIKA-QRHVTDLYEDLRDGHNLISLLEVLSGETLPREK---GRMRFHKLQNVQIALDFLRHRQVKLVNIR 123
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1988774682 124 NDDIADGnPKLTLGLIWTIILH 145
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1784-2459 |
3.69e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.34 E-value: 3.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1784 TEKSKQL--LEAEAAKmkdlaeeASRLRAISEEAKhQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEK 1861
Cdd:COG1196 196 GELERQLepLERQAEK-------AERYRELKEELK-ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1862 EAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAivdDTLKQRRVVEEEIRILKLNFEKASS 1941
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE---ELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1942 GKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLrkkaE 2021
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL----E 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2022 EARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLR 2101
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2102 QQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAaLMQKQQADTEMAKHKKLAEQTLKQKFQVEQEL 2181
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA-LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2182 TKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNK-IEEENQRLIKKDKDSTQKLLA 2260
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRrAVTLAGRLREVTLEGEGGSAG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2261 EEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLL 2340
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2341 EDKQLMQQRLEEETEEYHKSLEVErkrqlEIMAEAERLRLQVSQLSeaqaraeeeakkfkkqadKVATRlheteiATQEK 2420
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLE-----ELERELERLEREIEALG------------------PVNLL------AIEEY 790
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1988774682 2421 MTVVERLEF--ERLNT-SKEADDLRKAIADLENEKARLKKEA 2459
Cdd:COG1196 791 EELEERYDFlsEQREDlEEARETLEEAIEEIDRETRERFLET 832
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1611-2607 |
3.83e-24 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 112.61 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1611 EAERLKKQQEDAENSREEAEKELEKWRQKANEALR------------LRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKR 1678
Cdd:NF041483 23 EMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRslasrpaydgadIGYQAEQLLRNAQIQADQLRADAERELRDARAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1679 AK------AEESALKQKEMAEEELERQRKIAESTAQQKLTAEQ---------ELIRLRADfdnaEQQRSLLEDELYRLKN 1743
Cdd:NF041483 103 TQrilqehAEHQARLQAELHTEAVQRRQQLDQELAERRQTVEShvnenvawaEQLRARTE----SQARRLLDESRAEAEQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1744 EVAAA--------QQQRKQLEDELAKVRSEMD-ILIQLKTKAEK----------ETMSNTEKSKQLLEAEAAKMKDLAEE 1804
Cdd:NF041483 179 ALAAAraeaerlaEEARQRLGSEAESARAEAEaILRRARKDAERllnaastqaqEATDHAEQLRSSTAAESDQARRQAAE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1805 ASR------------LRAISEEAKHQRQIAEEEAARQRAEAE-------RILKEKLA-----AISEATRLKTEAEIALKE 1860
Cdd:NF041483 259 LSRaaeqrmqeaeeaLREARAEAEKVVAEAKEAAAKQLASAEsaneqrtRTAKEEIArlvgeATKEAEALKAEAEQALAD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1861 KEAENERLRRQAEDEAyQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRilKLNFEKAS 1940
Cdd:NF041483 339 ARAEAEKLVAEAAEKA-RTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEAD--RLRGEAAD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1941 SGkldlelelNKLKNIA-DETQQSKIRA---EEEAEKLRKLAleeekrrreaeekvkkiaaaeeeaARQRKAALEELERL 2016
Cdd:NF041483 416 QA--------EQLKGAAkDDTKEYRAKTvelQEEARRLRGEA------------------------EQLRAEAVAEGERI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2017 RKKA-EEARKQKDEADKEAEKQIVVAQQAAQKC-SAAEQQVQSVLAQQIEDSITQKKLKEEyekakklakeaeaakekae 2094
Cdd:NF041483 464 RGEArREAVQQIEEAARTAEELLTKAKADADELrSTATAESERVRTEAIERATTLRRQAEE------------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2095 reaaLLRQQAEEAERQKTaaeeeaanqaKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQ-QADTEMAKHKKLAEQTLKq 2173
Cdd:NF041483 525 ----TLERTRAEAERLRA----------EAEEQAEEVRAAAERAARELREETERAIAARQaEAAEELTRLHTEAEERLT- 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2174 kfQVEQELTKVKlklDETDKQKSVLDEELQRLKDEVDDAVKQ-RGQVEEELFKVKVQMEE------------LLKLKNKI 2240
Cdd:NF041483 590 --AAEEALADAR---AEAERIRREAAEETERLRTEAAERIRTlQAQAEQEAERLRTEAAAdasaaraegenvAVRLRSEA 664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2241 EEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQ-EAARLRQIAEDDLNQQRALAEkmlKEKMQAIQEASRLK 2319
Cdd:NF041483 665 AAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQeEAARRRREAEETLGSARAEAD---QERERAREQSEELL 741
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2320 AEAemlQKQKDLAQEQAQKLLED------------KQLMQQ------RLEEETEEYHKSLE------VERKRQlEIMAEA 2375
Cdd:NF041483 742 ASA---RKRVEEAQAEAQRLVEEadrratelvsaaEQTAQQvrdsvaGLQEQAEEEIAGLRsaaehaAERTRT-EAQEEA 817
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2376 ERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAtqEKMTVVERLefeRLNTSKEADDLR----KAIADLENE 2451
Cdd:NF041483 818 DRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVS--EAIAEAERL---RSDASEYAQRVRteasDTLASAEQD 892
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2452 KARLKKEAEELQNKSKEMADAQQKKIEHEKTVlqqtfmtekemllkkekliEDEKKRLESQFEEEVKKAKALKDEQERQK 2531
Cdd:NF041483 893 AARTRADAREDANRIRSDAAAQADRLIGEATS-------------------EAERLTAEARAEAERLRDEARAEAERVRA 953
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2532 QQMEQEKKTLQATMDAALSKQKEAEEEMLRKQkemQELERQRLEQERILAE---ENQKLREKLQQ-----LEDAQKDQHT 2603
Cdd:NF041483 954 DAAAQAEQLIAEATGEAERLRAEAAETVGSAQ---QHAERIRTEAERVKAEaaaEAERLRTEAREeadrtLDEARKDANK 1030
|
....
gi 1988774682 2604 RETD 2607
Cdd:NF041483 1031 RRSE 1034
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
164-264 |
8.89e-24 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 98.69 E-value: 8.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 164 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPEDV 243
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1988774682 244 DVPHPDEKSIITYVSSLYDAM 264
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1520-2462 |
1.04e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 111.30 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1520 KRKSEAEK--EAAKQKQKALED-LEKLRMQAEEAERQVKQAEieKEKQIKVAHEAAQKS-AAAELQSKHmsfaEKTSKLE 1595
Cdd:TIGR02168 172 ERRKETERklERTRENLDRLEDiLNELERQLKSLERQAEKAE--RYKELKAELRELELAlLVLRLEELR----EELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1596 ESLKQehgavlqLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREA 1675
Cdd:TIGR02168 246 EELKE-------AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1676 KKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQL 1755
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1756 EDELAKVRSEMDiliQLKTKAEKETmsnTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAER 1835
Cdd:TIGR02168 399 NNEIERLEARLE---RLEDRRERLQ---QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1836 ILKEKLAAISEATRLKTEAEIAlkekeaenERLRRQAEDEAYQRKALEDQASQHKQEIEE--KIVQLKKSSEAEME---- 1909
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSL--------ERLQENLEGFSEGVKALLKNQSGLSGILGVlsELISVDEGYEAAIEaalg 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1910 -RQKAIVDDTLKQrrvVEEEIRILKlnfeKASSGKLDLeLELNKLKniADETQQSKIRAEEEAEKLRKLALEEEKRRREA 1988
Cdd:TIGR02168 545 gRLQAVVVENLNA---AKKAIAFLK----QNELGRVTF-LPLDSIK--GTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1989 EEKVKKIAAAEEEAARQRKAaleeLERLRKKAEEARKQKDEADKEAEKQIVVAqqaaqkcsAAEQQVQSVLAQQIEdsit 2068
Cdd:TIGR02168 615 RKALSYLLGGVLVVDDLDNA----LELAKKLRPGYRIVTLDGDLVRPGGVITG--------GSAKTNSSILERRRE---- 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2069 qkkLKEeyekakklakeaeaakekaereaalLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAA 2148
Cdd:TIGR02168 679 ---IEE-------------------------LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2149 ALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKV 2228
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2229 QMEELLKLKNKIEEENQRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSVEaqeaarlrqiaeddLNQQRALAEKM---- 2304
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESL-ERRIAATERRLEDLEEQIEELSEDIESLAAE--------------IEELEELIEELesel 875
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2305 ---LKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKsLEVERKRQLEIMAEAERLRLQ 2381
Cdd:TIGR02168 876 ealLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLE 954
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2382 -VSQLSEAQARAEEEAKKFKKQADKVATRLHETEI-ATQEKMTVVERLEFerlnTSKEADDLRKAIADLENEKARLKKEA 2459
Cdd:TIGR02168 955 eAEALENKIEDDEEEARRRLKRLENKIKELGPVNLaAIEEYEELKERYDF----LTAQKEDLTEAKETLEEAIEEIDREA 1030
|
...
gi 1988774682 2460 EEL 2462
Cdd:TIGR02168 1031 RER 1033
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
161-261 |
1.13e-23 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 98.27 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 240
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1988774682 241 EDV---DVphPDEKSIITYVSSLY 261
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
148-263 |
1.21e-23 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 98.99 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 148 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 227
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774682 228 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
45-148 |
1.94e-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: 97.74 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 45 VQKKTFTKWVNKHLIKAQRH--VTDLYEDLRDGHNLISLLEVLSGETLP-REKGRMRFHKLQNVQIALDFLRHRQ-VKLV 120
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1988774682 121 NIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1673-2546 |
2.96e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 109.76 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1673 REAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKltaeQELIRLRADFDNAEQQRSL-----LEDELYRLKNEVAA 1747
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKA----ERYKELKAELRELELALLVlrleeLREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1748 AQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtmsntekskqlLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAA 1827
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1828 RQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHkQEIEEKIVQLKKSSEAE 1907
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL-ETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1908 MERQKAIvDDTLKQ--RRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRR 1985
Cdd:TIGR02168 399 NNEIERL-EARLERleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1986 REAEEKVKKIaaaeeeaaRQRKAALEEL-ERLRKKAEEARKQKDEADKEAEKQIVVAQQ--AAQKCSAAeqqVQSVLAQQ 2062
Cdd:TIGR02168 478 DAAERELAQL--------QARLDSLERLqENLEGFSEGVKALLKNQSGLSGILGVLSELisVDEGYEAA---IEAALGGR 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2063 IEDSITQKKlkeeyekAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKR 2142
Cdd:TIGR02168 547 LQAVVVENL-------NAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2143 AQAEAAALMQKQQADTEMAKHKK-------LAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQ 2215
Cdd:TIGR02168 620 YLLGGVLVVDDLDNALELAKKLRpgyrivtLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKA 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2216 RGQVEEELfkvkVQMEELLKLKNKIEEENQRLIkkdkDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLN 2295
Cdd:TIGR02168 700 LAELRKEL----EELEEELEQLRKELEELSRQI----SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2296 QQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKL---LEDKQLMQQRLEEETEEYHKSLEVERKRQLEIM 2372
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2373 AEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEK 2452
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2453 ARLKKEAEELQnkskemadaqqKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFE----------EEVKKAKA 2522
Cdd:TIGR02168 932 EGLEVRIDNLQ-----------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaiEEYEELKE 1000
|
890 900
....*....|....*....|....
gi 1988774682 2523 LKDEQERQKQQMEQEKKTLQATMD 2546
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEAIE 1024
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1246-1840 |
2.97e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 109.64 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1246 LKEQLAQEKKLLEEIEQNKDKVDECQKyakayidTIKDYELQLVAYKAQVEplvsplkktKLDSASDNIIQEYVTLRTRY 1325
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEA-------ELAELEAELEELRLELE---------ELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1326 SELmtltSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSK 1405
Cdd:COG1196 298 ARL----EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1406 REiAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAA 1485
Cdd:COG1196 374 LA-EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1486 EA-EKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQ 1564
Cdd:COG1196 453 ELeEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1565 IKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKqehgavlqlQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAL 1644
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK---------AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1645 RLRLQAEDEAHKKTLAQEEAEKQKEEAERE-AKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRAD 1723
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLEaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1724 fdnAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAE 1803
Cdd:COG1196 684 ---LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1988774682 1804 EASRLRAISEEAKhqRQI---------AEEEAARQRAEAERILKEK 1840
Cdd:COG1196 761 DLEELERELERLE--REIealgpvnllAIEEYEELEERYDFLSEQR 804
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1768-2601 |
3.53e-23 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 109.68 E-value: 3.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1768 ILIQLKtKAEKETMSNTEKSKQLLEAEA-AKMKDLAEEASR--LRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAI 1844
Cdd:pfam02463 137 FLVQGG-KIEIIAMMKPERRLEIEEEAAgSRLKRKKKEALKklIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1845 SEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKalEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIvddtlkqrrv 1924
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE--EIESSKQEIEKEEEKLAQVLKENKEEEKEKKL---------- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1925 VEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAAR 2004
Cdd:pfam02463 284 QEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2005 QRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAA--EQQVQSVLAQQIEDSITQKKLKEEYEKAKKL 2082
Cdd:pfam02463 364 LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLleLARQLEDLLKEEKKEELEILEEEEESIELKQ 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2083 AKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAK 2162
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2163 HKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKvqmeeLLKLKNKIEE 2242
Cdd:pfam02463 524 IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLK-----LPLKSIAVLE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2243 ENQRLIKKDKDSTqKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEA 2322
Cdd:pfam02463 599 IDPILNLAQLDKA-TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2323 EMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERL--RLQVSQLSEAQARAEEEAKKFK 2400
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKinEELKLLKQKIDEEEEEEEKSRL 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2401 KQADKVATRLHETEiatQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHE 2480
Cdd:pfam02463 758 KKEEKEEEKSELSL---KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2481 KtvlqqtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKtLQATMDAALSKQKEAEEEML 2560
Cdd:pfam02463 835 L---------EELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKL-KDELESKEEKEKEEKKELEE 904
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1988774682 2561 RKQKEMQELERQRLEQERI--LAEENQKLREKLQQLEDAQKDQ 2601
Cdd:pfam02463 905 ESQKLNLLEEKENEIEERIkeEAEILLKYEEEPEELLLEEADE 947
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
161-265 |
4.64e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 96.78 E-value: 4.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQRMTDGYqGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 240
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1988774682 241 EDVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1459-2355 |
2.49e-22 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 106.59 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1459 IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRqaEEELKRKSEAEKEAAKQKQKALE 1538
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQ--ELKLKEQAKKALEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1539 DLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKsaaAELQSKHMSFAEKTSKLEESLKQEhgavlQLQQEAERLKKQ 1618
Cdd:pfam02463 222 EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSK---QEIEKEEEKLAQVLKENKEEEKEK-----KLQEEELKLLAK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1619 QEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELER 1698
Cdd:pfam02463 294 EEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1699 QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEK 1778
Cdd:pfam02463 374 ELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1779 ETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKhqRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIAL 1858
Cdd:pfam02463 454 EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS--RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1859 KEKEAENERLRRQ---AEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVE-EEIRILKL 1934
Cdd:pfam02463 532 GDLGVAVENYKVAistAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIlNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1935 NFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKiaAAEEEAARQRKAALEELE 2014
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL--TKELLEIQELQEKAESEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2015 RLRKKAEEARKQKDEADKEAEKQIVVAQQaAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAE 2094
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLE-AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2095 REAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQK 2174
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2175 FQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQrgQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDS 2254
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE--SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2255 TQKLLAEEAENMRKLAEDAArlSVEAQEAARLRQIAEDDLNQQrALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQE 2334
Cdd:pfam02463 927 AEILLKYEEEPEELLLEEAD--EKEKEENNKEEEEERNKRLLL-AKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
890 900
....*....|....*....|.
gi 1988774682 2335 QAQKLLEDKQLMQQRLEEETE 2355
Cdd:pfam02463 1004 KKKLIRAIIEETCQRLKEFLE 1024
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
44-149 |
1.17e-21 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 93.61 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 44 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1988774682 121 NIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
44-149 |
1.60e-21 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 93.23 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 44 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1988774682 121 NIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1226-1701 |
2.28e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.07 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1226 ADAKQRQEKIQAVPITDSKTLKE----QLAQEKKLLEEIE---QNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPL 1298
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEaaekKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1299 VSPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDD-EEKAAEKLKAEERKKMAE---MQAELDKQ 1374
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEaKKKAEEAKKADEAKKKAEeakKKADEAKK 1504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1375 KQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEE 1454
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1455 EIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSeetQKKRQAEEELKRKSEAEKEAAKQKQ 1534
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE---QLKKKEAEEKKKAEELKKAEEENKI 1661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1535 KAledlEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKsaaaelqskhmsfAEKTSKLEESLKQEHGAVlqlqQEAER 1614
Cdd:PTZ00121 1662 KA----AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-------------AEEAKKAEELKKKEAEEK----KKAEE 1720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1615 LKKQQEDAENSREEAEKELEKWRQKANEAlrlrlqAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEE 1694
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEA------KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
....*..
gi 1988774682 1695 ELERQRK 1701
Cdd:PTZ00121 1795 EVDKKIK 1801
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1124-1884 |
2.66e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 103.21 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1124 VKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRE 1203
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1204 LEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKD 1283
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1284 YELQLVAYKAQVEPLVSplKKTKLDSASDNIIQEYVTLRTRYSELMtltsqyikfITDTQRRLDDEEKAAEKLKAEErkk 1363
Cdd:TIGR02168 391 LELQIASLNNEIERLEA--RLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEEL--- 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1364 mAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLK------MQEEVSKREIAAVDAEKQKTNIQLELQELKNL------- 1430
Cdd:TIGR02168 457 -ERLEEALEELREELEEAEQALDAAERELAQLQARldslerLQENLEGFSEGVKALLKNQSGLSGILGVLSELisvdegy 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1431 -------------------SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLR 1491
Cdd:TIGR02168 536 eaaieaalggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1492 KLAQ------------DEAEKLRKQVSEE---------------------------TQKKRQAEEELKRKSEAEKEAAKQ 1532
Cdd:TIGR02168 616 KALSyllggvlvvddlDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELEEKIAE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1533 KQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIkvaheaaqksaaaelqskhmsfaektSKLEESLKQEHGAVLQLQQEA 1612
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQI--------------------------SALRKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1613 ERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAhkktlaqeEAEKQKEEAEREAKKRAKAEESALKQK--- 1689
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI--------EQLKEELKALREALDELRAELTLLNEEaan 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1690 -----EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRS 1764
Cdd:TIGR02168 822 lrerlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1765 EMDILIQLKTKAEKETMSNTEKSKQL-LEAEAAKMKdLAEEASRLRA----ISEEAKHQRQIAEEEAARQRAEAERiLKE 1839
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLeLRLEGLEVR-IDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKR-LEN 979
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1988774682 1840 KLAAISEATRLkteaeiALKEKEAENER---LRRQAEDEAYQRKALED 1884
Cdd:TIGR02168 980 KIKELGPVNLA------AIEEYEELKERydfLTAQKEDLTEAKETLEE 1021
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
795-861 |
3.04e-21 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 90.01 E-value: 3.04e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774682 795 QLKPRNptTSIKGKLPIQAVCDFKQQEITVHKGDECALLNNSQPFKWKVLNRSGHEAMVPSVCFIVP 861
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2004-2600 |
4.37e-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: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2004 RQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSvLAQQIEDsitqkkLKEEYEKAKKLA 2083
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE-LELELEE------AQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2084 KEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKH 2163
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2164 KKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEE 2243
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2244 NQRLIKKDKDSTQKLLAEEAEnmrklaEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAE 2323
Cdd:COG1196 458 EEALLELLAELLEEAALLEAA------LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2324 MLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQA 2403
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2404 DKVATRLHETEIATQEkmtVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTV 2483
Cdd:COG1196 612 DARYYVLGDTLLGRTL---VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2484 LQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLrkQ 2563
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL--E 766
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1988774682 2564 KEMQELERQR----------LEQERILAEENQKLREKLQQLEDAQKD 2600
Cdd:COG1196 767 RELERLEREIealgpvnllaIEEYEELEERYDFLSEQREDLEEARET 813
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
161-261 |
6.79e-21 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 90.48 E-value: 6.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 240
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1988774682 241 EDVDV--PHPDEKSIITYVSSLY 261
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1824-2546 |
7.15e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.94 E-value: 7.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1824 EEAA------RQRAEAERilkeKLAAISEatRLkTEAEIALKEKEAENERLRRQAEDeayQRKALEDQASQHKQEIEEKI 1897
Cdd:COG1196 162 EEAAgiskykERKEEAER----KLEATEE--NL-ERLEDILGELERQLEPLERQAEK---AERYRELKEELKELEAELLL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1898 VQLKKSsEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKl 1977
Cdd:COG1196 232 LKLREL-EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1978 aleeekrrreaeekvkkiaaaeeeaarQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQS 2057
Cdd:COG1196 310 ---------------------------RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2058 VLAQQIEDSITQKKLKEEyekakklakeaeaakekaereaaLLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEF 2137
Cdd:COG1196 363 AEEALLEAEAELAEAEEE-----------------------LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2138 EAAKRAQAEaaalmQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRg 2217
Cdd:COG1196 420 EEELEELEE-----ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL- 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2218 qveeelfkvkvqmEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRkLAEDAARLSVEAQEAARLRQIAEDDLNQQ 2297
Cdd:COG1196 494 -------------LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI-GVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2298 RALAEKMLKEKM--QAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEA 2375
Cdd:COG1196 560 AAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2376 ERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARL 2455
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2456 KKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLiEDEKKRLESQFE----------EEVKKAKALKD 2525
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL-ERELERLEREIEalgpvnllaiEEYEELEERYD 798
|
730 740
....*....|....*....|.
gi 1988774682 2526 EQERQKQQMEQEKKTLQATMD 2546
Cdd:COG1196 799 FLSEQREDLEEARETLEEAIE 819
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
162-261 |
9.95e-21 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 89.93 E-value: 9.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 162 AKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPE 241
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1988774682 242 D-VDVPHPDEKSIITYVSSLY 261
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
161-260 |
1.33e-20 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 89.46 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINmgkvYQQTNLENLE----QAFSVAEKdLGVTR 236
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVD----YESLDPLDIKennkKAFEAFAS-LGVPR 75
|
90 100
....*....|....*....|....*
gi 1988774682 237 LLDPED-VDVPHPDEKSIITYVSSL 260
Cdd:cd21255 76 LLEPADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
165-262 |
3.48e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 88.56 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 165 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD-PEDV 243
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1988774682 244 DVPHPDEKSIITYVSSLYD 262
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1339-2355 |
9.68e-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: 9.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1339 ITDTQRRLDDEEKAAEKLKAE---------------------------ERKKMAEMQAELDKQKQLAEAHAKAIAKAEKE 1391
Cdd:pfam01576 105 IQDLEEQLDEEEAARQKLQLEkvtteakikkleedillledqnsklskERKLLEERISEFTSNLAEEEEKAKSLSKLKNK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1392 AQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKnlseQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKY 1471
Cdd:pfam01576 185 HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ----EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1472 TAESELKQLRDRAAEAEK---LRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKlrmqAE 1548
Cdd:pfam01576 261 NALKKIRELEAQISELQEdleSERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKK----AL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1549 EAERQVKQAEIEKEKQikvaheaAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREE 1628
Cdd:pfam01576 337 EEETRSHEAQLQEMRQ-------KHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1629 AEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQrkiaestAQ 1708
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE-------TR 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1709 QKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtmsnTEKSK 1788
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE----LEALT 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1789 QLLEAEAAKMKDLAEEASRLRA----ISEEAKHQRQIAEEEAARQRaEAERILKEKLAAISEATRLKTEAEIALKEKEAE 1864
Cdd:pfam01576 559 QQLEEKAAAYDKLEKTKNRLQQelddLLVDLDHQRQLVSNLEKKQK-KFDQMLAEEKAISARYAEERDRAEAEAREKETR 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1865 NERLRRQAEDEAYQRKALEDQASQHKQEIEEkIVQLKKS---SEAEMERQKAIVDDTLKQRRVVEEEiriLKLNFEKASS 1941
Cdd:pfam01576 638 ALSLARALEEALEAKEELERTNKQLRAEMED-LVSSKDDvgkNVHELERSKRALEQQVEEMKTQLEE---LEDELQATED 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1942 GKLDLELELNKLKNIADETQQSkiRAEEEAEKLRKLAleeekrrreaeEKVKKIAAAEEEAARQRKAALE-------ELE 2014
Cdd:pfam01576 714 AKLRLEVNMQALKAQFERDLQA--RDEQGEEKRRQLV-----------KQVRELEAELEDERKQRAQAVAakkklelDLK 780
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2015 RLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEdsiTQKKLKeeyekakklakeaeaakekae 2094
Cdd:pfam01576 781 ELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKE---SEKKLK--------------------- 836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2095 reaallrqqAEEAErqktaaeeeaanQAKAQED---AERLRKEAEFEaakraqaeaaalmqKQQADTEMAKHKKLAEQTL 2171
Cdd:pfam01576 837 ---------NLEAE------------LLQLQEDlaaSERARRQAQQE--------------RDELADEIASGASGKSALQ 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2172 KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKV---KVQMEELLK-LKNKIEEENQRL 2247
Cdd:pfam01576 882 DEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSesaRQQLERQNKeLKAKLQEMEGTV 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2248 IKKDKDSTQKLLAeeaenmrKLAEDAARLSVEAQE---AARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEM 2324
Cdd:pfam01576 962 KSKFKSSIAALEA-------KIAQLEEQLEQESRErqaANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQ 1034
|
1050 1060 1070
....*....|....*....|....*....|.
gi 1988774682 2325 LQKQKDLAQEQAQKLLEDKQLMQQRLEEETE 2355
Cdd:pfam01576 1035 LKRQLEEAEEEASRANAARRKLQRELDDATE 1065
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
46-146 |
2.27e-19 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 86.10 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 46 QKKTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLRHRQVKLVN 121
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1988774682 122 IRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1349-1970 |
3.30e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 96.68 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1349 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVS------KREIAAVDAEKQKT--NI 1420
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrvKEKIGELEAEIASLerSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1421 QLELQELKNLSEQQIKDKSQqVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 1500
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAE-IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1501 LRKQVSEETQKKRQAEEELKRKSE-------------AEKEAAKQKQKALED-LEKLRMQAEEAERQVKQ--AEIEKEKQ 1564
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEelqrlseeladlnAAIAGIEAKINELEEeKEDKALEIKKQEWKLEQlaADLSKYEQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1565 IKVA------------HEAAQKSAAAELQSKHMSFAEKTSK-----LEESLKQEHGAVLQLQQEAERLKKQQEDAENSR- 1626
Cdd:TIGR02169 470 ELYDlkeeydrvekelSKLQRELAEAEAQARASEERVRGGRaveevLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRl 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1627 --------EEAEKELEKWRQ-KANEA--LRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKA-------------E 1682
Cdd:TIGR02169 550 nnvvveddAVAKEAIELLKRrKAGRAtfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlvvedI 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1683 ESALKQK------EMAEEELERQRKI------AESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1750
Cdd:TIGR02169 630 EAARRLMgkyrmvTLEGELFEKSGAMtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQ 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1751 QRKQLEDELAKVRSEMDILIQLKTKAE---KETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAisEEAKHQRQIAEEEAA 1827
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKerlEELEEDLSSLEQEIENVKSELKELEARIEELEE--DLHKLEEALNDLEAR 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1828 RQRAEAERI------LKEKLAAISEATRlktEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLK 1901
Cdd:TIGR02169 788 LSHSRIPEIqaelskLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774682 1902 KsSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEE 1970
Cdd:TIGR02169 865 E-LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
164-260 |
6.27e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 84.67 E-value: 6.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 164 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN----LENLEQAFSVAEKDLGVTRLLD 239
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1988774682 240 PEDVDVPHPDEKSIITYVSSL 260
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 ... |
1351-2591 |
1.27e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 94.47 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1351 KAAEKLKAEERKKMAEMQ-AELD-KQKQLAE----------AHAKAIAKAEKEAQELKLKMQ--EEVSKREIAAVDAEKQ 1416
Cdd:pfam01576 10 KEEELQKVKERQQKAESElKELEkKHQQLCEeknalqeqlqAETELCAEAEEMRARLAARKQelEEILHELESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1417 KTNiqlELQELKNLSEQQIKDKSQQVDEALHSRTK--------------IEEEIRLIRIQLETTEKQKYTAESELKQLRD 1482
Cdd:pfam01576 90 RSQ---QLQNEKKKMQQHIQDLEEQLDEEEAARQKlqlekvtteakikkLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1483 RAAEAEKLRKLAQDEAEKLRKQVSE------ETQKKRQAEEELKRKSEAEKEAAKqkqkalEDLEKLRMQAEEAERQVKQ 1556
Cdd:pfam01576 167 NLAEEEEKAKSLSKLKNKHEAMISDleerlkKEEKGRQELEKAKRKLEGESTDLQ------EQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1557 AEIE-KEKQIKVAHEAAQKSAAaelQSKHMSFAEKTSKLEESLKQEHGAvlqlQQEAERLKKQ-QEDAENSREEAEKELE 1634
Cdd:pfam01576 241 KEEElQAALARLEEETAQKNNA---LKKIRELEAQISELQEDLESERAA----RNKAEKQRRDlGEELEALKTELEDTLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1635 KwrQKANEALRLRLQAEDEAHKKTLAqeeaekqkeeaerEAKKRAKAEESALKQK-----EMAEEELERQRKIAESTAQQ 1709
Cdd:pfam01576 314 T--TAAQQELRSKREQEVTELKKALE-------------EETRSHEAQLQEMRQKhtqalEELTEQLEQAKRNKANLEKA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1710 KLTAEQELIRLRADF-------DNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMS 1782
Cdd:pfam01576 379 KQALESENAELQAELrtlqqakQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1783 NTEKSKQLLEAEAAKMKDLAEE-------ASRLRAISEE-AKHQRQIAEEEAARQRAEaerilkeklaaiseatRLKTEA 1854
Cdd:pfam01576 459 LSKDVSSLESQLQDTQELLQEEtrqklnlSTRLRQLEDErNSLQEQLEEEEEAKRNVE----------------RQLSTL 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1855 EIALKEkeaenerLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEA--EMERQKAIVDDTLKQRRVVEEEIRIL 1932
Cdd:pfam01576 523 QAQLSD-------MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAydKLEKTKNRLQQELDDLLVDLDHQRQL 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1933 KLNFEKASSgKLDLELElnKLKNIADETQQSKIRAEEEAEKLRKLALEEEKrrreaeekvkkiaaaeeeaarqrkaALEE 2012
Cdd:pfam01576 596 VSNLEKKQK-KFDQMLA--EEKAISARYAEERDRAEAEAREKETRALSLAR-------------------------ALEE 647
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2013 LERLRKKAEEARKQKdEADKEaekQIVVAQQAAQKCSAAEQQVQSVLAQQIEDsitqkklkeeyekakklakeaeaakek 2092
Cdd:pfam01576 648 ALEAKEELERTNKQL-RAEME---DLVSSKDDVGKNVHELERSKRALEQQVEE--------------------------- 696
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2093 aereaalLRQQAEEAERQKTAAeeeaanqakaqEDAeRLRKEAEFEAAKRAQAeaaalmQKQQADTEMAKHKKlaEQTLK 2172
Cdd:pfam01576 697 -------MKTQLEELEDELQAT-----------EDA-KLRLEVNMQALKAQFE------RDLQARDEQGEEKR--RQLVK 749
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2173 QKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELlklknkieeenQRLIKKDK 2252
Cdd:pfam01576 750 QVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL-----------QRELEEAR 818
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2253 DSTQKLLAEEAENMRKLAedaarlSVEAQeaarLRQIAEDDLNQQRAlaekmlkeKMQAIQEASRLKAEAEMLQKQKDLA 2332
Cdd:pfam01576 819 ASRDEILAQSKESEKKLK------NLEAE----LLQLQEDLAASERA--------RRQAQQERDELADEIASGASGKSAL 880
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2333 QEQAQKLleDKQLMQqrLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHE 2412
Cdd:pfam01576 881 QDEKRRL--EARIAQ--LEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQE 956
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2413 TEIATQEKmtvverleferlntskeaddLRKAIADLEnekARLKKEAEELQNKSKEMADAQQKKIEHEKTVlqqtfmteK 2492
Cdd:pfam01576 957 MEGTVKSK--------------------FKSSIAALE---AKIAQLEEQLEQESRERQAANKLVRRTEKKL--------K 1005
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2493 EMLLkkekliedekkrlesQFEEEVKKAKALKDEQERQKQQMEQEKKTLQatmdaalskqkEAEEEMLRKQKEMQELERQ 2572
Cdd:pfam01576 1006 EVLL---------------QVEDERRHADQYKDQAEKGNSRMKQLKRQLE-----------EAEEEASRANAARRKLQRE 1059
|
1290 1300
....*....|....*....|..
gi 1988774682 2573 ---RLEQERILAEENQKLREKL 2591
Cdd:pfam01576 1060 lddATESNESMNREVSTLKSKL 1081
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1340-2036 |
1.95e-18 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 93.88 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1340 TDTQRRLDDEEKAAEK-LKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEvsKREIAAVDAEKQKT 1418
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKsLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT--QQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1419 NIQLELQELknLSEQQIKDKSQQVDEALHSRTKIEEEIR-------LIRIQLETTEKQKYTAESELK-QLRDRAAEAEKL 1490
Cdd:TIGR00618 253 EEQLKKQQL--LKQLRARIEELRAQEAVLEETQERINRArkaaplaAHIKAVTQIEQQAQRIHTELQsKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1491 RKLAQDEAEKLRKQVSEETQkkRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHE 1570
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTL--HSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1571 AAQksAAAELQskhmsfaektsklEESLKQEHGAVLQLQQEAerlkkQQEDAENSREEAEKELEKWRQKANEALRLRLQA 1650
Cdd:TIGR00618 409 QAT--IDTRTS-------------AFRDLQGQLAHAKKQQEL-----QQRYAELCAAAITCTAQCEKLEKIHLQESAQSL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1651 EDEAHK-KTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRK-IAESTAQQKLTAEQELIRLRADFDNAE 1728
Cdd:TIGR00618 469 KEREQQlQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1729 QQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRL 1808
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1809 RAISEEAKHQRQIAEEEAARQRAE---AERILKEKLAAISEATRLKTEA-EIALKEKEAENERLRRQAEDEAYQRKALED 1884
Cdd:TIGR00618 629 DVRLHLQQCSQELALKLTALHALQltlTQERVREHALSIRVLPKELLASrQLALQKMQSEKEQLTYWKEMLAQCQTLLRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1885 Q------ASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvveEEIRILKLNFEKASSGKLDLELELNKLKNIAD 1958
Cdd:TIGR00618 709 LethieeYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR---TVLKARTEAHFNNNEEVTAALQTGAELSHLAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1959 ETqQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQ--------RKAALEELERLRKKAEEARKQKDEA 2030
Cdd:TIGR00618 786 EI-QFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEqflsrleeKSATLGEITHQLLKYEECSKQLAQL 864
|
....*.
gi 1988774682 2031 DKEAEK 2036
Cdd:TIGR00618 865 TQEQAK 870
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1683-2596 |
2.26e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 93.59 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1683 ESALKQKEMAEEELERQRKIAESTAQQkltaeqeLIRLRADFDNAEQQRSLL----EDELYRLKNEVAAAQQQRKQLEDE 1758
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQ-------LERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1759 LAKVRSEMDILIQLKTKAEKETmsntEKSKQLLEAEAAKMKDLAEEasrlraisEEAKHQRQIAEEEAarQRAEAERILK 1838
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRL----EEIEQLLEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1839 EKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHK-------QEIEEKIVQLKKSSEAEMERQ 1911
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeledlrAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1912 KAIvDDTLKQRRVVEEEIRILKLNFEKASSGKLDLElelNKLKNIADETQQSKIRAEEEAEKLRKLaleeekrrreaEEK 1991
Cdd:TIGR02169 392 EKL-EKLKREINELKRELDRLQEELQRLSEELADLN---AAIAGIEAKINELEEEKEDKALEIKKQ-----------EWK 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1992 VKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEAdkEAEKQIVvaqQAAQKCSAAEQQVQSVLAQQIEDSITQ-K 2070
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA--EAQARAS---EERVRGGRAVEEVLKASIQGVHGTVAQlG 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2071 KLKEEYEKAKKLAKEAeaakekaereaallRQQAEEAErqktaaeeeaanqakAQEDAERLrkeaefeaakraqaeaaal 2150
Cdd:TIGR02169 532 SVGERYATAIEVAAGN--------------RLNNVVVE---------------DDAVAKEA------------------- 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2151 mqkqqadTEMAKHKKLAEQTLkqkfqveqeLTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKV-- 2228
Cdd:TIGR02169 564 -------IELLKRRKAGRATF---------LPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVve 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2229 QMEELLKLKNKIeeenqRLIKKDKDSTQK--LLAEEAENMRKLAEDAARLSVEAQE-AARLR--QIAEDDLNQQRALAEK 2303
Cdd:TIGR02169 628 DIEAARRLMGKY-----RMVTLEGELFEKsgAMTGGSRAPRGGILFSRSEPAELQRlRERLEglKRELSSLQSELRRIEN 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2304 MLKEKMQAIQEASR----LKAEAEMLQKQkdlaQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLR 2379
Cdd:TIGR02169 703 RLDELSQELSDASRkigeIEKEIEQLEQE----EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2380 LQVSQLseAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEA 2459
Cdd:TIGR02169 779 EALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2460 EELQNKSKEMaDAQQKKIEhektvlqqtfmtekemllKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 2539
Cdd:TIGR02169 857 ENLNGKKEEL-EEELEELE------------------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774682 2540 tLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERIlAEENQKLREKLQQLED 2596
Cdd:TIGR02169 918 -RLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV-QAELQRVEEEIRALEP 972
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1107-1854 |
3.17e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 93.21 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1107 LKQYEDCLREVHTVPSDVKEVETYRAKLKKMRTEAEDE----QPVFDSLEEELKKAS-----AVSDKMVRVHSER---DV 1174
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRleeiEQLLEELNKKIKDLGeeeqlRVKEKIGELEAEIaslER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1175 ELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQAVPITDSKTLKEQLAQEK 1254
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1255 KLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSplKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQ 1334
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA--KINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1335 YIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQK------------------------QLAEAHAKAIAKAEK 1390
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggraveevlkasiqgvhgtvaqlgSVGERYATAIEVAAG 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1391 EAQELKLKMQEEVSKREIAAVDAEKQK-------TNIQLELQELKNLSEQQIKD--------------------KSQQVD 1443
Cdd:TIGR02169 547 NRLNNVVVEDDAVAKEAIELLKRRKAGratflplNKMRDERRDLSILSEDGVIGfavdlvefdpkyepafkyvfGDTLVV 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1444 EALHSRTKIEEEIRLIRIQLETTEKQ----------------KYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSE 1507
Cdd:TIGR02169 627 EDIEAARRLMGKYRMVTLEGELFEKSgamtggsraprggilfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1508 ETQKKRQAEEELKRKSeaekeaaKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEkqikvAHEAAQKSAAAELQSKHmsf 1587
Cdd:TIGR02169 707 LSQELSDASRKIGEIE-------KEIEQLEQEEEKLKERLEELEEDLSSLEQEIE-----NVKSELKELEARIEELE--- 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1588 aEKTSKLEESL-----KQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELekwrqkaNEALRLRLQAEDEAHKKtlaqe 1662
Cdd:TIGR02169 772 -EDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL-------NRLTLEKEYLEKEIQEL----- 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1663 eAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAEstaqqkltAEQELIRLRADFDNAEQQRSLLEDELYRLK 1742
Cdd:TIGR02169 839 -QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD--------LESRLGDLKKERDELEAQLRELERKIEELE 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1743 NEVAAAQQQRKQLEDELAKVRSEMDILIQLKtKAEKETMSNT---EKSKQLLEAEAAKMKDLaeEASRLRAISEEAKHQR 1819
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEElslEDVQAELQRVEEEIRAL--EPVNMLAIQEYEEVLK 986
|
810 820 830
....*....|....*....|....*....|....*
gi 1988774682 1820 QIAEEEAARQRAEAERilKEKLAAISEATRLKTEA 1854
Cdd:TIGR02169 987 RLDELKEKRAKLEEER--KAILERIEEYEKKKREV 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1244-1815 |
4.86e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.43 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1244 KTLKEQLAQEKKLLEEIEQNKDKVDECQKYakayIDTIKDYELQLVAYKAQVEPLVSPLKKTKLDSASDNIIQEYVTLRT 1323
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLRE----INEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1324 R-YSELMTLTSQYIKFITDTQRRLDDEEKAAEKLK--AEERKKMAEMQAELDKQKQLAEahaKAIAKAEKEAQELKLKMq 1400
Cdd:PRK03918 255 RkLEEKIRELEERIEELKKEIEELEEKVKELKELKekAEEYIKLSEFYEEYLDELREIE---KRLSRLEEEINGIEERI- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1401 EEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQL 1480
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1481 RDRAAEAEKLRKLAQDEAEKLRK----------QVSEETQKKRQAE--EELKRKSEAEKEAAKQKQKALEDLEKLRMQAE 1548
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKELLEEytAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1549 EAERQVKQAEIEKekQIKVAHEAAQKSAAAELQSKhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLK----------KQ 1618
Cdd:PRK03918 491 KESELIKLKELAE--QLKELEEKLKKYNLEELEKK----AEEYEKLKEKLIKLKGEIKSLKKELEKLEelkkklaeleKK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1619 QEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEeaeREAKKRAKAEESAlkqkEMAEEELER 1698
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELE---REEKELKKLEEEL----DKAFEELAE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1699 QRKIAEStaqqkltAEQELIRLRADFDNAEQQRslLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDiliqlKTKAEK 1778
Cdd:PRK03918 638 TEKRLEE-------LRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLE-----KLKEEL 703
|
570 580 590
....*....|....*....|....*....|....*..
gi 1988774682 1779 ETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEA 1815
Cdd:PRK03918 704 EEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
161-260 |
5.16e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 82.21 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 240
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1988774682 241 ED-VDVPHPDEKSIITYVSSL 260
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1321-2251 |
5.72e-18 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 92.42 E-value: 5.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1321 LRTRYSELMTLTS-----QYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL 1395
Cdd:TIGR00606 171 LKQKFDEIFSATRyikalETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1396 KLKMQE-EVSKREIAAVDAE-KQKTNIQLELQELKNLSEQQIKDKSQQVDEAL------HSRTKIEEEIRLIRIQLETTE 1467
Cdd:TIGR00606 251 KNRLKEiEHNLSKIMKLDNEiKALKSRKKQMEKDNSELELKMEKVFQGTDEQLndlyhnHQRTVREKERELVDCQRELEK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1468 KQKytaeselkqlrdraaeaeKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEdleklrmQA 1547
Cdd:TIGR00606 331 LNK------------------ERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFE-------RG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1548 EEAERQVKQA-EIEKEKQIKVAHEAAQKsaAAELQSKHMSFAEKTSKLEESLKqehGAVLQLQQEAERLKKQQEDAENSR 1626
Cdd:TIGR00606 386 PFSERQIKNFhTLVIERQEDEAKTAAQL--CADLQSKERLKQEQADEIRDEKK---GLGRTIELKKEILEKKQEELKFVI 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1627 EEAE------KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEmaeeelERQR 1700
Cdd:TIGR00606 461 KELQqlegssDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH------TTTR 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1701 KIAESTAQQKLTAEQ-----------ELIRLRADFDNAEQqrslLEDELYRLKNEVaaaqqqrKQLEDELAKVRSEMDIL 1769
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEqirkiksrhsdELTSLLGYFPNKKQ----LEDWLHSKSKEI-------NQTRDRLAKLNKELASL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1770 IQLKTKAEKETMSNTEKSKQLLEA--EAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEA 1847
Cdd:TIGR00606 604 EQNKNHINNELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVC 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1848 TR-LKTEAEIALKEKEAENerLRRQAEDEayqRKALEDQASQHKQEIEEKIVqLKKSSEAEMERQKAIVDDTLKQRRVVE 1926
Cdd:TIGR00606 684 QRvFQTEAELQEFISDLQS--KLRLAPDK---LKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPELRNKLQKVN 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1927 EEIRILKLNFEKASS--GKLDLELELNK--------LKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVK--- 1993
Cdd:TIGR00606 758 RDIQRLKNDIEEQETllGTIMPEEESAKvcltdvtiMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKqhe 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1994 --KIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKK 2071
Cdd:TIGR00606 838 ldTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETF 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2072 LKEEYEKAKKLAKEAEAAKEKAEREAALLRqqaeeaERQKTAAEEEAANQAKAQEDAERlrkeaefeaakraqaeaaalm 2151
Cdd:TIGR00606 918 LEKDQQEKEELISSKETSNKKAQDKVNDIK------EKVKNIHGYMKDIENKIQDGKDD--------------------- 970
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2152 QKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEvdDAVKqrgQVEEELFKVKVQME 2231
Cdd:TIGR00606 971 YLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRE--NELK---EVEEELKQHLKEMG 1045
|
970 980
....*....|....*....|....
gi 1988774682 2232 ELLKLKNKIE----EENQRLIKKD 2251
Cdd:TIGR00606 1046 QMQVLQMKQEhqklEENIDLIKRN 1069
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1454-2212 |
5.95e-18 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 92.34 E-value: 5.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1454 EEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEaAKQK 1533
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ-TQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1534 QKALEDLEKLRMQAEEAERQVKQ--AEIEKEKQIKVAHEAAQKsaAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQ-Q 1610
Cdd:TIGR00618 242 HAYLTQKREAQEEQLKKQQLLKQlrARIEELRAQEAVLEETQE--RINRARKAAPLAAHIKAVTQIEQQAQRIHTELQsK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1611 EAERLKKQQEDAENSREEAekELEKWRQKANEALRLRLQAEDEAHKKTLaqeeaekqkeeaEREAKKRAKAEESALKQKE 1690
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQS--SIEEQRRLLQTLHSQEIHIRDAHEVATS------------IREISCQQHTLTQHIHTLQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1691 MAEEELERQRKIAeSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILI 1770
Cdd:TIGR00618 386 QQKTTLTQKLQSL-CKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1771 QLKTKAEKETMSNTEkskQLLEAEAAKMKdlaeeasrlraisEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEA-TR 1849
Cdd:TIGR00618 465 AQSLKEREQQLQTKE---QIHLQETRKKA-------------VVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPlTR 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1850 LKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEiEEKIVQLKKSSEAEMERQKAIVDDTLKQrrvVEEEI 1929
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQDL---TEKLS 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1930 RILKLNFEKASSGKLDLELELNKLKNIADETQQSKiraEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAA 2009
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ---ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLA 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2010 LEELERLRKKA---EEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIED-SITQKKLKEEYEKAKKLAKE 2085
Cdd:TIGR00618 682 LQKMQSEKEQLtywKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAlNQSLKELMHQARTVLKARTE 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2086 AEAAKEKAEREAALLRQQAEEAERQktaaeeEAANQAKAQEDAERLR-KEAEFEAAKRAQAEAAALMQKQQADTEMAKHK 2164
Cdd:TIGR00618 762 AHFNNNEEVTAALQTGAELSHLAAE------IQFFNRLREEDTHLLKtLEAEIGQEIPSDEDILNLQCETLVQEEEQFLS 835
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1988774682 2165 KLAEQTLKQkfqveQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDA 2212
Cdd:TIGR00618 836 RLEEKSATL-----GEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
161-259 |
6.45e-18 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 81.90 E-value: 6.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQRMTDGYqgiRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLD 239
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENpLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1988774682 240 PEDVDVPHPDEKSIITYVSS 259
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1548-2605 |
6.67e-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: 92.16 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1548 EEAERQVKQAEIEKEKQIKVAHEAAQKsaaaELQSKHMSFAEKTSKLEESLKQEHgavlQLQQEAERLKKQQEDAENSRE 1627
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELK----ELEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMRARLAARKQELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1628 EAEKELEKwrqkanealrlRLQAEDEAHKKTLAQeeaekqkeeaereaKKRAKAEESALKQkEMAEEELERQR-KIAEST 1706
Cdd:pfam01576 75 EILHELES-----------RLEEEEERSQQLQNE--------------KKKMQQHIQDLEE-QLDEEEAARQKlQLEKVT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1707 AQQKLTAEQELIRLRADFDNAEQ-QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILiQLKTKAEKETMSNTE 1785
Cdd:pfam01576 129 TEAKIKKLEEDILLLEDQNSKLSkERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDL-EERLKKEEKGRQELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1786 KSKQLLEAEAAkmkDLAEEASRLRAISEEAKHQRQIAEEE----------AARQRAEAERILKEKLAAISEATR------ 1849
Cdd:pfam01576 208 KAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEElqaalarleeETAQKNNALKKIRELEAQISELQEdleser 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1850 -LKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEkivqLKKSSEAEMERQKAIVDD-TLKQRRVVE- 1926
Cdd:pfam01576 285 aARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTE----LKKALEEETRSHEAQLQEmRQKHTQALEe 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1927 -----EEIRILKLNFEKAssgKLDLELELNKLKNIADETQQSKIRAEEEAEKLrklaleeekrrreaEEKVKKIAAAEEE 2001
Cdd:pfam01576 361 lteqlEQAKRNKANLEKA---KQALESENAELQAELRTLQQAKQDSEHKRKKL--------------EGQLQELQARLSE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2002 AARQRKAALEELERLRKKAEEARKQKDEADKEAEKqivvaqqAAQKCSAAEQQVQSvlAQQIEDSITQKKLKeeyekakk 2081
Cdd:pfam01576 424 SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK-------LSKDVSSLESQLQD--TQELLQEETRQKLN-------- 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2082 lakEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfeAAKRAQAEAAALMQKQQADTEMA 2161
Cdd:pfam01576 487 ---LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAG--TLEALEEGKKRLQRELEALTQQL 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2162 KHKKLAEQTL-KQKFQVEQELTKVKLKLDET--------DKQK---SVLDEE---LQRLKDEVDDAVKQRGQVEEELFKV 2226
Cdd:pfam01576 562 EEKAAAYDKLeKTKNRLQQELDDLLVDLDHQrqlvsnleKKQKkfdQMLAEEkaiSARYAEERDRAEAEAREKETRALSL 641
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2227 KVQMEELLKLKNKIEEENQRL------IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDdlnqqral 2300
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLraemedLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATED-------- 713
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2301 AEKMLKEKMQAiqeasrLKAEAEM-LQKQKDLAQEQAQKLLedKQLMQQRLEEETEEYHKSLEVERKRQLEImaEAERLR 2379
Cdd:pfam01576 714 AKLRLEVNMQA------LKAQFERdLQARDEQGEEKRRQLV--KQVRELEAELEDERKQRAQAVAAKKKLEL--DLKELE 783
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2380 LQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKmtvverleferLNTSKEADdlrKAIADLENEKARLKkea 2459
Cdd:pfam01576 784 AQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI-----------LAQSKESE---KKLKNLEAELLQLQ--- 846
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2460 EELQNKSKEMADAQQKKIEHEKTVLQQTfmTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 2539
Cdd:pfam01576 847 EDLAASERARRQAQQERDELADEIASGA--SGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTT 924
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 2540 TLQATMDAAlSKQKEAEEEMLRKQKE----MQELERQ-RLEQERILAeenqKLREKLQQLEDaQKDQHTRE 2605
Cdd:pfam01576 925 ELAAERSTS-QKSESARQQLERQNKElkakLQEMEGTvKSKFKSSIA----ALEAKIAQLEE-QLEQESRE 989
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
163-273 |
1.22e-17 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 81.58 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 163 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 242
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|..
gi 1988774682 243 -VDVPHPDEKSIITYVSSLYdampRTDVHDGM 273
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY----RCLVQKGL 110
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
157-262 |
1.34e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 81.15 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 157 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTR 236
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1988774682 237 LLDPEDV-DVPHPDEKSIITYVSSLYD 262
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2261-2598 |
1.61e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.77 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2261 EEAEnmRKLAEDAARLsveaqeaARLRQIAE------DDLNQQRALAEKMlkekmQAIQEASRLKaEAEMLQKQKDLAQE 2334
Cdd:COG1196 175 EEAE--RKLEATEENL-------ERLEDILGelerqlEPLERQAEKAERY-----RELKEELKEL-EAELLLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2335 QAQKLLEDKQLMQQRLEEETEEY---HKSLEVERKRQLEIMAEAERLRLQVSQLSEAQAraeeeakkfkkQADKVATRLH 2411
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELaelEAELEELRLELEELELELEEAQAEEYELLAELA-----------RLEQDIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2412 ETEIATQEKMtvvERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEKTVLQQTFMTE 2491
Cdd:COG1196 309 ERRRELEERL---EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE-AEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2492 KEMLLKKEKLIEDEKKRLESQfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELER 2571
Cdd:COG1196 385 AEELLEALRAAAELAAQLEEL-EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340
....*....|....*....|....*..
gi 1988774682 2572 QRLEQERILAEENQKLREKLQQLEDAQ 2598
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAA 490
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
47-144 |
2.37e-17 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 80.46 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 47 KKTFTKWVNKHL-IKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLRHRQV-KLVNI 122
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1988774682 123 RNDDI-ADGNPKLTLGLIWTIIL 144
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
163-262 |
4.64e-17 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 79.62 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 163 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 242
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1988774682 243 VDV--PHPDEKSIITYVSSLYD 262
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2264-2575 |
6.05e-17 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 88.64 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2264 ENMRKLAEDAARLSVEAQEAARLRQIAED---DLNQQRALAEKMlKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLL 2340
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEkarEVERRRKLEEAE-KARQAEMDRQAAIYAEQERMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2341 EDKQLMQQRLEEETEEYHKSLEVERkRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEK 2420
Cdd:pfam17380 358 RKRELERIRQEEIAMEISRMRELER-LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2421 MtvvERLEFERlntSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKtvlQQTFMTEKEMLLKKEK 2500
Cdd:pfam17380 437 V---RRLEEER---AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE---QRRKILEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2501 LIEDEKKR--LESQFEEEVK----KAKALKDEQERQKQQMEQEKKTLQATMDAALSKQK-----EAEEEMLRKQKEmQEL 2569
Cdd:pfam17380 508 MIEEERKRklLEKEMEERQKaiyeEERRREAEEERRKQQEMEERRRIQEQMRKATEERSrleamEREREMMRQIVE-SEK 586
|
....*.
gi 1988774682 2570 ERQRLE 2575
Cdd:pfam17380 587 ARAEYE 592
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
163-269 |
7.77e-17 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 79.32 E-value: 7.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 163 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 242
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*....
gi 1988774682 243 VDV--PHPDEKSIITYVSSLYDAMPRTDV 269
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRRHEM 111
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1408-2224 |
9.33e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.59 E-value: 9.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1408 IAAVDAEKQKTNIQLELQElKNLSEQQ--IKDKSQQVDEALHSRTKIEE--EIRLIRIQLETTE--KQKYTAESELKQLR 1481
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVE-ENIERLDliIDEKRQQLERLRREREKAERyqALLKEKREYEGYEllKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1482 DRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALE-DLEKLRMQAEEAERQVKQAEiE 1560
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELEDAE-E 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1561 KEKQIKVAHEAaQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKA 1640
Cdd:TIGR02169 323 RLAKLEAEIDK-LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1641 NEALRLRLQAEDEAHKKTlaqeeaekQKEEAEREAKKRAKAEESALK-QKEMAEEELERQRKIAESTAQQKLTAEQELIR 1719
Cdd:TIGR02169 402 NELKRELDRLQEELQRLS--------EELADLNAAIAGIEAKINELEeEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1720 LRADFDNAEQQRSLLEDELYRLKNEVAAAQQ-------QRKQLEDELAKVRSEMDILIQLKTKAEK-------------- 1778
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEErvrggraVEEVLKASIQGVHGTVAQLGSVGERYATaievaagnrlnnvv 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1779 -ETMSNTEKSKQLLEAEAA---------KMKDLAEEASRLRA----------ISEEAKHQRQIA----------EEEAAR 1828
Cdd:TIGR02169 554 vEDDAVAKEAIELLKRRKAgratflplnKMRDERRDLSILSEdgvigfavdlVEFDPKYEPAFKyvfgdtlvveDIEAAR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1829 QRAEAERI------LKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKK 1902
Cdd:TIGR02169 634 RLMGKYRMvtlegeLFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1903 SSEAEMERQKAIvDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKL-RKLALEE 1981
Cdd:TIGR02169 714 ASRKIGEIEKEI-EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1982 EKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQ 2061
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2062 qiedsiTQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQED-AERLRKEAEFEAA 2140
Cdd:TIGR02169 873 ------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEElSEIEDPKGEDEEI 946
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2141 KRAQAEAAALMQKQQADTEmakhkklAEQTLKQ-KFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQV 2219
Cdd:TIGR02169 947 PEEELSLEDVQAELQRVEE-------EIRALEPvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
....*
gi 1988774682 2220 EEELF 2224
Cdd:TIGR02169 1020 FMEAF 1024
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1349-1815 |
1.39e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.79 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1349 EEKAAEKLKAEERKKMA--------EMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqEEVSKREIAAVDAEKQKTNI 1420
Cdd:PRK02224 223 ERYEEQREQARETRDEAdevleeheERREELETLEAEIEDLRETIAETEREREELA----EEVRDLRERLEELEEERDDL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1421 QLELQelknLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 1500
Cdd:PRK02224 299 LAEAG----LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1501 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAEL 1580
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKC 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1581 --------QSKHMSFAEKTSKLEESLKQEhgaVLQLQQEAERLKKQQEDAENSReEAEKELEKWRQKANEALRLRLQAED 1652
Cdd:PRK02224 455 pecgqpveGSPHVETIEEDRERVEELEAE---LEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1653 EAHKKTLAQEEAEKQKEEAEREAK-KRAKAEESALKQKEMAE-------------EELERQRKIAESTAQQKlTAEQELI 1718
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEeKREAAAEAEEEAEEAREevaelnsklaelkERIESLERIRTLLAAIA-DAEDEIE 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1719 RL---RADFDNAEQQR-----------SLLEDELYrlKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtMSNT 1784
Cdd:PRK02224 610 RLrekREALAELNDERrerlaekrerkRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAE-IGAV 686
|
490 500 510
....*....|....*....|....*....|.
gi 1988774682 1785 EKSKQLLEAEAAKMKDLAEEASRLRAISEEA 1815
Cdd:PRK02224 687 ENELEELEELRERREALENRVEALEALYDEA 717
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
163-264 |
1.79e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 78.20 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 163 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 242
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1988774682 243 -VDVPHPDEKSIITYVSSLYDAM 264
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1447-2071 |
5.10e-16 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 86.05 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1447 HSRTKIEEEIRliriQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRqaeEELKRKSEAE 1526
Cdd:pfam12128 241 PEFTKLQQEFN----TLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKR---DELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1527 KEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAeLQSKHMSFAEKTSKLEESLKQEHGAVL 1606
Cdd:pfam12128 314 DAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LTGKHQDVTAKYNRRRSKIKEQNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1607 QLQQEaeRLKKQQEDAENSREEAEKELEK----WRQKANEALRlRLQAEDEAHKKTLAqeeaekqkeeaerEAKKR---A 1679
Cdd:pfam12128 393 AGIKD--KLAKIREARDRQLAVAEDDLQAleseLREQLEAGKL-EFNEEEYRLKSRLG-------------ELKLRlnqA 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1680 KAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQ-------- 1751
Cdd:pfam12128 457 TATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtl 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1752 ----RKQL---EDELAKVRSEmdiliQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEE 1824
Cdd:pfam12128 537 lhflRKEApdwEQSIGKVISP-----ELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEE 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1825 EAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSS 1904
Cdd:pfam12128 612 ALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQL 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1905 EAEMERQKAIVDDTLKQRRvveeEIRILKLNFEKASSGKLDLELELNKlkniadetqqSKIRAEEEAEKLRKLALEEEKR 1984
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKR----EARTEKQAYWQVVEGALDAQLALLK----------AAIAARRSGAKAELKALETWYK 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1985 RREAEEKVKKIaaAEEEAARQRKAALEELERLRKKAEEARKQKD--EADKEAEKQIVVAQQAAQKCSAAEQQVQsvLAQQ 2062
Cdd:pfam12128 758 RDLASLGVDPD--VIAKLKREIRTLERKIERIAVRRQEVLRYFDwyQETWLQRRPRLATQLSNIERAISELQQQ--LARL 833
|
....*....
gi 1988774682 2063 IEDSITQKK 2071
Cdd:pfam12128 834 IADTKLRRA 842
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1125-1939 |
5.72e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 85.79 E-value: 5.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1125 KEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQREL 1204
Cdd:pfam02463 265 EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1205 EQLGRQLGYYRESydwlirwIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDY 1284
Cdd:pfam02463 345 KELEIKREAEEEE-------EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1285 ELQLVAYKAQVEPLVSPLKKTKLdsasdnIIQEYVTLRTRYSELMTLTSqyikfitdtQRRLDDEEKAAEKLKAEERKKM 1364
Cdd:pfam02463 418 EDLLKEEKKEELEILEEEEESIE------LKQGKLTEEKEELEKQELKL---------LKDELELKKSEDLLKETQLVKL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1365 AEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVskREIAAVDAEKQKTNIQLELQELKNLSeqqikdkSQQVDE 1444
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG--GRIISAHGRLGDLGVAVENYKVAIST-------AVIVEV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1445 ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAeAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSE 1524
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSI-AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1525 AEKEAAKQKQKALEDLEKLRMQAE-EAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHG 1603
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEgLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1604 AVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlaqeeaekqkeeAEREAKKRAKAEE 1683
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK-------------SELSLKEKELAEE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1684 SALKQKEMAEEELERQRKIAESTaqqkLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEvaaAQQQRKQLEDELAKVR 1763
Cdd:pfam02463 780 REKTEKLKVEEEKEEKLKAQEEE----LRALEEELKEEAELLEEEQLLIEQEEKIKEEELE---ELALELKEEQKLEKLA 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1764 SEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAA 1843
Cdd:pfam02463 853 EEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLK 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1844 ISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEdqASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRR 1923
Cdd:pfam02463 933 YEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL--GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRA 1010
|
810
....*....|....*.
gi 1988774682 1924 VVEEEIRILKLNFEKA 1939
Cdd:pfam02463 1011 IIEETCQRLKEFLELF 1026
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
166-261 |
1.09e-15 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 75.86 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 166 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEkDLGVTRLLDPED-VD 244
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1988774682 245 VPHPDEKSIITYVSSLY 261
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1449-2360 |
1.09e-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: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1449 RTKIEEEIRLIriqlETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKqvseETQKKRQAEEELKRKSEAE-K 1527
Cdd:TIGR02169 155 RRKIIDEIAGV----AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRR----EREKAERYQALLKEKREYEgY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1528 EAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKtskleeslkqehgavLQ 1607
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---------------LR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1608 LQQEAERLKKQQEDAENSREEAEKELEKW--RQKANEALRLRLQAEDEAHKKTLAqeeaekqkeeaeREAKKRAKAEESA 1685
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAeeRLAKLEAEIDKLLAEIEELEREIE------------EERKRRDKLTEEY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1686 LKQKEmaEEELERQRKIAESTAQQklTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSE 1765
Cdd:TIGR02169 360 AELKE--ELEDLRAELEEVDKEFA--ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1766 MDILIQLKTKAEKETMSNTEKSKQL---LEAEAAKMKDLAEEASRLRaiSEEAKHQRQIAEEEAARQRAE--------AE 1834
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQEWKLEQLaadLSKYEQELYDLKEEYDRVE--KELSKLQRELAEAEAQARASEervrggraVE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1835 RILKEKL----AAISEATRLKTEAEIALkEKEAENERLRRQAEDEAYQRKALEdQASQHK---------QEIEEKIVQLK 1901
Cdd:TIGR02169 514 EVLKASIqgvhGTVAQLGSVGERYATAI-EVAAGNRLNNVVVEDDAVAKEAIE-LLKRRKagratflplNKMRDERRDLS 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1902 KSSEA----------EMERQ-----KAIVDDTLkqrrVVE--EEIRILKLNFEKASsgkldLELEL-----------NKL 1953
Cdd:TIGR02169 592 ILSEDgvigfavdlvEFDPKyepafKYVFGDTL----VVEdiEAARRLMGKYRMVT-----LEGELfeksgamtggsRAP 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1954 KNIADETQQSKIRAEEEAEKLRKLaleeekrrreaeekvkkiaaaeeeaARQRKAALEELERLRKKAEEARkqkdEADKE 2033
Cdd:TIGR02169 663 RGGILFSRSEPAELQRLRERLEGL-------------------------KRELSSLQSELRRIENRLDELS----QELSD 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2034 AEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDsitQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTA 2113
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEED---LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH 790
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2114 AEEEAANQAKAQEDAERLRKEAEFEaaKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDEtdk 2193
Cdd:TIGR02169 791 SRIPEIQAELSKLEEEVSRIEARLR--EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE--- 865
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2194 qksvLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKlLAEEAENMRKLAEDA 2273
Cdd:TIGR02169 866 ----LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIEDPK 940
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2274 ARLSVEAQEAARLRQIAEDDLNQQRALaEKMLKEKMQAIQEAsrlkaeAEMLQKQKDLaQEQAQKLLEDKQLMQQRLEEE 2353
Cdd:TIGR02169 941 GEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEY------EEVLKRLDEL-KEKRAKLEEERKAILERIEEY 1012
|
....*..
gi 1988774682 2354 TEEYHKS 2360
Cdd:TIGR02169 1013 EKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2258-2600 |
1.24e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2258 LLAEEAENMRKLAEDAARlsveAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQ-EASRLKAEAEMLQKQkdlaQEQA 2336
Cdd:COG1196 194 ILGELERQLEPLERQAEK----AERYRELKEELKELEAELLLLKLRELEAELEELEaELEELEAELEELEAE----LAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2337 QKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIA 2416
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2417 TQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQqtfmtEKEMLL 2496
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-----RLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2497 KKEKLIEDEkkrlESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQ 2576
Cdd:COG1196 421 EELEELEEA----LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
330 340
....*....|....*....|....
gi 1988774682 2577 ERILAEENQKLREKLQQLEDAQKD 2600
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLR 520
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1345-1976 |
1.41e-15 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 84.39 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1345 RLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSK------------------R 1406
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdlikennatrhlcnllK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1407 EIAAVDAEK----------------------------------QKTNIQLEL-----------QELKNLSEQQIKDKSQQ 1441
Cdd:pfam05483 162 ETCARSAEKtkkyeyereetrqvymdlnnniekmilafeelrvQAENARLEMhfklkedhekiQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1442 VDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKR 1521
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1522 KSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSaAAELQSKHMSFAEKTSKLEESLKQE 1601
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN-EDQLKIITMELQKKSSELEEMTKFK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1602 HGAVLQLqQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKK-RAK 1680
Cdd:pfam05483 401 NNKEVEL-EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlKTE 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1681 AEESALKQKEM---AEEELERQRKIAESTAQQKLtaeqELIRLRADFDNAEQQRSlledelyRLKNEVAAAQQQRKQLED 1757
Cdd:pfam05483 480 LEKEKLKNIELtahCDKLLLENKELTQEASDMTL----ELKKHQEDIINCKKQEE-------RMLKQIENLEEKEMNLRD 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1758 ELAKVRSEM-DILIQLKTKAEKETMSNTEKSKQLLEAEaAKMKDLAEEASRLRA-ISEEAKHQRQIAEE-EAARQRAEAE 1834
Cdd:pfam05483 549 ELESVREEFiQKGDEVKCKLDKSEENARSIEYEVLKKE-KQMKILENKCNNLKKqIENKNKNIEELHQEnKALKKKGSAE 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1835 -------RILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQA-EDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEA 1906
Cdd:pfam05483 628 nkqlnayEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKlLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVA 707
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1907 EMERQKAIVDDTLKQRrvvEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRK 1976
Cdd:pfam05483 708 LMEKHKHQYDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKM 774
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
165-262 |
2.01e-15 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 74.92 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 165 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD-PEDV 243
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1988774682 244 DVPHPDEKSIITYVSSLYD 262
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1334-1954 |
2.20e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 84.01 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1334 QYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKaIAKAEKEAQElklkmqeevskreiaavDA 1413
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMAD-IRRRESQSQE-----------------DL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1414 EKQKTNIQLELQELKNLSEQQIKDKSQQVDE---ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRdraaeaekL 1490
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIEQlrkMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMH--------F 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1491 RKLAQDEAEKLRKQVSEETQKKRQ---AEEELkrksEAEKEAAKQKQKALedlekLRMQAEEAERQVKQAEIEKEKQIKV 1567
Cdd:pfam15921 216 RSLGSAISKILRELDTEISYLKGRifpVEDQL----EALKSESQNKIELL-----LQQHQDRIEQLISEHEVEITGLTEK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1568 AHEAaqKSAAAELQSKhMSFAEKTSKLEESLKQEH-----GAVLQLQQEAERLKKQQEDaenSREEAEKELEKWRQKANE 1642
Cdd:pfam15921 287 ASSA--RSQANSIQSQ-LEIIQEQARNQNSMYMRQlsdleSTVSQLRSELREAKRMYED---KIEELEKQLVLANSELTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1643 ALRLRLQAE------DEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESA-----------LKQKEMAEEELERQRKIAES 1705
Cdd:pfam15921 361 ARTERDQFSqesgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGnsitidhlrreLDDRNMEVQRLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1706 TAQQKLtaEQELIRLRADFDNAEQQRSL---LEDELYRLKNEVAAAQQQRKQLEDELAKVrSEMDILIQLKTKAEKETMS 1782
Cdd:pfam15921 441 ECQGQM--ERQMAAIQGKNESLEKVSSLtaqLESTKEMLRKVVEELTAKKMTLESSERTV-SDLTASLQEKERAIEATNA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1783 NTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQR-QIAEEEAARQ--RAEAERILkeKLAAISEATRLKTEAEIALK 1859
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVIEilRQQIENMT--QLVGQHGRTAGAMQVEKAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1860 EKEAENERLRRQaedeayQRKALEDQASQHKQEIEEKIVQLK----KSSEAEMERQKAIVDdtLKQRR------------ 1923
Cdd:pfam15921 596 EKEINDRRLELQ------EFKILKDKKDAKIRELEARVSDLElekvKLVNAGSERLRAVKD--IKQERdqllnevktsrn 667
|
650 660 670
....*....|....*....|....*....|....
gi 1988774682 1924 ---VVEEEIRILKLNFEKASSgklDLELELNKLK 1954
Cdd:pfam15921 668 elnSLSEDYEVLKRNFRNKSE---EMETTTNKLK 698
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
46-146 |
3.33e-15 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 74.26 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 46 QKKTFTKWVNKHLIK--AQRHVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMRfhklQNVQIALDFLRHRQV 117
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1988774682 118 KLVNIRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
43-142 |
3.47e-15 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 74.49 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 43 DRVQKKTFTKWVNKHLIKAQ-RHVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLRHR-QV 117
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 1988774682 118 KLVNIRNDDIADGNPKLTLGLIWTI 142
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1673-1930 |
3.75e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 82.86 E-value: 3.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1673 REAKKRAKAEESALKQ-KEMAEEELERQRKIAES-TAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1750
Cdd:pfam17380 288 QQQEKFEKMEQERLRQeKEEKAREVERRRKLEEAeKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1751 QRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKH-QRQIAEEEAARq 1829
Cdd:pfam17380 368 EEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQrEVRRLEEERAR- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1830 raEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQE-IEEKivQLKKSSEAEM 1908
Cdd:pfam17380 447 --EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmIEEE--RKRKLLEKEM 522
|
250 260
....*....|....*....|...
gi 1988774682 1909 E-RQKAIVDDtlKQRRVVEEEIR 1930
Cdd:pfam17380 523 EeRQKAIYEE--ERRREAEEERR 543
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1424-1833 |
4.48e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 82.48 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1424 LQELKNLSEQQIKDKSQqvdealhsrtKIEEEirliRIQLETTEKQKytaesELKQlRDRAAEAEKLRKLAQDE-----A 1498
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE----------KMEQE----RLRQEKEEKAR-----EVER-RRKLEEAEKARQAEMDRqaaiyA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1499 EKLRKQVSEETQKKRQAEEELKRkseaEKEAAKQKQKALE-----DLEKLRMQAEEAERQVKQaEIEKEKQIKVAHEAAQ 1573
Cdd:pfam17380 338 EQERMAMERERELERIRQEERKR----ELERIRQEEIAMEisrmrELERLQMERQQKNERVRQ-ELEAARKVKILEEERQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1574 KSAaaelqSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENsreeaEKELEKWRQKANEALRLRLQAEde 1653
Cdd:pfam17380 413 RKI-----QQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQER-----QQQVERLRQQEEERKRKKLELE-- 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1654 ahkktlaqeeaekqkeeaeREAKKRAKAEEsaLKQKEMAEEELERQRKIAEStaqqkltaeqelirlradfdnaEQQRSL 1733
Cdd:pfam17380 481 -------------------KEKRDRKRAEE--QRRKILEKELEERKQAMIEE----------------------ERKRKL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1734 LEDELYRLKNEVAAAQQQRKQLEdelakvrsemdiliqlktkaEKETMSNTEKSKQLLEaeaaKMKDLAEEASRLRAISE 1813
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAEE--------------------ERRKQQEMEERRRIQE----QMRKATEERSRLEAMER 573
|
410 420
....*....|....*....|
gi 1988774682 1814 EAKHQRQIAEEEAARQRAEA 1833
Cdd:pfam17380 574 EREMMRQIVESEKARAEYEA 593
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1879-2602 |
4.79e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 82.71 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1879 RKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKassgkLDLELELNKLKNIAD 1958
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQ-----LKEKLELEEEYLLYL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1959 ETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQI 2038
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2039 VVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAkekaereaaLLRQQAEEAERQKTAAEEEA 2118
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE---------LEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2119 ANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEqtlkqkfqveqeltkvKLKLDETDKQKSVL 2198
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELE----------------ILEEEEESIELKQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2199 DEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRlIKKDKDSTQKLLAEEAENMRklaedaaRLSV 2278
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR-QKLEERSQKESKARSGLKVL-------LALI 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2279 EAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYH 2358
Cdd:pfam02463 517 KDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2359 KSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAtQEKMTVVERLEFERLNTSKEA 2438
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL-EEGLAEKSEVKASLSELTKEL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2439 DDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVK 2518
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2519 KAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQErILAEENQKLREKLQQLEDAQ 2598
Cdd:pfam02463 756 RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA-ELLEEEQLLIEQEEKIKEEE 834
|
....
gi 1988774682 2599 KDQH 2602
Cdd:pfam02463 835 LEEL 838
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2302-2601 |
6.64e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 82.09 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2302 EKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEdkQLMQQRLEEETEEyhKSLEVERKRQLEimaEAERLR-- 2379
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFE--KMEQERLRQEKEE--KAREVERRRKLE---EAEKARqa 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2380 -------LQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQ-EKMTVVERLEFERLNTS----KEADDLRKAIAD 2447
Cdd:pfam17380 328 emdrqaaIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEiSRMRELERLQMERQQKNervrQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2448 LENEKARLKKEAEELQNKSKEMADAQQKKIEhektVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQ 2527
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVR----RLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK 483
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774682 2528 ERQKQQMEQEKKTLQATMDAalSKQKEAEEEMLRKQKEMQELERQRL---EQERILAEENqklREKLQQLEDAQKDQ 2601
Cdd:pfam17380 484 RDRKRAEEQRRKILEKELEE--RKQAMIEEERKRKLLEKEMEERQKAiyeEERRREAEEE---RRKQQEMEERRRIQ 555
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
975-1761 |
7.11e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.42 E-value: 7.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 975 EKGQQNETLC--KNYISELKDLRLRIEDCEAgtvarirkpveKEPLKEYIQKTTEQKKVQGELDGLKKDLDKVSVKTQEV 1052
Cdd:TIGR02169 195 EKRQQLERLRreREKAERYQALLKEKREYEG-----------YELLKEKEALERQKEAIERQLASLEEELEKLTEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1053 lasPQPSASAPVLRSELDLTVQKMDHAHMLSsvYLEKLKTVEMVIRNTQGAEGVLKQYEDCLREvhTVPSDVKEVETYRA 1132
Cdd:TIGR02169 264 ---EKRLEEIEQLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1133 KLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLG 1212
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1213 YYRESYDWLIRWIADAKQRQEKIQavpiTDSKTLKEQLAQEKKLLEEIEQNKDKVDEcQKYAK-----AYIDTIKDYELQ 1287
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELE----EEKEDKALEIKKQEWKLEQLAADLSKYEQ-ELYDLkeeydRVEKELSKLQRE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1288 LVAYKAQVEPLV--SPLKKTKLDSASDNIIQEYVTLRtrysELMTLTSQYIKFI-TDTQRRL-----DDEEKAAEKLK-A 1358
Cdd:TIGR02169 492 LAEAEAQARASEerVRGGRAVEEVLKASIQGVHGTVA----QLGSVGERYATAIeVAAGNRLnnvvvEDDAVAKEAIElL 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1359 EERK----------KMAEMQAELDKqkqLAEAHAKAIAK-----AEKEAQELKLKMQEEVSKREIAAvdAEKQKTNIQL- 1422
Cdd:TIGR02169 568 KRRKagratflplnKMRDERRDLSI---LSEDGVIGFAVdlvefDPKYEPAFKYVFGDTLVVEDIEA--ARRLMGKYRMv 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1423 ----ELQELK-------NLSEQQIKDKSQQVDEALHSRTKIEEeirlIRIQLETTEKQKYTAESELKQLRDRAAEAEKLR 1491
Cdd:TIGR02169 643 tlegELFEKSgamtggsRAPRGGILFSRSEPAELQRLRERLEG----LKRELSSLQSELRRIENRLDELSQELSDASRKI 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1492 KLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEaEKEAAKQKQKAL--------EDLEKLRMQAEEAER-------QVKQ 1556
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ-EIENVKSELKELearieeleEDLHKLEEALNDLEArlshsriPEIQ 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1557 AEIEKEKQIKVAHEAAQKSAAAELQSKHM--SFAEKTSKLEESLKQE---------------HGAVLQLQQEAERLKKQQ 1619
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLekEYLEKEIQELQEQRIDlkeqiksiekeienlNGKKEELEEELEELEAAL 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1620 EDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlaqeeaekQKEEAEREAKKRAKAEESALKQKEMAEEELERQ 1699
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK---------RKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 1700 RKIAESTAQQKLTAEQELIRLRADFDN-AEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAK 1761
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMlAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1401-1884 |
8.04e-15 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 81.60 E-value: 8.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1401 EEVSKREIAAVDAEKQKTNIQlELQELKNLSEQQIKDKSQQVDEALHSRTkIEEEIRLIRIqletteKQKYTAESELKQL 1480
Cdd:NF033838 38 EEVRGGNNPTVTSSGNESQKE-HAKEVESHLEKILSEIQKSLDKRKHTQN-VALNKKLSDI------KTEYLYELNVLKE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1481 RDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEeelKRKSEAEKEAAKQKQKALEDL-----EKLRMQAEEAERQVK 1555
Cdd:NF033838 110 KSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEAT---KKVEEAEKKAKDQKEEDRRNYptntyKTLELEIAESDVEVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1556 QAEIEKEKQikvaheaaqksaaaelqskhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEK 1635
Cdd:NF033838 187 KAELELVKE-----------------------EAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1636 WRQKANEALrlrlqaEDEAHKKTLAQEEAEKQKEEAEREAKKR--AKAEESALKQKEMAEEELERQRKIAEstAQQKLTA 1713
Cdd:NF033838 244 KLKEAVEKN------VATSEQDKPKRRAKRGVLGEPATPDKKEndAKSSDSSVGEETLPSPSLKPEKKVAE--AEKKVEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1714 EQElirlRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELakvrsemdiliqlkTKAEKETMSNTEKSKQLLEA 1793
Cdd:NF033838 316 AKK----KAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELEL--------------VKEEAKEPRNEEKIKQAKAK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1794 EAAKMKdlaeEASRLraisEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAEN---ERLRR 1870
Cdd:NF033838 378 VESKKA----EATRL----EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQpkaEKPAD 449
|
490
....*....|....
gi 1988774682 1871 QAEDEAYQRKALED 1884
Cdd:NF033838 450 QQAEEDYARRSEEE 463
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1377-1839 |
8.34e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 81.35 E-value: 8.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1377 LAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLsEQQIKDKSQQVDEALHSRTKIEEEI 1456
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEL-EEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1457 RLIRIQLETTEkqkytAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKA 1536
Cdd:COG4717 126 QLLPLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1537 LEDLEKLRMQAEEAERQVKQ------AEIEKEKQIKVAHEAAQK-----------SAAAELQSKHMSFAEKTSKLEESLK 1599
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEeleeleEELEQLENELEAAALEERlkearlllliaAALLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1600 QEHG----AVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKAnEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREA 1675
Cdd:COG4717 281 LVLGllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELL-AALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1676 KKRAKAEESALKQKEM-----AEEELERQRKIAESTAQQKLTAEQELI--RLRADFDNAEQQ-----RSLLEDELYRLKN 1743
Cdd:COG4717 360 EEELQLEELEQEIAALlaeagVEDEEELRAALEQAEEYQELKEELEELeeQLEELLGELEELlealdEEELEEELEELEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1744 EVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtmsntekskQLLEAEAAKMKDLAEEASRLRAISEE-AKHQRQIA 1822
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEEDGELAELL---------QELEELKAELRELAEEWAALKLALELlEEAREEYR 510
|
490
....*....|....*..
gi 1988774682 1823 EEEAARQRAEAERILKE 1839
Cdd:COG4717 511 EERLPPVLERASEYFSR 527
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2334-2605 |
1.14e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2334 EQAQKLLEDkqlMQQRLE------EETEEYHKSLEVERKRQL---EIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQAD 2404
Cdd:COG1196 175 EEAERKLEA---TEENLErledilGELERQLEPLERQAEKAEryrELKEELKELEAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2405 KVATRLHETEIATQEKMTVVERLEFERLNTSKEA--DDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKT 2482
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEaqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2483 VLQQTfmTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRK 2562
Cdd:COG1196 332 LEELE--EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1988774682 2563 QKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRE 2605
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1531-1883 |
1.38e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 80.94 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1531 KQKQKALEDLEKLRMQAE------EAERQVKQAEIEKEKQIKVAHEAAqksaaaeLQSKHMSFAEKTSKLEESLKQEhga 1604
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEkeekarEVERRRKLEEAEKARQAEMDRQAA-------IYAEQERMAMERERELERIRQE--- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1605 vlQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAedeAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 1684
Cdd:pfam17380 357 --ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA---ARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1685 AlKQKEMAEEELERQRKIaESTAQQKLTAEQELIRLRADfdnaeqqrslledelyrlknevaAAQQQRKQLEDElakvrs 1764
Cdd:pfam17380 432 A-RQREVRRLEEERAREM-ERVRLEEQERQQQVERLRQQ-----------------------EEERKRKKLELE------ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1765 emdiliqlktKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIA-EEEAARQRAEAER---ILKEK 1840
Cdd:pfam17380 481 ----------KEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAiYEEERRREAEEERrkqQEMEE 550
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1988774682 1841 LAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAyQRKALE 1883
Cdd:pfam17380 551 RRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4035-4073 |
1.56e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.05 E-value: 1.56e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1988774682 4035 LLEAQIATGGIIDPEESHRLPVEVAYNRGFFDEEMNEIL 4073
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1111-1932 |
1.61e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.27 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1111 EDCLREVHTVPSDVKEVETY----RAKLKKMRTEAEDEQPvFDSLEEELkkasavsdkmvrvhseRDVELDHFRQQLSSL 1186
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIidekRQQLERLRREREKAER-YQALLKEK----------------REYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1187 QDRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKiqavpitdsKTLKEQLAQEKKLLE---EIEQN 1263
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD---------LGEEEQLRVKEKIGEleaEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1264 KDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKKTKLDSASdnIIQEYVTLRTRYSELmtltsqyikfitdtQ 1343
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK--LTEEYAELKEELEDL--------------R 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1344 RRLDDEEKAAeklkAEERKKMAEMQAELDKqkqlaeahakaiakaekeaqelkLKMQEEVSKREIAAVDAEKQKTNIQLE 1423
Cdd:TIGR02169 371 AELEEVDKEF----AETRDELKDYREKLEK-----------------------LKREINELKRELDRLQEELQRLSEELA 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1424 lqELKNlseqQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKL-- 1501
Cdd:TIGR02169 424 --DLNA----AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAea 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1502 RKQVSEETQKKRQAEEELKRKS--------EAEKEAAKQKQKALEDLEKLRMQA---EEAERQVKQAEIEKEKQI----- 1565
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASiqgvhgtvAQLGSVGERYATAIEVAAGNRLNNvvvEDDAVAKEAIELLKRRKAgratf 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1566 ----KVAHEAAQKSAAA-----------------------------------ELQSKHMSFAEKTSkLEESLKQEHGAV- 1605
Cdd:TIGR02169 578 lplnKMRDERRDLSILSedgvigfavdlvefdpkyepafkyvfgdtlvvediEAARRLMGKYRMVT-LEGELFEKSGAMt 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1606 -------------LQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRlqaeDEAHKKTlaqeeaekqkeeae 1672
Cdd:TIGR02169 657 ggsraprggilfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL----SDASRKI-------------- 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1673 REAKKRAkaeESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 1752
Cdd:TIGR02169 719 GEIEKEI---EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPE 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1753 KQLE-DELAKVRSEMD-ILIQLKTKAEKETMSNT--EKSKQLLEAEAAKMKDlaEEASRLRAISEEAKHQRQIAEEEAAR 1828
Cdd:TIGR02169 796 IQAElSKLEEEVSRIEaRLREIEQKLNRLTLEKEylEKEIQELQEQRIDLKE--QIKSIEKEIENLNGKKEELEEELEEL 873
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1829 QRAEAERI--LKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASqhkqEIEEKIVQLKKSSEA 1906
Cdd:TIGR02169 874 EAALRDLEsrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEE 949
|
890 900
....*....|....*....|....*.
gi 1988774682 1907 EMerqkaIVDDTLKQRRVVEEEIRIL 1932
Cdd:TIGR02169 950 EL-----SLEDVQAELQRVEEEIRAL 970
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1220-1896 |
2.26e-14 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 80.15 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1220 WLIRWIADAKQRQEKIQ---AVPITDSKTLKE-QLAQEK---KLLEEIEQNKDKVDE----------CQKYAKAYIDTIK 1282
Cdd:pfam05483 93 WKVSIEAELKQKENKLQenrKIIEAQRKAIQElQFENEKvslKLEEEIQENKDLIKEnnatrhlcnlLKETCARSAEKTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1283 DYELQ-------LVAYKAQVEPLVSPLKKTKLdSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRL--------- 1346
Cdd:pfam05483 173 KYEYEreetrqvYMDLNNNIEKMILAFEELRV-QAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVsllliqite 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1347 -DDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQ 1425
Cdd:pfam05483 252 kENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1426 ELKNLSEQQIKDKSQQ---VDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLR 1502
Cdd:pfam05483 332 EKEAQMEELNKAKAAHsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1503 KQVSEETQ---KKRQAE---EELKRKSEAEKEAAKQKQKALEDLEkLRMQAEEAERQVKQAEIEKEKqikvaheaaqksa 1576
Cdd:pfam05483 412 KILAEDEKlldEKKQFEkiaEELKGKEQELIFLLQAREKEIHDLE-IQLTAIKTSEEHYLKEVEDLK------------- 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1577 aAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRlqAEDEAHK 1656
Cdd:pfam05483 478 -TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR--DELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1657 KTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMA--EEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLL 1734
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1735 EDELYRLKNEVAAAQQQRKQLEDELAKVrsemdilIQLKTKAEKETMSNTEKSKQLLEaEAAKM-----KDLAEEASRLR 1809
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDNYQKE-------IEDKKISEEKLLEEVEKAKAIAD-EAVKLqkeidKRCQHKIAEMV 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1810 AISEEAKHQRQIAEEEaarqRAEAERILKEKLaaiSEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQH 1889
Cdd:pfam05483 707 ALMEKHKHQYDKIIEE----RDSELGLYKNKE---QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKEN 779
|
....*..
gi 1988774682 1890 KQEIEEK 1896
Cdd:pfam05483 780 TAILKDK 786
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
161-258 |
2.63e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 71.64 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLD 239
Cdd:cd21230 1 TPKQRLLGWIQ---NKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1988774682 240 PEDVDVPHPDEKSIITYVS 258
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2259-2571 |
2.84e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2259 LAEEAENmrklAEDAARLSVEAQEA-ARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQ 2337
Cdd:COG1196 205 LERQAEK----AERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2338 KLLEDKQLMQQRLEEETEEYHKSLEVERKR-------QLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRL 2410
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERrreleerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2411 HETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMT 2490
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2491 EKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELE 2570
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
.
gi 1988774682 2571 R 2571
Cdd:COG1196 521 G 521
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1895-2578 |
3.64e-14 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 79.77 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1895 EKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASsgkLDLELELNKLKNIADETQQSKIRAEEEAEKL 1974
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVS---LKLEEEIQENKDLIKENNATRHLCNLLKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1975 RKLAlEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELerlRKKAEEARKQKDEADKEAEKQIVVAQQAAQK-CSAAEQ 2053
Cdd:pfam05483 165 ARSA-EKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL---RVQAENARLEMHFKLKEDHEKIQHLEEEYKKeINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2054 QVQSVLAQQIEDSITQKKLkeeyekakklakeaeaakekaereAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRK 2133
Cdd:pfam05483 241 QVSLLLIQITEKENKMKDL------------------------TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2134 EaeFEAAKRAQAEAAALMQKQQADTEMAKhKKLAEQTLKQKFQVEqELTKVK----LKLDETDKQKSVLDEELQRLKDEV 2209
Cdd:pfam05483 297 E--LEDIKMSLQRSMSTQKALEEDLQIAT-KTICQLTEEKEAQME-ELNKAKaahsFVVTEFEATTCSLEELLRTEQQRL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2210 DDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLiKKDKDSTQKLLaEEAENMRKLAEDaarLSVEAQEAARLRQI 2289
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEEL-KKILAEDEKLL-DEKKQFEKIAEE---LKGKEQELIFLLQA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2290 AEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQ-KQKDLAQEQAQKLLEDKQLMQQR--LEEETEEYHKSLEVERK 2366
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHCDKLLLENKELTQEAsdMTLELKKHQEDIINCKK 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2367 RQLEIMAEAERLRLQVSQLseaQARAEEEAKKFKKQADKVATRLHETE-------IATQEKMTVVERLEFERLNTSKEAD 2439
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNL---RDELESVREEFIQKGDEVKCKLDKSEenarsieYEVLKKEKQMKILENKCNNLKKQIE 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2440 DLRKAIADLENEKARLKKEAEElQNKSKEMADAQQKKIEHEKTVLQQTFmteKEMLLKKEKLIEDeKKRLESQFEEEVKK 2519
Cdd:pfam05483 605 NKNKNIEELHQENKALKKKGSA-ENKQLNAYEIKVNKLELELASAKQKF---EEIIDNYQKEIED-KKISEEKLLEEVEK 679
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774682 2520 AKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRlEQER 2578
Cdd:pfam05483 680 AKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNK-EQEQ 737
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
161-261 |
4.79e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 71.64 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 240
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1988774682 241 ED-VDVPHPDEKSIITYVSSLY 261
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1320-1964 |
5.70e-14 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 79.03 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1320 TLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDkqkqlaeahakAIAKAEKEAQELKLKM 1399
Cdd:pfam07111 52 SLELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELD-----------ALAVAEKAGQAEAEGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1400 QEEVSKREIAAVDAEKQKtniQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTekqkytaeselkq 1479
Cdd:pfam07111 121 RAALAGAEMVRKNLEEGS---QRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETK------------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1480 lrdRAAEAEKLrKLAQDEAEKLRKQVSeETQKKRQAEEELkrkseaekeaakqkqkaLEDLEKLRMQAEEAERQVKQAEI 1559
Cdd:pfam07111 185 ---RAGEAKQL-AEAQKEAELLRKQLS-KTQEELEAQVTL-----------------VESLRKYVGEQVPPEVHSQTWEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1560 EKEKQIKVAHEAaqKSAAAELQSkhmsfaekTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSR--EEAEKELEKWR 1637
Cdd:pfam07111 243 ERQELLDTMQHL--QEDRADLQA--------TVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEfpKKCRSLLNRWR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1638 QKANeALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERqrkIAESTAQQKLTAEQEL 1717
Cdd:pfam07111 313 EKVF-ALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVER---MSAKGLQMELSRAQEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1718 -IRLRADFDNAEQQRSL-----------LEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAE--KETMSN 1783
Cdd:pfam07111 389 rRRQQQQTASAEEQLKFvvnamsstqiwLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQlrQESCPP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1784 TEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQiAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEA 1863
Cdd:pfam07111 469 PPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1864 ENERLRRQ--AEDEAYQRKALEDQASQHKQEIEEKIVQL------------KKSSEAEMERQKAIVDDTLKQRRVVEE-- 1927
Cdd:pfam07111 548 EVARQGQQesTEEAASLRQELTQQQEIYGQALQEKVAEVetrlreqlsdtkRRLNEARREQAKAVVSLRQIQHRATQEke 627
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1988774682 1928 ---EIRILKLNFEKASSGKLDLEL-ELNKLKNIADETQQSK 1964
Cdd:pfam07111 628 rnqELRRLQDEARKEEGQRLARRVqELERDKNLMLATLQQE 668
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1274-1900 |
6.21e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.19 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1274 AKAYIDTIKDYELQLVAYKAQVEPLvSPLKKTKldsasdniiQEYVTLRTRYSELMTLtsqyikfitDTQRRLDDEEKAA 1353
Cdd:COG4913 230 LVEHFDDLERAHEALEDAREQIELL-EPIRELA---------ERYAAARERLAELEYL---------RAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1354 EKLKAEERkkmaEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQE------EVSKREIAavDAEKQKTNIQLELQEL 1427
Cdd:COG4913 291 ELLEAELE----ELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrlEQLEREIE--RLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1428 KNL----------SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQkytAESELKQLRDRAAEAEKLRKLAQDE 1497
Cdd:COG4913 365 EALlaalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIASLERRKSNIPAR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1498 AEKLRKQVSEETQKKrqaEEELK--------RKSEAEKEAA----------------KQKQKALEDLE----KLRMQAEE 1549
Cdd:COG4913 442 LLALRDALAEALGLD---EAELPfvgelievRPEEERWRGAiervlggfaltllvppEHYAAALRWVNrlhlRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1550 AERQVKQAEIEKEK------QIKVAHEAAQKSAAAELQsKHMSFAEKTSklEESLKQEHGAVL---QLQQEAERLKKQQE 1620
Cdd:COG4913 519 VRTGLPDPERPRLDpdslagKLDFKPHPFRAWLEAELG-RRFDYVCVDS--PEELRRHPRAITragQVKGNGTRHEKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1621 DAENSR----EEAEKELEKWRQKANEalrlrLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEEL 1696
Cdd:COG4913 596 RRIRSRyvlgFDNRAKLAALEAELAE-----LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1697 ERqrkiaestaqqkltAEQELIRLRADFDNAEQqrslLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKA 1776
Cdd:COG4913 671 AE--------------LEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1777 EKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKE--------------KLA 1842
Cdd:COG4913 733 QDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldaDLE 812
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774682 1843 AISE-ATRLKTEAEIALKEKEAENERLRRQAEDEayQRKALEDQASQHKQEIEEKIVQL 1900
Cdd:COG4913 813 SLPEyLALLDRLEEDGLPEYEERFKELLNENSIE--FVADLLSKLRRAIREIKERIDPL 869
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
620-809 |
6.28e-14 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 74.02 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 620 LHAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDIQALGDRLVRDGHPGKKTVESFT 699
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 700 AALQTQWSWILQLCCCIEAHLKENTAYYQFFADVKEAQDKMKKMQENMKkkySCDRSTTATRLEDLLQDAAEEKEQLNEF 779
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 1988774682 780 KTVVAGLNKRSRSIIQLKPRNPTTSIKGKL 809
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3721-3759 |
7.81e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 68.12 E-value: 7.81e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1988774682 3721 LLEAQAATGFIVDPLKNETLTVDEAVRKGVVGPEIHDKL 3759
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3388-3426 |
1.26e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 67.35 E-value: 1.26e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1988774682 3388 LLEAQAASGFIVDPVRNQCLSVDEAVKSGVVGPELHEKL 3426
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1423-1902 |
1.75e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.65 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1423 ELQELKNLsEQQIKDKSQQVD-----EALHSR-TKIEEEIRLIRIQLETTekQKYTAESELKQLRDRAAEAEKLRKLAQD 1496
Cdd:COG4913 233 HFDDLERA-HEALEDAREQIEllepiRELAERyAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1497 EAEKLRKQVSEETQKKRQAEEEL-----KRKSEAEKEAAkQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEA 1571
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIrgnggDRLEQLEREIE-RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1572 AQkSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQ----EDAENSREEAEKEL-------------- 1633
Cdd:COG4913 389 AA-ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEALgldeaelpfvgeli 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1634 ------EKWRQKANEAL---RLRLQAEDEAHKK-------TLAQEEAEKQKEEAEREAKKRAKAEESALKQK-------- 1689
Cdd:COG4913 468 evrpeeERWRGAIERVLggfALTLLVPPEHYAAalrwvnrLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKldfkphpf 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1690 -EMAEEELERQRKIA--ESTAQQK-----LTAE------------QELIRLRAD----FDNAEQqRSLLEDELYRLKNEV 1745
Cdd:COG4913 548 rAWLEAELGRRFDYVcvDSPEELRrhpraITRAgqvkgngtrhekDDRRRIRSRyvlgFDNRAK-LAALEAELAELEEEL 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1746 AAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKE--------TMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKH 1817
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAELEELEE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1818 QRQIAEEEAARQRAEAERI------LKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAY-QRKALEDQASQHK 1890
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAeeeldeLQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEeRIDALRARLNRAE 786
|
570
....*....|..
gi 1988774682 1891 QEIEEKIVQLKK 1902
Cdd:COG4913 787 EELERAMRAFNR 798
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2342-2601 |
1.85e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2342 DKQLmqQRLEEE---TEEYHKSLEVERKRQLEIMA-EAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAT 2417
Cdd:COG1196 199 ERQL--EPLERQaekAERYRELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2418 QEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLK 2497
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2498 KEKLIEDEKKRLESqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQE 2577
Cdd:COG1196 357 EAELAEAEEALLEA--EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260
....*....|....*....|....
gi 1988774682 2578 RILAEENQKLREKLQQLEDAQKDQ 2601
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEE 458
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
161-261 |
2.50e-13 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 69.29 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 240
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1988774682 241 ED-VDVPHPDEKSIITYVSSLY 261
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1393-1952 |
3.26e-13 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 75.84 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1393 QELKlKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQ-QIKDKSQQVDEAlHSRTKIE-EEIRLIRIQLETTEKQK 1470
Cdd:pfam05701 42 LELE-KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEElKLNLERAQTEEA-QAKQDSElAKLRVEEMEQGIADEAS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1471 YTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQ----VSEETQKKRQAEEELKrkseaekeAAKQKQKALEDLEKLRMQ 1546
Cdd:pfam05701 120 VAAKAQLEVAKARHAAAVAELKSVKEELESLRKEyaslVSERDIAIKRAEEAVS--------ASKEIEKTVEELTIELIA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1547 AEEAERQVKQAEIEKEKqikvaheaaQKSAAAelqskhMSFAEKTSKLEESLKqehgavlQLQQEAERLKKQQedaeNSR 1626
Cdd:pfam05701 192 TKESLESAHAAHLEAEE---------HRIGAA------LAREQDKLNWEKELK-------QAEEELQRLNQQL----LSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1627 EEAEKELEkwrqkANEALRLRLQAEDEAHKktlaqeeaekqKEEAEREAKKRAKAEESALKQKEM---AEEELERQRKIA 1703
Cdd:pfam05701 246 KDLKSKLE-----TASALLLDLKAELAAYM-----------ESKLKEEADGEGNEKKTSTSIQAAlasAKKELEEVKANI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1704 EstaqqKLTAEQELIRLRAdfdnaeqqrSLLEDELYRLKNEVAAAQQQR-------KQLEDELAKVRSEMDiLIQLKTKA 1776
Cdd:pfam05701 310 E-----KAKDEVNCLRVAA---------ASLRSELEKEKAELASLRQREgmasiavSSLEAELNRTKSEIA-LVQAKEKE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1777 EKETMsnTEKSKQLLEA--EAAKMKDLAEEA-SRLRAISEEAKHQRqiAEEEAARQRAEAerILKEKLAAIsEATRLKTE 1853
Cdd:pfam05701 375 AREKM--VELPKQLQQAaqEAEEAKSLAQAArEELRKAKEEAEQAK--AAASTVESRLEA--VLKEIEAAK-ASEKLALA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1854 AEIALKEKEAENERLRRQA----------EDEAYQRKALEDQASQHKQeIEEKIVQLKKSSEAEMeRQKAIVDDTLKQRR 1923
Cdd:pfam05701 448 AIKALQESESSAESTNQEDsprgvtlsleEYYELSKRAHEAEELANKR-VAEAVSQIEEAKESEL-RSLEKLEEVNREME 525
|
570 580
....*....|....*....|....*....
gi 1988774682 1924 VVEEEIRILKLNFEKASSGKLDLELELNK 1952
Cdd:pfam05701 526 ERKEALKIALEKAEKAKEGKLAAEQELRK 554
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
40-145 |
3.29e-13 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 68.85 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 40 DERDrvqKKTFTKWVNKHLIKAQRHvtDLYEDLRDGhnlISLLEVL--------SGETLPREKGRMRFHKLQNVQIALDF 111
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDPLIN--NLYEDLRDG---LVLLQVLdkiqpgcvNWKKVNKPKPLNKFKKVENCNYAVDL 73
|
90 100 110
....*....|....*....|....*....|....
gi 1988774682 112 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 145
Cdd:cd21219 74 AKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1674-1906 |
3.67e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 74.80 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1674 EAKKRAKAEESALKQK-EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 1752
Cdd:COG4942 20 DAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1753 KQLEDELAKVRSEMdiliqlktkaekETMSNTEKSKQLLEAEaakmkDLAEEASRLRAISEEAKHQRQIAEE------EA 1826
Cdd:COG4942 100 EAQKEELAELLRAL------------YRLGRQPPLALLLSPE-----DFLDAVRRLQYLKYLAPARREQAEElradlaEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1827 ARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEA 1906
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
64-143 |
4.47e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 68.39 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 64 HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM----RFHKLQNVQIALDFLRHRQV----KLVNIRNDDIADGNPKLT 135
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1988774682 136 LGLIWTII 143
Cdd:cd21223 105 LALLWRII 112
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3057-3095 |
7.51e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.43 E-value: 7.51e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1988774682 3057 LLEAQAGTGYLVDPVHNQKYTVDEAVKAGVVGPELHEKL 3095
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1587-2065 |
8.09e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.80 E-value: 8.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1587 FAEKTSKLEEsLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANealRLRLQAEDEAHKKTLAQEEAEK 1666
Cdd:COG4717 73 LKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ---LLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1667 qkeeaeREAKKRAKAEESALKQKEMAEEELER-QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEV 1745
Cdd:COG4717 149 ------EELEERLEELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1746 AAAQQQRKQLEDELA------KVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKmkdLAEEASRLRAISEEAKHQR 1819
Cdd:COG4717 223 EELEEELEQLENELEaaaleeRLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF---LVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1820 QIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAyqrKALEDQASQhkQEIEEKIVQ 1899
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA---EELEEELQL--EELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1900 LKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLeLELNKLKNIADETQQSKIRAEEEAEKLRKLal 1979
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEEELEEL-- 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1980 eeekrrreaeekvkkiaAAEEEAARQRKAALE---ELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQ 2056
Cdd:COG4717 452 -----------------REELAELEAELEQLEedgELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
....*....
gi 1988774682 2057 SVLAQQIED 2065
Cdd:COG4717 515 PPVLERASE 523
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2014-2609 |
9.54e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 75.39 E-value: 9.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2014 ERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQsVLAQQIEDSITQKKLKEEyEKAKKLAKEAEAAKEKA 2093
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAE-LIIDLEELKLQELKLKEQ-AKKALEYYQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2094 EREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQ 2173
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE-KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2174 KFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKD 2253
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2254 STQKLLAEEAENmRKLAEDAARLSVEAQEAARLRQIAEDDL---NQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKD 2330
Cdd:pfam02463 382 ESERLSSAAKLK-EEELELKSEEEKEAQLLLELARQLEDLLkeeKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2331 LAQEQAQKLLEDKqlmQQRLEEETEEYHKSLEVERK-----RQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADK 2405
Cdd:pfam02463 461 LKDELELKKSEDL---LKETQLVKLQEQLELLLSRQkleerSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2406 VATRLHETEIATQEKMTVVERLEFERLN----TSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEK 2481
Cdd:pfam02463 538 VENYKVAISTAVIVEVSATADEVEERQKlvraLTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2482 TVLQQTFMTEKEMLLKKEKLIE-------------------DEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQ 2542
Cdd:pfam02463 618 DDKRAKVVEGILKDTELTKLKEsakakesglrkgvsleeglAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774682 2543 ATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKV 2609
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1122-1907 |
9.66e-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: 75.21 E-value: 9.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1122 SDVKEVETYRAKLKKMRTEAEdeqPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRwkavftqidlrq 1201
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHE---AMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ------------ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1202 reLEQLGRQLGYYRESydwlirwIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQnkdkvdECQKYAKAYiDTI 1281
Cdd:pfam01576 231 --IAELRAQLAKKEEE-------LQAALARLEEETAQKNNALKKIRELEAQISELQEDLES------ERAARNKAE-KQR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1282 KDYELQLVAYKAQVEplvsplkkTKLDSAsdNIIQEyvtlrtryselmtLTSQYIKFITDTQRRLDDEEKAAEKLKAEER 1361
Cdd:pfam01576 295 RDLGEELEALKTELE--------DTLDTT--AAQQE-------------LRSKREQEVTELKKALEEETRSHEAQLQEMR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1362 KKMA----EMQAELDKQKQLAEAHAKAIAKAEKEAQELklkmQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKD 1437
Cdd:pfam01576 352 QKHTqaleELTEQLEQAKRNKANLEKAKQALESENAEL----QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1438 KSQQVDEAlhsrTKIEEEIRLIRIQLETTEKQKYTAESELKQL---------------RDRAAEAEKLRKLaQDEAEKLR 1502
Cdd:pfam01576 428 RAELAEKL----SKLQSELESVSSLLNEAEGKNIKLSKDVSSLesqlqdtqellqeetRQKLNLSTRLRQL-EDERNSLQ 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1503 KQVSEETQKKRQAEE----------ELKRKSEAEKEAAKQ----KQKALEDLEKLRMQAEEAERQVKQAEIEKEkqiKVA 1568
Cdd:pfam01576 503 EQLEEEEEAKRNVERqlstlqaqlsDMKKKLEEDAGTLEAleegKKRLQRELEALTQQLEEKAAAYDKLEKTKN---RLQ 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1569 HEAAQKSAAAELQSKHMSFAEKTS-KLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALR-- 1645
Cdd:pfam01576 580 QELDDLLVDLDHQRQLVSNLEKKQkKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERtn 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1646 --LRLQAEDEAHKKtlaqeeaeKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTaqqKLTAEQELIRLRAD 1723
Cdd:pfam01576 660 kqLRAEMEDLVSSK--------DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDA---KLRLEVNMQALKAQ 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1724 FDN--------AEQQRSLLEDELYRLKNEVAAAQQQRKQLEDelAKVRSEMDiLIQLKTKAEKETMSNTEKSKQLLEAEa 1795
Cdd:pfam01576 729 FERdlqardeqGEEKRRQLVKQVRELEAELEDERKQRAQAVA--AKKKLELD-LKELEAQIDAANKGREEAVKQLKKLQ- 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1796 AKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERiLKEKLAAiseatrlkteAEIALKEKEAENERLRRQAEDE 1875
Cdd:pfam01576 805 AQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQ-LQEDLAA----------SERARRQAQQERDELADEIASG 873
|
810 820 830
....*....|....*....|....*....|..
gi 1988774682 1876 AYQRKALEDQasqhKQEIEEKIVQLKKSSEAE 1907
Cdd:pfam01576 874 ASGKSALQDE----KRRLEARIAQLEEELEEE 901
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2008-2606 |
1.29e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 74.62 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2008 AALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQ------KCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKK 2081
Cdd:TIGR00618 170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctpcmpDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2082 LAKEAEAAkekaereaalLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAAlmQKQQADTEMA 2161
Cdd:TIGR00618 250 EAQEEQLK----------KQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQ--QAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2162 KHKKLAEQTLKQKFQVEQEltkvklklDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIE 2241
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQ--------QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2242 EENQRLikkdKDSTQKLLAEEAENMRKLAEDAARlSVEAQEAARLR---QIAEDDLNQQRALAEKMLKEKMQAIQEASR- 2317
Cdd:TIGR00618 390 TLTQKL----QSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKkqqELQQRYAELCAAAITCTAQCEKLEKIHLQEs 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2318 ---LKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQ-----VSQLSEAQ 2389
Cdd:TIGR00618 465 aqsLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQrgeqtYAQLETSE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2390 ARAEEEAKKFKKQA----DKVATRLHETEIATQEKMTVVERLEferlNTSKEADDLRKAIADLENEKARLKKEAEELQNK 2465
Cdd:TIGR00618 545 EDVYHQLTSERKQRaslkEQMQEIQQSFSILTQCDNRSKEDIP----NLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2466 SKEMADAQQKKIE----HEKTVLQQTFMTEKEMLLKKEK------LIEDEKKRLESQFEEEVKKAKALKDEQERQKQQME 2535
Cdd:TIGR00618 621 LQPEQDLQDVRLHlqqcSQELALKLTALHALQLTLTQERvrehalSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 2536 QEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRET 2606
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1913-2609 |
1.32e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.72 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1913 AIVDDTLKQRRVVEEEIRILKlnFEKASSGKLDLELELNKLKniadETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKV 1992
Cdd:PRK03918 139 AILESDESREKVVRQILGLDD--YENAYKNLGEVIKEIKRRI----ERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1993 KKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVqSVLAQQIEDSITQKKL 2072
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI-EELEEKVKELKELKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2073 KEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKE-AEFEAAKRAQaeaaalm 2151
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRlEELEERHELY------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2152 qkqqadtEMAKHKKLAEQTLKQKFQVEqELTKVKLKLDETDKQKSVLDEELQRLKDEvddavkqRGQVEEELFKVKVQME 2231
Cdd:PRK03918 365 -------EEAKAKKEELERLKKRLTGL-TPEKLEKELEELEKAKEEIEEEISKITAR-------IGELKKEIKELKKAIE 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2232 ELLKLKNKIEEENQRLIKKDKdstQKLLAEEAENMRKLAEDAARLsveaqeAARLRQIaeddlnqqralaEKMLKEKMQA 2311
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHR---KELLEEYTAELKRIEKELKEI------EEKERKL------------RKELRELEKV 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2312 IQEASRLKAEAEMLQKQKDLAQEQAQKLLEDkqlmqqrLEEETEEYHKSLEverkRQLEIMAEAERLRLQVSQLSEAQAR 2391
Cdd:PRK03918 489 LKKESELIKLKELAEQLKELEEKLKKYNLEE-------LEKKAEEYEKLKE----KLIKLKGEIKSLKKELEKLEELKKK 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2392 AEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMAD 2471
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAE 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2472 AQqKKIEhektvlqqtfMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQatmdaalsK 2551
Cdd:PRK03918 638 TE-KRLE----------ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE--------K 698
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774682 2552 QKEAEEEMLRKQKEMQELERQRleqerilaEENQKLREKLQQLEDAQKDQHTRETDKV 2609
Cdd:PRK03918 699 LKEELEEREKAKKELEKLEKAL--------ERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2165-2597 |
1.51e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.03 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2165 KLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEeelfkvkvQMEELLKLKNKIEEEN 2244
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP--------LYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2245 QRLikkdkdstqKLLAEEAENMRKLAEDAARLSVEAQEAarlrqiaeddlnqQRALAEKMLKEKMQAIQEASRLKAEAEM 2324
Cdd:COG4717 146 ERL---------EELEERLEELRELEEELEELEAELAEL-------------QEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2325 LQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEE---------- 2394
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2395 ------------EAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEEL 2462
Cdd:COG4717 284 gllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2463 QNKSKEmadaqqkkiEHEKTVLQQTFMTEKEMLLKKEKL------IEDEKKRLESQFEEEVKKAKALKDEQErqKQQMEQ 2536
Cdd:COG4717 364 QLEELE---------QEIAALLAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEELLEALD--EEELEE 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 2537 EKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQEriLAEENQKLREKLQQLEDA 2597
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE--LLQELEELKAELRELAEE 491
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
48-149 |
1.74e-12 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 66.88 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 48 KTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVL-------SGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1988774682 121 NIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1749-2599 |
2.01e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 74.09 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1749 QQQRKQLEDELAKVRSEMDiliQLKTKAEKETMSNTEKSKQ-------LLEAEAAKMK-------DLAEEASR-LRAISE 1813
Cdd:NF041483 7 QESHRADDDHLSRFEAEMD---RLKTEREKAVQHAEDLGYQvevlrakLHEARRSLASrpaydgaDIGYQAEQlLRNAQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1814 EAKHQRQIAEEEAARQRAEAERILKEKlaaISEATRLKTEAeialkEKEAeNERLRRQAEDEAYQRKALEDQ-------A 1886
Cdd:NF041483 84 QADQLRADAERELRDARAQTQRILQEH---AEHQARLQAEL-----HTEA-VQRRQQLDQELAERRQTVESHvnenvawA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1887 SQHKQEIEEKIVQLKKSSEAEMErqKAIVDDTLKQRRVVEEEIRILKLNFEKASSgkldlelelnklkniadETQQSKIR 1966
Cdd:NF041483 155 EQLRARTESQARRLLDESRAEAE--QALAAARAEAERLAEEARQRLGSEAESARA-----------------EAEAILRR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1967 AEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAAL---------EELERLRKKAEEARKQKDEADKEAEKQ 2037
Cdd:NF041483 216 ARKDAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELsraaeqrmqEAEEALREARAEAEKVVAEAKEAAAKQ 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2038 IVVAQQA-AQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAAL-------LRQQAEEAER 2109
Cdd:NF041483 296 LASAESAnEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAaedtaaqLAKAARTAEE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2110 QKTAAEE-EAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQA---DTE--MAKHKKLAEQTLKQKFQVEQeltk 2183
Cdd:NF041483 376 VLTKASEdAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAakdDTKeyRAKTVELQEEARRLRGEAEQ---- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2184 vkLKLDETDKQKSVLDEELQRLKDEVDDAVKqrgQVEEELFKVKVQMEElLKLKNKIEEENQRLIKKDKDSTQKLLAEEA 2263
Cdd:NF041483 452 --LRAEAVAEGERIRGEARREAVQQIEEAAR---TAEELLTKAKADADE-LRSTATAESERVRTEAIERATTLRRQAEET 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2264 enMRKLAEDAARLSVEAQE-AARLRQIAEDDLNQQRALAEK-MLKEKMQAIQEASRLKAEAEmlqkQKDLAQEQAqklLE 2341
Cdd:NF041483 526 --LERTRAEAERLRAEAEEqAEEVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAE----ERLTAAEEA---LA 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2342 DKQLMQQRLEEETEEYHKSLEV---ERKRQLEIMAEAERLRLQVSQLSEAQARaeeeakkfKKQADKVATRLHETEIATQ 2418
Cdd:NF041483 597 DARAEAERIRREAAEETERLRTeaaERIRTLQAQAEQEAERLRTEAAADASAA--------RAEGENVAVRLRSEAAAEA 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2419 EKMTVVERLEFERLNTSKEADDLR------KAIADLENEKARLKKEAEELQNKSKEMADAQQKKI-EHEKTVLQQTFMTE 2491
Cdd:NF041483 669 ERLKSEAQESADRVRAEAAAAAERvgteaaEALAAAQEEAARRRREAEETLGSARAEADQERERArEQSEELLASARKRV 748
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2492 KEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMD-AALSKQKEAEEEMLRKQKEMQElE 2570
Cdd:NF041483 749 EEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEhAAERTRTEAQEEADRVRSDAYA-E 827
|
890 900
....*....|....*....|....*....
gi 1988774682 2571 RQRleqeriLAEENQKLREKLQQLEDAQK 2599
Cdd:NF041483 828 RER------ASEDANRLRREAQEETEAAK 850
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1765-2539 |
2.47e-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: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1765 EMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAI 1844
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1845 SEATRLKTEAEIALKEKEAENERLRRQaedeayqrkaleDQASQHKQEIEEKIVQlkkssEAEMERQKAIVDDTLKQRRV 1924
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQ------------QLLKQLRARIEELRAQ-----EAVLEETQERINRARKAAPL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1925 VEEEIRILKLNFeKASSGKLDLELELNKLkniADETQQSKIRAEEEAEKLRKLALeeEKRRREAEEKVKKIAAAEEEAAR 2004
Cdd:TIGR00618 296 AAHIKAVTQIEQ-QAQRIHTELQSKMRSR---AKLLMKRAAHVKQQSSIEEQRRL--LQTLHSQEIHIRDAHEVATSIRE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2005 QRKAALEELERLRKKAEEarKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAK 2084
Cdd:TIGR00618 370 ISCQQHTLTQHIHTLQQQ--KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2085 EAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHK 2164
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLT 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2165 KLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELlklknkieeen 2244
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL----------- 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2245 qrlikkdkdstQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKML-KEKMQAIQEASRLKAEAE 2323
Cdd:TIGR00618 597 -----------QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTaLHALQLTLTQERVREHAL 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2324 MLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKrQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQA 2403
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRE-LETHIEEYDREFNEIENASSSLGSDLAAREDALNQS 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2404 DKVATRLHETEIATQEkmtvverLEFERLNTSKEADDLRKA-IADLENEKARLKKEAEELQNKSKEMADAQQKKIEH--- 2479
Cdd:TIGR00618 745 LKELMHQARTVLKART-------EAHFNNNEEVTAALQTGAeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSded 817
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2480 EKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 2539
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1495-1754 |
2.48e-12 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 71.80 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1495 QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKA-LEDLEKL--RMQAEEAERQVKQAEIEKEKQIKVAHEA 1571
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAeQARQKELeqRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1572 AQKSAaaelqskhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRlRLQAE 1651
Cdd:TIGR02794 125 KAKQA-----------AEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEA-KAKAE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1652 DEAHKKtlaqeeaekqkeeaeREAKKRAKAEESALKQKE-MAEEELERQRKIAESTAQQKLTAEQELirlradfdNAEQQ 1730
Cdd:TIGR02794 193 EAKAKA---------------EAAKAKAAAEAAAKAEAEaAAAAAAEAERKADEAELGDIFGLASGS--------NAEKQ 249
|
250 260
....*....|....*....|....
gi 1988774682 1731 RSLLEDELYRLKNEVAAAQQQRKQ 1754
Cdd:TIGR02794 250 GGARGAAAGSEVDKYAAIIQQAIQ 273
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1344-1883 |
2.59e-12 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 73.24 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1344 RRLDDEEKAAEKLK---AEERKKMAEMQAELDK-QKQLAEAHAKAiaKAEKEAQELKLKMQEEVSK----REIAAVDAEK 1415
Cdd:pfam05557 27 RARIELEKKASALKrqlDRESDRNQELQKRIRLlEKREAEAEEAL--REQAELNRLKKKYLEALNKklneKESQLADARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1416 QKTNIQLELQELKnlseQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKL-RKLA 1494
Cdd:pfam05557 105 VISCLKNELSELR----RQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELeFEIQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1495 Q--DEAEKLRKQVSE-------ETQKKRQAEE-----ELKRKSEAEKEAAKQKQKALEDLEKlrMQAEEAERQVKQAEIE 1560
Cdd:pfam05557 181 SqeQDSEIVKNSKSElaripelEKELERLREHnkhlnENIENKLLLKEEVEDLKRKLEREEK--YREEAATLELEKEKLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1561 KEKQ--IKVAHEA--------AQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAE 1630
Cdd:pfam05557 259 QELQswVKLAQDTglnlrspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1631 KELEKWRQKAnealrLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTA--- 1707
Cdd:pfam05557 339 ALVRRLQRRV-----LLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELggy 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1708 -QQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQlktkaeketMSNTEK 1786
Cdd:pfam05557 414 kQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQG---------DYDPKK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1787 SK--QLLEAEAAKMKD-LAEEASRLRaiseeakhqrqiAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEA 1863
Cdd:pfam05557 485 TKvlHLSMNPAAEAYQqRKNQLEKLQ------------AEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKEL 552
|
570 580
....*....|....*....|
gi 1988774682 1864 ENERLRRQAEDEAYQRKALE 1883
Cdd:pfam05557 553 ESAELKNQRLKEVFQAKIQE 572
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4309-4347 |
2.65e-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: 2.65e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1988774682 4309 LLEAQACTGGIIDPTSGEKYSIAEATEKGLVDKIMVDRL 4347
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1483-1697 |
3.58e-12 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 71.76 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1483 RAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKaledleklrmQAEEAERQVKQAEIEKE 1562
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK----------QAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1563 KQIKVAHEAAQKSAAAElqskHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDA-ENSREEAEKELEKWRQKan 1641
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAE----AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAaAKAAAEAKKKAEAEAKK-- 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774682 1642 ealrlrlQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELE 1697
Cdd:PRK09510 210 -------KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1378-1632 |
5.51e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 70.95 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1378 AEAHAKAIAKAEKEAQELKLKMQEEVSKREiaavDAEKQKTNIQLELQELknlsEQQIKDKSQQVDEalhsrtkIEEEIR 1457
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAAL----ERRIAALARRIRA-------LEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1458 LIRIQLETTEKQKYTAESELKQLRDRAAE-AEKLRKLAQDEAEKLRKQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKA 1536
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1537 LEDLEKLRmqaeeaerqvkqAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLK 1616
Cdd:COG4942 159 LAELAALR------------AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*.
gi 1988774682 1617 KQQEDAENSREEAEKE 1632
Cdd:COG4942 227 ALIARLEAEAAAAAER 242
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2730-2767 |
5.73e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.73 E-value: 5.73e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1988774682 2730 LLEAQAATGYMLDPIKNQKLSVNAAVKEGLIGPELHNK 2767
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1824-2461 |
6.02e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 72.45 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1824 EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAL--EDQASQHKQEI--EEKIVQ 1899
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikENNATRHLCNLlkETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1900 LKKSSEAEMERQKAI-----VDDTLKQRRVVEEEIRIlklnfeKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKL 1974
Cdd:pfam05483 168 AEKTKKYEYEREETRqvymdLNNNIEKMILAFEELRV------QAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1975 RKLALEEEKRRREAEEKVKKIAAAEeeaaRQRKAALEELERLR-KKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQ 2053
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEES----RDKANQLEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2054 QVQ---SVLAQQIEDSITQkkLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAER 2130
Cdd:pfam05483 318 DLQiatKTICQLTEEKEAQ--MEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2131 L-----RKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTL-----------------------------KQKFQ 2176
Cdd:pfam05483 396 MtkfknNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqarekeihdleiqltaiktseehylKEVED 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2177 VEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLiKKDKDSTQ 2256
Cdd:pfam05483 476 LKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNL-RDELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2257 KLLAEEAENMR----KLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLA 2332
Cdd:pfam05483 555 EEFIQKGDEVKckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2333 QEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEE-----------AKKFKK 2401
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiaemvalMEKHKH 714
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774682 2402 QADKVA----TRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEE 2461
Cdd:pfam05483 715 QYDKIIeerdSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2154-2685 |
7.61e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.26 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2154 QQADTEMAKHKKLAEQTlkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQmeEL 2233
Cdd:COG4913 265 AAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD--RL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2234 LKLKNKIEEENQRLIKKDKDSTQklLAEEAENMR-KLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAI 2312
Cdd:COG4913 341 EQLEREIERLERELEERERRRAR--LEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2313 QEASRLKAEAEMLQKQK---DLAQEQAQKLLEDK------------QLMQQRLEEEteEYHKSLE-----------VERK 2366
Cdd:COG4913 419 RELRELEAEIASLERRKsniPARLLALRDALAEAlgldeaelpfvgELIEVRPEEE--RWRGAIErvlggfaltllVPPE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2367 RQLEIMA--EAERLRLQVSQLSEAQARAEEEAKKFKKQ--ADKVATRLH------ETEIATQEKMTVVERLE-FERLN-- 2433
Cdd:COG4913 497 HYAAALRwvNRLHLRGRLVYERVRTGLPDPERPRLDPDslAGKLDFKPHpfrawlEAELGRRFDYVCVDSPEeLRRHPra 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2434 -----------TSKEADDL-------------RKAIADLENEKARLKKEAEELQNKSKEMADAQQ--KKIEHEKTVLQQT 2487
Cdd:COG4913 577 itragqvkgngTRHEKDDRrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEY 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2488 FMTEKEMLLKKEKL--IEDEKKRLES------QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEM 2559
Cdd:COG4913 657 SWDEIDVASAEREIaeLEAELERLDAssddlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2560 LRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKVlhkdiihlTTIETTKTVYNGQNVGDVVDGI 2639
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAE--------EELERAMRAFNREWPAETADLD 808
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1988774682 2640 DKKPDPLAFDGIRDKVPASRLHELgvlpKKEFDKLKNgETTVQELG 2685
Cdd:COG4913 809 ADLESLPEYLALLDRLEEDGLPEY----EERFKELLN-ENSIEFVA 849
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
163-262 |
9.75e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 64.28 E-value: 9.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 163 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN---LENLEQAFSVAEK-DLGVTRLL 238
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1988774682 239 DPEDVdVPHPDEKSIITYVSSLYD 262
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2806-2843 |
1.57e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.57e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1988774682 2806 VLEAQLATGGIIDPINSHRVPTETAYKQGHYDAEMNKI 2843
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
41-140 |
1.66e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 63.98 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 41 ERDRvQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLE-VLSGE-------TLPREKGRMRFHKLQNVQIALDFL 112
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1988774682 113 RHRQVKLVNIRNDDIADGNPKLTLGLIW 140
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3798-3835 |
1.66e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.66e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1988774682 3798 LEAQTATGGIIDPEFQFHLPTDVAMQRGYINKETNEKL 3835
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
163-263 |
1.82e-11 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 63.53 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 163 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 242
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1988774682 243 VdVPHPDEKSIITYVSSLYDA 263
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2187-2600 |
1.98e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.84 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2187 KLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEE--------ENQRLIKKDKDSTQKL 2258
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDlretiaetEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2259 LAEEAENMRKLAEDAARLSVEAQEAARLRQiaeDDLNQQRALAEKMLKEKMQAIQEAsrlKAEAEMLQKQKDLAQEQAQK 2338
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEAVEARR---EELEDRDEELRDRLEECRVAAQAH---NEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2339 LLEDKQlmqqRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQ 2418
Cdd:PRK02224 361 LREEAA----ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2419 EKMTVVERLEfERLNTSK---------------EADDLRKAIADLENEKARLKKEAEELQNKSKEMADAqqKKIEHEKTV 2483
Cdd:PRK02224 437 TARERVEEAE-ALLEAGKcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL--VEAEDRIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2484 LQQTFMTEKEMLLKKEKLIEDEKKRLESQFEE--------EVKKAKALKDEQERQKQQ-----MEQEKKTLQATMDA--- 2547
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERaaeleaeaEEKREAAAEAEEEAEEAReevaeLNSKLAELKERIESler 593
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 2548 ---ALSKQKEAEEEMLR---KQKEMQELERQRLEQ-----ERI--LAEEN-----QKLREKLQQLEDAQKD 2600
Cdd:PRK02224 594 irtLLAAIADAEDEIERlreKREALAELNDERRERlaekrERKreLEAEFdeariEEAREDKERAEEYLEQ 664
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1588-2033 |
2.07e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.84 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1588 AEKTSK-LEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLR-----LQ---AEDEAHKKT 1658
Cdd:PRK02224 197 EEKEEKdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEaeiedLRetiAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1659 LAQEEAEKQKEEAEREAKKRAKAEESAL----------------KQKEMAEEELERQR-----------------KIAES 1705
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLddadaeavearreeleDRDEELRDRLEECRvaaqahneeaeslredaDDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1706 TAQQKL----TAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQ--LKTKAEKE 1779
Cdd:PRK02224 357 RAEELReeaaELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREreAELEATLR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1780 TMSNT-EKSKQLLEA--------------EAAKMKDLAEEASRLRAISEEAKHQRQIAEE--EAARQRAEAERILKEKLA 1842
Cdd:PRK02224 437 TARERvEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEErlERAEDLVEAEDRIERLEE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1843 AISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLkksseAEMERQKAIVDDTLKQR 1922
Cdd:PRK02224 517 RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV-----AELNSKLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1923 RVVEEEirilklnFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLAleeekrrreaeekvKKIAAAEEEA 2002
Cdd:PRK02224 592 ERIRTL-------LAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELE--------------AEFDEARIEE 650
|
490 500 510
....*....|....*....|....*....|..
gi 1988774682 2003 ARQRKAALEE-LERLRKKAEEARKQKDEADKE 2033
Cdd:PRK02224 651 AREDKERAEEyLEQVEEKLDELREERDDLQAE 682
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1696-2577 |
2.09e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 70.85 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1696 LERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRslleDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTK 1775
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIR----DQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1776 AEK--ETMSNTEKSKQLLEAEAAKMKDLAEEAsrLRAISEEAK---HQRQIAEEEAARQRAEAERILKEKLAAISEATRL 1850
Cdd:TIGR00606 264 IMKldNEIKALKSRKKQMEKDNSELELKMEKV--FQGTDEQLNdlyHNHQRTVREKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1851 KTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQAS----QHKQEIEEKIVQLKKSSEAEMERQKAIV---------DD 1917
Cdd:TIGR00606 342 KTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfERGPFSERQIKNFHTLVIERQEDEAKTAaqlcadlqsKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1918 TLKQRRVVEEEIRILKLNfEKASSGKLDLELELNKLKNIADETQQ---SKIRAEEEAEKLRKLALEEEKRRREAEEKVKK 1994
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLG-RTIELKKEILEKKQEELKFVIKELQQlegSSDRILELDQELRKAERELSKAEKNSLTETLK 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1995 iaaaeeeaARQRKAALEELERLRKKAEEARKQKD-EADKEAEKQIvvaQQAAQKCSAAEQQVQSVLAQQIEDSITQ---- 2069
Cdd:TIGR00606 501 --------KEVKSLQNEKADLDRKLRKLDQEMEQlNHHTTTRTQM---EMLTKDKMDKDEQIRKIKSRHSDELTSLlgyf 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2070 ----------KKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQE---DAERLRKEAE 2136
Cdd:TIGR00606 570 pnkkqledwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDeesDLERLKEEIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2137 FEAAKRAQAEAAALMQKQQAdTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDET-----DKQKSvLDEELQRLKDEVDD 2211
Cdd:TIGR00606 650 KSSKQRAMLAGATAVYSQFI-TQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKlrlapDKLKS-TESELKKKEKRRDE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2212 AVkqrGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKD-STQKLLAEEAENMRKLAEDA-------ARLSVEAQEA 2283
Cdd:TIGR00606 728 ML---GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDiEEQETLLGTIMPEEESAKVCltdvtimERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2284 AR--LRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLledkqlmQQRLEE-ETEEYHKS 2360
Cdd:TIGR00606 805 ERkiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL-------KSKTNElKSEKLQIG 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2361 LEVERKRQLE-----IMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERlefERLNTS 2435
Cdd:TIGR00606 878 TNLQRRQQFEeqlveLSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE---KVKNIH 954
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2436 KEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEK--EMLLKKE---KLIEDEKKRLE 2510
Cdd:TIGR00606 955 GYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKiqERWLQDNltlRKRENELKEVE 1034
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2511 ---SQFEEEVKKAKALKDEQERQKqqMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQE 2577
Cdd:TIGR00606 1035 eelKQHLKEMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1345-1870 |
2.27e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1345 RLDDEEKAAEKLKaEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqEEVSKREIAAVDAEKQKTNIQLEL 1424
Cdd:PRK03918 156 GLDDYENAYKNLG-EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVL----REINEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1425 QELKNLSEQqIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKqkytaesELKQLRDRAAEAEKLRKLAqDEAEKLRKQ 1504
Cdd:PRK03918 231 KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKK-------EIEELEEKVKELKELKEKA-EEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1505 VSEETQKKRQAEEELKRKSEAEKEAakqkQKALEDLEKLRMQAEEAERQVKqaEIEKEKqikvaheaaqksaaAELQSKH 1584
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGI----EERIKELEEKEERLEELKKKLK--ELEKRL--------------EELEERH 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1585 MSFAEKTSKLE--ESLKQEHGAvlqlqQEAERLKKQQEDAENSREEAEKELEKWRQK----ANEALRLRLQAE------- 1651
Cdd:PRK03918 362 ELYEEAKAKKEelERLKKRLTG-----LTPEKLEKELEELEKAKEEIEEEISKITARigelKKEIKELKKAIEelkkakg 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1652 ---------DEAHKKTLAQ---------EEAEKQKEEAEREAKKRAKAEESAL-------KQKEMAE------------- 1693
Cdd:PRK03918 437 kcpvcgrelTEEHRKELLEeytaelkriEKELKEIEEKERKLRKELRELEKVLkkeseliKLKELAEqlkeleeklkkyn 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1694 -EELERQRKIAESTAQQKLTAEQELIRLRADF-----------------DNAEQQRSLLEDELY---------------- 1739
Cdd:PRK03918 517 lEELEKKAEEYEKLKEKLIKLKGEIKSLKKELekleelkkklaelekklDELEEELAELLKELEelgfesveeleerlke 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1740 ---------RLKN---EVAAAQQQRKQLEDELAKVRSEMDiliQLKTKAEKETMSNTEKSKQLLEAEAAKMKD----LAE 1803
Cdd:PRK03918 597 lepfyneylELKDaekELEREEKELKKLEEELDKAFEELA---ETEKRLEELRKELEELEKKYSEEEYEELREeyleLSR 673
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774682 1804 EASRLRAISEEAKHQRQIAEEEAarqraeaeRILKEKLAAISEATRLKTEAEIALKEKEAENERLRR 1870
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTL--------EKLKEELEEREKAKKELEKLEKALERVEELREKVKK 732
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2199-2573 |
5.31e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.33 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2199 DEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKiEEENQRLIKKDKDSTQKLLAEEAENMRKLAE--DAARL 2276
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKEKREYEGYELLKEKEALERQKEaiERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2277 SVEAQEAARLRQIaeDDLNQQRALAEKMLKEKMQAIQEasrlKAEAEMLQKQKDLA-----QEQAQKLLEDKQLMQQRLE 2351
Cdd:TIGR02169 248 SLEEELEKLTEEI--SELEKRLEEIEQLLEELNKKIKD----LGEEEQLRVKEKIGeleaeIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2352 EETEEYhkslEVERKRQLEimaEAERLRLQVSQLseaqaraeeeakkfKKQADKVATRLHETEiatQEKMTVVERLEFEr 2431
Cdd:TIGR02169 322 ERLAKL----EAEIDKLLA---EIEELEREIEEE--------------RKRRDKLTEEYAELK---EELEDLRAELEEV- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2432 lntSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEhektvlqqtfmtEKEMLLKKEKLIEDEKKRLES 2511
Cdd:TIGR02169 377 ---DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE------------ELADLNAAIAGIEAKINELEE 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 2512 QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMdaalSKQKEAEEEMLRKQKEMQELERQR 2573
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK----EEYDRVEKELSKLQRELAEAEAQA 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2444-2608 |
5.63e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2444 AIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLEsQFEEEVKKAKAL 2523
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEE-LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2524 KDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHT 2603
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
....*
gi 1988774682 2604 RETDK 2608
Cdd:COG1196 391 ALRAA 395
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3133-3171 |
5.91e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.03 E-value: 5.91e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1988774682 3133 LLDAQMTTGGIIDPVKSHRIPHDVACKRNYFDDEMKQAL 3171
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1692-1913 |
5.95e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 67.93 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1692 AEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQ 1771
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1772 lktkAEKETMSNTEKSKQLLEAEaakmkDLAEEASRLRAISEEAKHQRQI------AEEEAARQRAEAERILKEKLAAIS 1845
Cdd:COG3883 94 ----ALYRSGGSVSYLDVLLGSE-----SFSDFLDRLSALSKIADADADLleelkaDKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774682 1846 EATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKA 1913
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3464-3502 |
6.03e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.03 E-value: 6.03e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1988774682 3464 LLEAQIVSGGIIDPVKSHRVPTDVAYQKNILSRDIAKTL 3502
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1513-1916 |
6.37e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.21 E-value: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1513 RQAEEE---LKRKSEAEKE-AAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAeLQSKHMSFA 1588
Cdd:COG3096 275 RHANERrelSERALELRRElFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1589 EKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWrQKANEALRLR-------LQAEDEAhkKTLAQ 1661
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADY-QQALDVQQTRaiqyqqaVQALEKA--RALCG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1662 EEAEKQKEEAEREAKKRAKAEES-----ALKQK----EMA----EEELERQRKIA-ESTAQQKLTAEQELIRLRADFDNA 1727
Cdd:COG3096 431 LPDLTPENAEDYLAAFRAKEQQAteevlELEQKlsvaDAArrqfEKAYELVCKIAgEVERSQAWQTARELLRRYRSQQAL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1728 EQQRSLLEDELYRLKNEVAAAQQQRKQLEdELAKvrsemdiliqlktKAEKETMSNTEKSKQLLEAEAaKMKDLAEEASR 1807
Cdd:COG3096 511 AQRLQQLRAQLAELEQRLRQQQNAERLLE-EFCQ-------------RIGQQLDAAEELEELLAELEA-QLEELEEQAAE 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1808 LRAISEEAKHQRqiaeEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAyQRKALEDQAS 1887
Cdd:COG3096 576 AVEQRSELRQQL----EQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERER-EATVERDELA 650
|
410 420
....*....|....*....|....*....
gi 1988774682 1888 QHKQEIEEKIVQLKKSSEAEMERQKAIVD 1916
Cdd:COG3096 651 ARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1125-1618 |
7.20e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1125 KEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQREL 1204
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1205 EQLGRQLGYYRESY-DWLIRWIADAKQRQEKIQAvpitdsktLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKD 1283
Cdd:COG1196 361 AEAEEALLEAEAELaEAEEELEELAEELLEALRA--------AAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1284 YELQLVAYKAQVEplvsplkktKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKK 1363
Cdd:COG1196 433 LEEEEEEEEEALE---------EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1364 MAEMQAELDKQKQLA---------------EAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQ--KTNIQLELQE 1426
Cdd:COG1196 504 EGFLEGVKAALLLAGlrglagavavligveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgrATFLPLDKIR 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1427 LKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEK-----QKYTAESELKQLRDRAAEAEKLRKLAQDEAEKL 1501
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRtlvaaRLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1502 RKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQ 1581
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
490 500 510
....*....|....*....|....*....|....*..
gi 1988774682 1582 SKHMSFAEKTSKLEESLKQEhgavlQLQQEAERLKKQ 1618
Cdd:COG1196 744 EEELLEEEALEELPEPPDLE-----ELERELERLERE 775
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2174-2599 |
8.16e-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: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2174 KFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEE-LFKVKVQMEELLKLKNKIEEENQR---LIK 2249
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERlkaLTG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2250 KDKDSTQKLLAEEA----ENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQ-RALAEKMLKEKMQAIQEASRLKAEAEM 2324
Cdd:pfam12128 369 KHQDVTAKYNRRRSkikeQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeSELREQLEAGKLEFNEEEYRLKSRLGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2325 LQKQKDLAQeqaqklLEDKQLMQQRLEEEteeyhkslEVERKRQLEIMAEAERLRLQvsqlseaqaraeEEAKKFKKQAD 2404
Cdd:pfam12128 449 LKLRLNQAT------ATPELLLQLENFDE--------RIERAREEQEAANAEVERLQ------------SELRQARKRRD 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2405 KVATRLHETEIATQEKMTVVERLEFERLNTSKEADD-LRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHE--- 2480
Cdd:pfam12128 503 QASEALRQASRRLEERQSALDELELQLFPQAGTLLHfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNlyg 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2481 -KTVLQQTFMTEKEMLlkkekliEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEM 2559
Cdd:pfam12128 583 vKLDLKRIDVPEWAAS-------EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDL 655
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1988774682 2560 LRKQKEMQELERQRleqERILAEENQKLREKLQQLEDAQK 2599
Cdd:pfam12128 656 RRLFDEKQSEKDKK---NKALAERKDSANERLNSLEAQLK 692
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1473-1710 |
9.34e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.10 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1473 AESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVseetqkkRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAER 1552
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1553 QVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKE 1632
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1633 LEKWRQ--KANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 1710
Cdd:COG4942 173 RAELEAllAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1521-1934 |
9.39e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 9.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1521 RKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQ 1600
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1601 EHGAVLQLQQEAERLKKQQEDaensREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAK 1680
Cdd:COG4717 144 LPERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1681 AE----ESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQR---------SLLEDELYRLKNEVAA 1747
Cdd:COG4717 220 EEleelEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1748 AQQQRKQLEDELAKVRSEMDILIQLKtkaeKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAE---- 1823
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELL----AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaal 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1824 --------EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAEN--ERLRRQAEDEAYQRKALEDQASQHKQEI 1893
Cdd:COG4717 376 laeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1988774682 1894 EEKIVQLKK-SSEAEMERQKAIVDDTLKQRRVVEEEIRILKL 1934
Cdd:COG4717 456 AELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
163-258 |
1.01e-10 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 61.63 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 163 KEKLLLWSQRMtdgYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLI-NMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPE 241
Cdd:cd21229 5 KKLMLAWLQAV---LPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1988774682 242 DVDVPHPDEKSIITYVS 258
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1353-1813 |
1.09e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 68.70 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1353 AEKLKAEERKKMAEMQAEldKQKQLAEAHAKA---IAKAEKEAQE-------LKLKMQEEVSK-REIAAVDAEKQKTNIQ 1421
Cdd:NF041483 737 SEELLASARKRVEEAQAE--AQRLVEEADRRAtelVSAAEQTAQQvrdsvagLQEQAEEEIAGlRSAAEHAAERTRTEAQ 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1422 LELQELKNlseqqikDKSQQVDEALHSRTKIEEEIRliriqlETTEKQKYTAEselKQLRDRAAEAEKLRKLAQDEAEKL 1501
Cdd:NF041483 815 EEADRVRS-------DAYAERERASEDANRLRREAQ------EETEAAKALAE---RTVSEAIAEAERLRSDASEYAQRV 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1502 RKQVSEetqkkrqaeeelkRKSEAEKEAAKQKQKALEDLEKLRMQA------------EEAERQVKQAEIEKEKQIKVAH 1569
Cdd:NF041483 879 RTEASD-------------TLASAEQDAARTRADAREDANRIRSDAaaqadrligeatSEAERLTAEARAEAERLRDEAR 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1570 EAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKqqeDAENSREEAEKELEKWRQKA-NEALRLRL 1648
Cdd:NF041483 946 AEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRT---EAERVKAEAAAEAERLRTEArEEADRTLD 1022
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1649 QAEDEAHKK-TLAQEEAEKQKEEAEREAKK-RAKAEESALKQKEMAEEEL---------ERQRKIAESTAQ--------- 1708
Cdd:NF041483 1023 EARKDANKRrSEAAEQADTLITEAAAEADQlTAKAQEEALRTTTEAEAQAdtmvgaarkEAERIVAEATVEgnslvekar 1102
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1709 -------------------------QKLTAEQELIRLRADFDNAEQQRSLLEdelyRLKNEVAAAQQQRKQLE------- 1756
Cdd:NF041483 1103 tdadellvgarrdataireraeelrDRITGEIEELHERARRESAEQMKSAGE----RCDALVKAAEEQLAEAEakakelv 1178
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1757 ----DELAKVR----SEMDILI---------------QLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISE 1813
Cdd:NF041483 1179 sdanSEASKVRiaavKKAEGLLkeaeqkkaelvreaeKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAEISRVQDVLE 1258
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3959-3997 |
1.14e-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: 1.14e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1988774682 3959 LLESQAATGYVIDPIKNLKLTVNEAVKMGIVGPEFKDKL 3997
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4307-4344 |
1.18e-10 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 59.03 E-value: 1.18e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1988774682 4307 QRLLEAQACTGGIIDPTSGEKYSIAEATEKGLVDKIMV 4344
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1349-1582 |
1.70e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 66.37 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1349 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEahakaiakaekeAQELKlkmqeevskreiaavdaekqktniQLELQELK 1428
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAE------------QERLK------------------------QLEKERLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1429 nlSEQQIKDKSQQVDEALHSRTKIEEEirliriQLETTEKQKYTAESELKQLRDRAAEAE-KLRKLAQDEAEklrKQVSE 1507
Cdd:PRK09510 113 --AQEQKKQAEEAAKQAALKQKQAEEA------AAKAAAAAKAKAEAEAKRAAAAAKKAAaEAKKKAEAEAA---KKAAA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 1508 ETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQS 1582
Cdd:PRK09510 182 EAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1343-1564 |
1.77e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 67.46 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1343 QRRLDDEEKAAEKLKAEERKK------MAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL----KLKMQEEVSKREIAAVD 1412
Cdd:pfam17380 340 ERMAMERERELERIRQEERKRelerirQEEIAMEISRMRELERLQMERQQKNERVRQELeaarKVKILEEERQRKIQQQK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1413 AEKQKTNIQLE---LQELKNLSEQQIKDKSQQVDEALHSRTKIE------EEIRLIRIQLETTEKQKYTAESELKQLRDR 1483
Cdd:pfam17380 420 VEMEQIRAEQEearQREVRRLEEERAREMERVRLEEQERQQQVErlrqqeEERKRKKLELEKEKRDRKRAEEQRRKILEK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1484 AAEAeklRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQ------------KALEdlEKLRMQAEEAE 1551
Cdd:pfam17380 500 ELEE---RKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEmeerrriqeqmrKATE--ERSRLEAMERE 574
|
250
....*....|...
gi 1988774682 1552 RQVKQAEIEKEKQ 1564
Cdd:pfam17380 575 REMMRQIVESEKA 587
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1834-2601 |
2.00e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.45 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1834 ERILKEKLAAISEATRLKTEAEiALKEKEAENER-----LRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEaEM 1908
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLNESN-ELHEKQKFYLRqsvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH-EL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1909 ERQKAIVDDTLKQ--------RRV------VEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAE-- 1972
Cdd:pfam15921 155 EAAKCLKEDMLEDsntqieqlRKMmlshegVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEis 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1973 --KLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALE---ELERLRKKAEEARKQKDEADKEAEkqiVVAQQAAQK 2047
Cdd:pfam15921 235 ylKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEhevEITGLTEKASSARSQANSIQSQLE---IIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2048 CSAAEQQVQsvlaqQIEDSITQkkLKEEYEKAKKlakeaeaakekaereaaLLRQQAEEAERQKTAAeeeaanqakaqeD 2127
Cdd:pfam15921 312 NSMYMRQLS-----DLESTVSQ--LRSELREAKR-----------------MYEDKIEELEKQLVLA------------N 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2128 AERLRKEAEFEAAKRAQAEAAALMQKQQADTemakHKKLAEQTLkqkfqvEQELTKvklKLDETDKQKSVLDEELQRlkd 2207
Cdd:pfam15921 356 SELTEARTERDQFSQESGNLDDQLQKLLADL----HKREKELSL------EKEQNK---RLWDRDTGNSITIDHLRR--- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2208 EVDDAVKQRGQVEEELFKVKV----QMEELLKlknKIEEENQRLIKKDKDSTQklLAEEAENMRKLAED--AARLSVEAQ 2281
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSecqgQMERQMA---AIQGKNESLEKVSSLTAQ--LESTKEMLRKVVEEltAKKMTLESS 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2282 EaarlRQIAedDLNQQralaekmLKEKMQAIQEASrlkAEAEMLQKQKDLAQEQAQKL------LEDKQLMQQRLEEETE 2355
Cdd:pfam15921 495 E----RTVS--DLTAS-------LQEKERAIEATN---AEITKLRSRVDLKLQELQHLknegdhLRNVQTECEALKLQMA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2356 EYHKSLEVERKrQLEIMAE--------AERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQ----EKMTV 2423
Cdd:pfam15921 559 EKDKVIEILRQ-QIENMTQlvgqhgrtAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSdlelEKVKL 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2424 V----ERLEFERlNTSKEADDLRKAIADLENEKARLKKEAEELQ----NKSKEMADAQQK---KIEHEKTVLQQTFMTEK 2492
Cdd:pfam15921 638 VnagsERLRAVK-DIKQERDQLLNEVKTSRNELNSLSEDYEVLKrnfrNKSEEMETTTNKlkmQLKSAQSELEQTRNTLK 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2493 EM----------LLKKEKLIEDEKKRLES-----QFEEEV-----KKAKALKDEQERQKQQME---QEKKTLQATMDAAL 2549
Cdd:pfam15921 717 SMegsdghamkvAMGMQKQITAKRGQIDAlqskiQFLEEAmtnanKEKHFLKEEKNKLSQELStvaTEKNKMAGELEVLR 796
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 2550 SKQKEAEEEMLRKQKEMQELERQRLE-QERILAEENQKLREKLQQLEDAQKDQ 2601
Cdd:pfam15921 797 SQERRLKEKVANMEVALDKASLQFAEcQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2334-2624 |
2.05e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2334 EQAQKLLEDKQLMQQRLE---EETEEYHKSLEVERK---RQLEIMAEAERLRLQVSQLSEAQARAEEeaKKFKKQADKVA 2407
Cdd:TIGR02168 175 KETERKLERTRENLDRLEdilNELERQLKSLERQAEkaeRYKELKAELRELELALLVLRLEELREEL--EELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2408 TRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKA-------IADLENEKARLKKEAEELQNKSKEMADAQQKKIEHe 2480
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESK- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2481 ktvlqqtfmteKEMLLKKEKLIEDEKKRLESQFEEEVKKAKalkdEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEML 2560
Cdd:TIGR02168 332 -----------LDELAEELAELEEKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774682 2561 RKQKEMQELERQ--RLEQER-ILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDIIHLTTIETTK 2624
Cdd:TIGR02168 397 SLNNEIERLEARleRLEDRReRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
524-713 |
2.14e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 63.62 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 524 LRYVQDLLAWVEENQRRIDNAEWGSDLPSMESQLGSHRGLHQTVEDFKSKIERAKADETQL---SPVSKGTYREYLGKLD 600
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 601 LQYGKLLNSSKSRLRNLE---SLHAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDI 677
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1988774682 678 QALGDRLVRDGHPGK-KTVESFTAALQTQWSWILQLC 713
Cdd:cd00176 166 NELAEELLEEGHPDAdEEIEEKLEELNERWEELLELA 202
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
47-146 |
2.24e-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: 61.06 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 47 KKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLP----REKGRMRFHKLQNVQIALDFLRHRQVKLVNI 122
Cdd:cd21222 18 KELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELMEDAGISTPKI 97
|
90 100
....*....|....*....|....
gi 1988774682 123 RNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21222 98 RPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1432-1631 |
2.39e-10 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 65.64 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1432 EQQIKDKSQQVDEAlhsRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKlaqdeAEKLRKQVSEetqk 1511
Cdd:TIGR02794 49 AQQANRIQQQKKPA---AKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEE---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1512 KRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAElqskhmsfAEKT 1591
Cdd:TIGR02794 117 KQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAE--------AEAK 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1988774682 1592 SKLEESLKQEHGAVLQLQQEAERlKKQQEDAENSREEAEK 1631
Cdd:TIGR02794 189 AKAEEAKAKAEAAKAKAAAEAAA-KAEAEAAAAAAAEAER 227
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1763-2484 |
3.22e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 66.79 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1763 RSEMDILIQLKTKAEKETMSNTEKSKQLL---EAEAAKMKDLAEEAS-------RLRAISEEAK-HQRQIAEEEAARQRA 1831
Cdd:pfam12128 205 ILEDDGVVPPKSRLNRQQVEHWIRDIQAIagiMKIRPEFTKLQQEFNtlesaelRLSHLHFGYKsDETLIASRQEERQET 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1832 EAEriLKEKLAA--------ISEATRLKTEAEIALKEKEAENERLRRQA----EDEAYQRKALEDQASQHKQEIEEKIVQ 1899
Cdd:pfam12128 285 SAE--LNQLLRTlddqwkekRDELNGELSAADAAVAKDRSELEALEDQHgaflDADIETAAADQEQLPSWQSELENLEER 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1900 LK------KSSEAEMERQKAIVDDTLKqrRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEK 1973
Cdd:pfam12128 363 LKaltgkhQDVTAKYNRRRSKIKEQNN--RDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEY 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1974 LRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKqivvAQQAAQKCSAAEQ 2053
Cdd:pfam12128 441 RLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ----ASEALRQASRRLE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2054 QVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEaakekaereaalLRQQAEEAERQKTAAEEEAANQAKAQE------- 2126
Cdd:pfam12128 517 ERQSALDELELQLFPQAGTLLHFLRKEAPDWEQS------------IGKVISPELLHRTDLDPEVWDGSVGGElnlygvk 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2127 -DAERLRKEAEFEAAKRAQAEAAALmqKQQADTEMAKHKKLAEQTLKQKFQVEQ---ELTKVKLKLDETDKQKSVLDEEL 2202
Cdd:pfam12128 585 lDLKRIDVPEWAASEEELRERLDKA--EEALQSAREKQAAAEEQLVQANGELEKasrEETFARTALKNARLDLRRLFDEK 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2203 QRLKDEVDDAVKQR-GQVEEELFKVKVQMEELL-KLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAE-DAARLSVE 2279
Cdd:pfam12128 663 QSEKDKKNKALAERkDSANERLNSLEAQLKQLDkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALlKAAIAARR 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2280 AQEAARLRQIAEDdlnQQRALAEKMLKEkmqaiQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHK 2359
Cdd:pfam12128 743 SGAKAELKALETW---YKRDLASLGVDP-----DVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLAT 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2360 SLEverkrqlEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLheteiatQEKMTVVeRLEFERLNTSKEAD 2439
Cdd:pfam12128 815 QLS-------NIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRL-------SENLRGL-RCEMSKLATLKEDA 879
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1988774682 2440 DlrkaIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVL 2484
Cdd:pfam12128 880 N----SEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVI 920
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1514-1917 |
4.44e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1514 QAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVkQAEIEKEKQIKVAHEAA----QKSAAAELQSKHM---- 1585
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMAREL-AELNEAESDLEQDYQAAsdhlNLVQTALRQQEKIeryq 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1586 -SFAEKTSKLEESLkqehgAVLQLQQEaerlkkQQEDAENSREEAEKELEKWR------QKANEALRLR-------LQAE 1651
Cdd:PRK04863 355 aDLEELEERLEEQN-----EVVEEADE------QQEENEARAEAAEEEVDELKsqladyQQALDVQQTRaiqyqqaVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1652 DEAhkKTLAQEEAEKQKEEAEREAKKRAKAEESALkqkemAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQ- 1730
Cdd:PRK04863 424 ERA--KQLCGLPDLTADNAEDWLEEFQAKEQEATE-----ELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWd 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1731 --RSLLED--ELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKeTMSNTEKSKQLLEAEAAKMKDLAEEAS 1806
Cdd:PRK04863 497 vaRELLRRlrEQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGK-NLDDEDELEQLQEELEARLESLSESVS 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1807 RLRAISEEAKHQRqiaeEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAlEDQA 1886
Cdd:PRK04863 576 EARERRMALRQQL----EQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVE-RDEL 650
|
410 420 430
....*....|....*....|....*....|.
gi 1988774682 1887 SQHKQEIEEKIVQLKKSSEAEMERQKAIVDD 1917
Cdd:PRK04863 651 AARKQALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1513-2026 |
5.85e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1513 RQAEEELKRKSEAEKEA--AKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKqikVAHEAAQKsAAAELQskhmsfaek 1590
Cdd:COG4913 228 DALVEHFDDLERAHEALedAREQIELLEPIRELAERYAAARERLAELEYLRAA---LRLWFAQR-RLELLE--------- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1591 tsKLEESLKQEHGavlQLQQEAERLKKQQEDAENSREEAEkelEKWRQKANEALRlRLQAEDEAHKKTLaqeeaekqkee 1670
Cdd:COG4913 295 --AELEELRAELA---RLEAELERLEARLDALREELDELE---AQIRGNGGDRLE-QLEREIERLEREL----------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1671 aeREAKKRAKAEESALKQKEMA----EEELERQRKIAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVA 1746
Cdd:COG4913 355 --EERERRRARLEALLAALGLPlpasAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1747 AAQQQ-----------RKQLEDELAKVRSEMDI---LIQLKTKAEKETMS--------------------------NTEK 1786
Cdd:COG4913 430 SLERRksniparllalRDALAEALGLDEAELPFvgeLIEVRPEEERWRGAiervlggfaltllvppehyaaalrwvNRLH 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1787 SKQLLEAEAAKMKDLAEEASRL-------------------------------------------RAISEE--AKH---- 1817
Cdd:COG4913 510 LRGRLVYERVRTGLPDPERPRLdpdslagkldfkphpfrawleaelgrrfdyvcvdspeelrrhpRAITRAgqVKGngtr 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1818 -----QRQIAEE-----EAARQRAEAERILKEKLAAISEATRLKTEaeiaLKEKEAENERLRRQAEDEAYQRKALEDQAS 1887
Cdd:COG4913 590 hekddRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1888 QHKQ--EIEEKIVQLKKSS------EAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEkassgklDLELELNKLKNIADE 1959
Cdd:COG4913 666 AEREiaELEAELERLDASSddlaalEEQLEELEAELEELEEELDELKGEIGRLEKELE-------QAEEELDELQDRLEA 738
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774682 1960 tqqskirAEEEAEKLRKLALEEEKRRREAEEKVKKIaaaEEEAARQRKAALEELERLRKKAEEARKQ 2026
Cdd:COG4913 739 -------AEDLARLELRALLEERFAAALGDAVEREL---RENLEERIDALRARLNRAEEELERAMRA 795
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1410-1605 |
6.11e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.83 E-value: 6.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1410 AVDAEKQKTNIQL----ELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRiqlettEKQKYTAESELKQLRDRAA 1485
Cdd:PRK09510 74 AKRAEEQRKKKEQqqaeELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAA------LKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1486 EAEKLRKLAQDEAeklrKQVSEETQKKRQAEEELKRKSEAEKEA-AKQKQKALEDLEKlrmqAEEAERQVKQAEIEKEKQ 1564
Cdd:PRK09510 148 KAEAEAKRAAAAA----KKAAAEAKKKAEAEAAKKAAAEAKKKAeAEAAAKAAAEAKK----KAEAEAKKKAAAEAKKKA 219
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1988774682 1565 IKVAHEAAQKsAAAELQSKHMSFAEKTSKLEESLKQEHGAV 1605
Cdd:PRK09510 220 AAEAKAAAAK-AAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1510-1716 |
6.38e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.83 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1510 QKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEE---AERQVKQAE----IEKEKQiKVAHEAAQKSAAAelqs 1582
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKErlaAQEQKKQAEeaakQAALKQ-KQAEEAAAKAAAA---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1583 khmsfaektSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTlaqe 1662
Cdd:PRK09510 145 ---------AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKA---- 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1988774682 1663 eaekqkeeaEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQE 1716
Cdd:PRK09510 212 ---------AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1124-1619 |
7.01e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.91 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1124 VKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVrvhSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRE 1203
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL---TEARTERDQFSQESGNLDDQLQKLLADLHKREKE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1204 --LEQLGRQLGYYRE-----SYDWLIRWIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKA 1276
Cdd:pfam15921 393 lsLEKEQNKRLWDRDtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLES 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1277 YIDTIKDYELQLVAYKAQVEP---LVSPLKKT--KLDSASDNIIQEYVTLRTRYsELMTLTSQYIKFITDTQRRLDDEEK 1351
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLESserTVSDLTASlqEKERAIEATNAEITKLRSRV-DLKLQELQHLKNEGDHLRNVQTECE 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1352 AAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAI-------AKAEKEAQELKLKMQE---EVSKREIAAVDAEKQKTNIQ 1421
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAgamqvekAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARVSDLE 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1422 LELQELKNLSEQQ---IKDKSQQVDEALH----SRTKIE---EEIRLIRI-------QLETT----EKQKYTAESELKQL 1480
Cdd:pfam15921 632 LEKVKLVNAGSERlraVKDIKQERDQLLNevktSRNELNslsEDYEVLKRnfrnkseEMETTtnklKMQLKSAQSELEQT 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1481 RDRAAEAEKLRKLAQDEAEKLRKQVS------EETQKKRQAEEELKRKSEAEKEAAKQKQKALEdlEKLRMQAEEAERQV 1554
Cdd:pfam15921 712 RNTLKSMEGSDGHAMKVAMGMQKQITakrgqiDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS--QELSTVATEKNKMA 789
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 1555 KQAEIEKEKQIKVAHEAAQKSAAaeLQSKHMSFAEKTSKLEeslKQEhgavlqlqQEAERLKKQQ 1619
Cdd:pfam15921 790 GELEVLRSQERRLKEKVANMEVA--LDKASLQFAECQDIIQ---RQE--------QESVRLKLQH 841
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2202-2600 |
8.11e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 8.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2202 LQRLKDEVDDAVKQRGQ-----------VEEELFKVKVQMEELLKLKNKIEEENQRL---------IKKDKDSTQKLLA- 2260
Cdd:COG4717 48 LERLEKEADELFKPQGRkpelnlkelkeLEEELKEAEEKEEEYAELQEELEELEEELeeleaeleeLREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2261 -----EEAENMRKLAEDAARL-SVEAQEAARLRQIAE-DDLNQ-----QRALAEKMLKEKMQAIQEASRLKAEAEMLQKQ 2328
Cdd:COG4717 128 lplyqELEALEAELAELPERLeELEERLEELRELEEElEELEAelaelQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2329 KDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEE-------------- 2394
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvlglla 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2395 --------EAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKS 2466
Cdd:COG4717 288 llflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2467 KEmadaqqkkiEHEKTVLQQTFMTEKEMLLKKEKL------IEDEKKRLESQFEEEVKKAKALKDEQErqKQQMEQEKKT 2540
Cdd:COG4717 368 LE---------QEIAALLAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEELLEALD--EEELEEELEE 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 2541 LQAtmdaalsKQKEAEEEMLRKQKEMQELERQ--RLEQERILAEENQKLREKLQQLEDAQKD 2600
Cdd:COG4717 437 LEE-------ELEELEEELEELREELAELEAEleQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2101-2381 |
8.21e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 65.14 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2101 RQQAEEAERQKTAAEEEAANQAKaqEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKL----AEQTLKQKFQ 2176
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKA--REVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELerirQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2177 VEQELTKVKL-KLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRlikkdkdST 2255
Cdd:pfam17380 365 IRQEEIAMEIsRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR-------EV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2256 QKLLAEEAENMRKLAEDAARlsvEAQEAARLRQIAEDdlNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQ-KQKDLAQE 2334
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQE---RQQQVERLRQQEEE--RKRKKLELEKEKRDRKRAEEQRRKILEKELEErKQAMIEEE 512
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1988774682 2335 QAQKLLEDKQLMQQRLEEETEEYHKSlEVERKRQLEImaeAERLRLQ 2381
Cdd:pfam17380 513 RKRKLLEKEMEERQKAIYEEERRREA-EEERRKQQEM---EERRRIQ 555
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1745-2071 |
8.49e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 65.14 E-value: 8.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1745 VAAAQQQRKQLEDELAKVRSEmdiliqlktkaEKETMSNTEKSKQLLEAEAAKMKDLAEEAS----RLRAISEEAKHQRQ 1820
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQE-----------KEEKAREVERRRKLEEAEKARQAEMDRQAAiyaeQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1821 IAEEEAARqraEAERILKEKLAAisEATRLKtEAEIALKEKEAENERLRRQAEdEAYQRKALEDQASQHKQEIEEKIVQL 1900
Cdd:pfam17380 353 IRQEERKR---ELERIRQEEIAM--EISRMR-ELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1901 KKSSEAEMERQkaivddtlkQRRVVEEEIRilklnfekassgkldlELELNKLKNIADETQQSKIRAEEEAEKLRKLALE 1980
Cdd:pfam17380 426 RAEQEEARQRE---------VRRLEEERAR----------------EMERVRLEEQERQQQVERLRQQEEERKRKKLELE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1981 EEKRRREAEEKV-KKIAAAEEEAARQ------------------RKAALEELERLRKKAEEARKQKD-EADKEAEKQIVV 2040
Cdd:pfam17380 481 KEKRDRKRAEEQrRKILEKELEERKQamieeerkrkllekemeeRQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRK 560
|
330 340 350
....*....|....*....|....*....|.
gi 1988774682 2041 AQQAAQKCSAAEQQVQsvLAQQIEDSITQKK 2071
Cdd:pfam17380 561 ATEERSRLEAMERERE--MMRQIVESEKARA 589
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1432-1634 |
9.92e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.06 E-value: 9.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1432 EQQIKDKSQQVDEALHSRTKIEEEIRLIriqlettEKQKYTAESELKQlrdrAAEAEKLRKLAQDEAEKLRKQVSEETQK 1511
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQL-------EKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1512 KrqAEEELKRKSEAEKEAAKQKQKaLEDLEKLRMQAEEAerqvkQAEIEKEKQIKVAHEAAQKsAAAELQSKHMSFAEKT 1591
Cdd:PRK09510 148 K--AEAEAKRAAAAAKKAAAEAKK-KAEAEAAKKAAAEA-----KKKAEAEAAAKAAAEAKKK-AEAEAKKKAAAEAKKK 218
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1988774682 1592 SKLEESLKQEHGAVlQLQQEAERLKKQQEDAENSREEAEKELE 1634
Cdd:PRK09510 219 AAAEAKAAAAKAAA-EAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1514-1771 |
1.24e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 63.33 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1514 QAEEELKRKSEAEKEAAKQKQKALEDLEKlrmQAEEAERQvKQAEIEKEKQIKVAHEAAQKSAAAELQSKHmsfAEKTSK 1593
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQ---QAEEAEKQ-RAAEQARQKELEQRAAAEKAAKQAEQAAKQ---AEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1594 LEESLKQEHGAVLQLQQEAERLKKQQEDAENsreeaekelekwrqkanealrlrlQAEDEAHKKTLAQEEAEKQKEEAER 1673
Cdd:TIGR02794 120 QAEEAKAKQAAEAKAKAEAEAERKAKEEAAK------------------------QAEEEAKAKAAAEAKKKAEEAKKKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1674 EAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRK 1753
Cdd:TIGR02794 176 EAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGA 255
|
250
....*....|....*...
gi 1988774682 1754 QLEDELAKVRSEMDILIQ 1771
Cdd:TIGR02794 256 AAGSEVDKYAAIIQQAIQ 273
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1363-1704 |
1.39e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 63.01 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1363 KMAEMQAELDKQKqlaeAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLEL--QELKNLSEQQIKDKSQ 1440
Cdd:pfam13868 16 LAAKCNKERDAQI----AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyrQELEEQIEEREQKRQE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1441 QVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELK 1520
Cdd:pfam13868 92 EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1521 RKSEAEKEAAKQKqkaledlEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsfAEKTSKLEESLKQ 1600
Cdd:pfam13868 172 EAEREEIEEEKER-------EIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREE-----AEKKARQRQELQQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1601 EHgavlQLQQEAERLKKQQEdaensREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAK 1680
Cdd:pfam13868 240 AR----EEQIELKERRLAEE-----AEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAER 310
|
330 340 350
....*....|....*....|....*....|.
gi 1988774682 1681 AEESALKQKEMAEEEL-------ERQRKIAE 1704
Cdd:pfam13868 311 EEELEEGERLREEEAErrerieeERQKKLKE 341
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1115-1642 |
1.58e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1115 REVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKasavSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVF 1194
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE----LEERIEELKKEIEELEEKVKELKELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1195 TQIDLRQRELEQLGR---QLGYYRESYDWLIRWIADAKQRQEKIqavpitdsktlkeqlaqeKKLLEEIEQNKDKVDECQ 1271
Cdd:PRK03918 297 KLSEFYEEYLDELREiekRLSRLEEEINGIEERIKELEEKEERL------------------EELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1272 KYAKAYiDTIKDYELQLVAYKAQVEPLvsplkktkldsASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEK 1351
Cdd:PRK03918 359 ERHELY-EEAKAKKEELERLKKRLTGL-----------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1352 AAEKLKAEERK-KMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQE-EVSKREIAAVDAEKQKTNIQLEL-QELK 1428
Cdd:PRK03918 427 AIEELKKAKGKcPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKlRKELRELEKVLKKESELIKLKELaEQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1429 NLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTE---KQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQV 1505
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1506 SEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAER--QVKQAEIEK-EKQIKVAHEAAQKSAAAELQS 1582
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEelAETEKRLEElRKELEELEKKYSEEEYEELRE 666
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1583 KHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKeLEKWRQKANE 1642
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEE 725
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1477-1896 |
1.69e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1477 LKQLRDRAAEAEKLR----KLAQDEAEKLRKQVSEETQKK---RQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEE 1549
Cdd:COG4717 48 LERLEKEADELFKPQgrkpELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1550 AERQVKQAEIEKEKQIK-------VAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQ----EHGAVLQLQQEAERLKKQ 1618
Cdd:COG4717 128 LPLYQELEALEAELAELperleelEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1619 QEDAENSREEAEKELEkwrQKANEALRLRLQAEDEAHKKTLAQEEAEKQ------------------------------- 1667
Cdd:COG4717 208 LAELEEELEEAQEELE---ELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1668 --KEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLED-ELYRLKNE 1744
Cdd:COG4717 285 llALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1745 VAAAQQQRKQLEDElAKVRSEMDILIQLKTKAEKEtmsntEKSKQLLEAEAAkMKDLAEEASRLRAISEEAKHQRQIAEE 1824
Cdd:COG4717 365 LEELEQEIAALLAE-AGVEDEEELRAALEQAEEYQ-----ELKEELEELEEQ-LEELLGELEELLEALDEEELEEELEEL 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 1825 EAARQRAEAERI-LKEKLAAISEATR-LKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQA-SQHKQEIEEK 1896
Cdd:COG4717 438 EEELEELEEELEeLREELAELEAELEqLEEDGELAELLQELEELKAELRELAEEWAALKLALELlEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2165-2384 |
2.01e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2165 KLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELfkvKVQMEELLKLKNKIEEEN 2244
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2245 QRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAAR----LRQIAEDDLNQQRALAEKmLKEKMQAIQEASRLKA 2320
Cdd:COG4942 97 AEL-EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRrlqyLKYLAPARREQAEELRAD-LAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774682 2321 EAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQ 2384
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1315-1771 |
2.38e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.21 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1315 IQEYVTLRTRYSELMTLTSQYIKF----ITDTQRRLDDEEKAAEKLKAEERKKMA-------EMQAELDKQK-------- 1375
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYVAAdymrHANERRVHLEEALELRRELYTSRRQLAaeqyrlvEMARELAELNeaesdleq 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1376 ------------QLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAvdaekqktNIQLELQELKNLSEQQIKD-KSQQV 1442
Cdd:PRK04863 329 dyqaasdhlnlvQTALRQQEKIERYQADLEELEERLEEQNEVVEEAD--------EQQEENEARAEAAEEEVDElKSQLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1443 D--EALhsrtkIEEEIRLIRIQletTEKQKYTAESELKQLRDRAAEAeklrklAQDEAEKLRKQVSEETQKKRQAEEELk 1520
Cdd:PRK04863 401 DyqQAL-----DVQQTRAIQYQ---QAVQALERAKQLCGLPDLTADN------AEDWLEEFQAKEQEATEELLSLEQKL- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1521 rkSEAEkEAAKQKQKALEDLEKL--RMQAEEAERQVKQAEIEKEKQikvAHEAAQKSAaaeLQSKHmsfaektSKLEESL 1598
Cdd:PRK04863 466 --SVAQ-AAHSQFEQAYQLVRKIagEVSRSEAWDVARELLRRLREQ---RHLAEQLQQ---LRMRL-------SELEQRL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1599 KQehgavlqlQQEAERLKKQQEDAENSREEAEKELekwrqkanEALRLRLQAEDEAHKktlaqeeaekqkeeaerEAKKR 1678
Cdd:PRK04863 530 RQ--------QQRAERLLAEFCKRLGKNLDDEDEL--------EQLQEELEARLESLS-----------------ESVSE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1679 AKAEESALKQKemaEEELERQRKIAESTAQQKLTAEQELIRLR----ADFDNAEQQRSLLEDELYRLKnevaAAQQQRKQ 1754
Cdd:PRK04863 577 ARERRMALRQQ---LEQLQARIQRLAARAPAWLAAQDALARLReqsgEEFEDSQDVTEYMQQLLERER----ELTVERDE 649
|
490
....*....|....*..
gi 1988774682 1755 LEDELAKVRSEMDILIQ 1771
Cdd:PRK04863 650 LAARKQALDEEIERLSQ 666
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
47-143 |
2.57e-09 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 57.58 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 47 KKTFTKWVN---------KHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDFL 112
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1988774682 113 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 143
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1374-1581 |
2.83e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 62.17 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1374 QKQLAEAHAKAIAKAEKEAqelKLKMQEEVSKREIAAVDAEKQKtniQLELQELKNLSEQQIKDKSqqvdealhsrTKIE 1453
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPA---AKKEQERQKKLEQQAEEAEKQR---AAEQARQKELEQRAAAEKA----------AKQA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1454 EEIRLiriqlETTEKQKYTAESELKQLRDRAAEAEKLRKlaQDEAEKLRKQVSEETQKKRQAE-----EELKRKSEAEKE 1528
Cdd:TIGR02794 108 EQAAK-----QAEEKQKQAEEAKAKQAAEAKAKAEAEAE--RKAKEEAAKQAEEEAKAKAAAEakkkaEEAKKKAEAEAK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774682 1529 A---AKQKQKALEDLEKLRMQAEEAERQVKqAEIEKEKQIKVAHEAAQKSAAAELQ 1581
Cdd:TIGR02794 181 AkaeAEAKAKAEEAKAKAEAAKAKAAAEAA-AKAEAEAAAAAAAEAERKADEAELG 235
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2436-2606 |
3.11e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2436 KEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEE 2515
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2516 EVKKAKALKdEQERQKQQMEQEKKTLQATMDAAL-SKQKEAEEEMLRKQKEMQELERQRLEQERILA---EENQKLREKL 2591
Cdd:COG4717 151 LEERLEELR-ELEEELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQRLAELEEELEeaqEELEELEEEL 229
|
170
....*....|....*
gi 1988774682 2592 QQLEDAQKDQHTRET 2606
Cdd:COG4717 230 EQLENELEAAALEER 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
996-1570 |
3.42e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 996 LRIEDCE--AGTVARIRKPV--EKEPLKEYIQKTTEQKKVQGELdglKKDLDKVSVKTQEVlaspqpSASAPVLRSELDl 1071
Cdd:PRK03918 155 LGLDDYEnaYKNLGEVIKEIkrRIERLEKFIKRTENIEELIKEK---EKELEEVLREINEI------SSELPELREELE- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1072 tvqkmdhahMLSSVYLEKLKTVEMVirntqgaEGVLKQYEDCLREVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSL 1151
Cdd:PRK03918 225 ---------KLEKEVKELEELKEEI-------EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1152 EEELKKASAVS---DKMVRVHSERDVELDHFRQQLSSLQDRWKavftqidlrqrELEQLGRQLGYYRESYDWLIRWIADA 1228
Cdd:PRK03918 289 KEKAEEYIKLSefyEEYLDELREIEKRLSRLEEEINGIEERIK-----------ELEEKEERLEELKKKLKELEKRLEEL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1229 KQRQEKIQavpitDSKTLKEQLAQEKKLLEEIEqnKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKKT--K 1306
Cdd:PRK03918 358 EERHELYE-----EAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1307 LDSASDNII--------QEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEER-----KKMAEMQAELdk 1373
Cdd:PRK03918 431 LKKAKGKCPvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklKELAEQLKEL-- 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1374 QKQLAEAHAKAIAKAEKEAQELK-----LKMQEEVSKREIAAVDA-EKQKTNIQLELQEL-KNLSE--QQIKDKSQQVDE 1444
Cdd:PRK03918 509 EEKLKKYNLEELEKKAEEYEKLKeklikLKGEIKSLKKELEKLEElKKKLAELEKKLDELeEELAEllKELEELGFESVE 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1445 ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEetQKKRQAEEELKRKSE 1524
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE--LEKKYSEEEYEELRE 666
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1988774682 1525 AEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHE 1570
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1791-2601 |
3.71e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1791 LEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEaaRQRAEAERILKEKLAAIsEATRLKTEAEIALKEK---EAENER 1867
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREY-EGYELLKEKEALERQKeaiERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1868 LRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLE 1947
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1948 LELNKLKniaDETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRkaalEELERLRKKAEEARKQK 2027
Cdd:TIGR02169 329 AEIDKLL---AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR----DELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2028 DEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEyekakklakeaeaakekaereaalLRQQAEEA 2107
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE------------------------IKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2108 ERQKTAAEEEAANQAKAQEDAERLRKEaefeaakraqaeaaaLMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLK 2187
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKE---------------LSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2188 LDETDKQKSVLDEELQ---------RLKDEV--DDAVKQRGQveEELFKVKVQMEELLKLkNKIEEENQRLIKKDKDSTQ 2256
Cdd:TIGR02169 523 VHGTVAQLGSVGERYAtaievaagnRLNNVVveDDAVAKEAI--ELLKRRKAGRATFLPL-NKMRDERRDLSILSEDGVI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2257 KLLAEEAENMRKLAEDAA-----RLSVEAQEAA-------RLRQIAEDDLNQQRALAEKMLKEKmQAIQEASRLKAEAEM 2324
Cdd:TIGR02169 600 GFAVDLVEFDPKYEPAFKyvfgdTLVVEDIEAArrlmgkyRMVTLEGELFEKSGAMTGGSRAPR-GGILFSRSEPAELQR 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2325 LQKQKdlaqEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLrlqvsqlseaqaraeeeakkfKKQAD 2404
Cdd:TIGR02169 679 LRERL----EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL---------------------EQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2405 KVATRLheteiatQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQnksKEMADAQQKKIEHEKTVL 2484
Cdd:TIGR02169 734 KLKERL-------EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEIQAELSKL 803
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2485 qqtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVkkAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQK 2564
Cdd:TIGR02169 804 ------EEEVSRIEARLREIEQKLNRLTLEKEY--LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
810 820 830
....*....|....*....|....*....|....*..
gi 1988774682 2565 EMQELERQRLEqeriLAEENQKLREKLQQLEDAQKDQ 2601
Cdd:TIGR02169 876 ALRDLESRLGD----LKKERDELEAQLRELERKIEEL 908
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1108-1635 |
4.01e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 63.45 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1108 KQYEDCLREVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQ 1187
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1188 -------------DRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIAD--AKQRQEKIQAVPITD---SKTLKEQ 1249
Cdd:TIGR00618 380 hihtlqqqkttltQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQqeLQQRYAELCAAAITCtaqCEKLEKI 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1250 LAQE--KKLLEEIEQNKDKVDECQKYAKayIDTIKDYELQLVA-------------YKAQVEPLVSPLKKTKLDSASDNI 1314
Cdd:TIGR00618 460 HLQEsaQSLKEREQQLQTKEQIHLQETR--KKAVVLARLLELQeepcplcgscihpNPARQDIDNPGPLTRRMQRGEQTY 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1315 IQEYVTLRTRYSELMTLTSQyIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQE 1394
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1395 LKLKMQEEVSKREIAAVDAEKQKTNIQLEL---QELKNLSEQQIKDKSqqvdealhSRTKIEEEIRLIRIQLETTEkqky 1471
Cdd:TIGR00618 617 LLRKLQPEQDLQDVRLHLQQCSQELALKLTalhALQLTLTQERVREHA--------LSIRVLPKELLASRQLALQK---- 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1472 tAESELKQLRDRAAEAEKLRKLAQDEAEKLrKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAE 1551
Cdd:TIGR00618 685 -MQSEKEQLTYWKEMLAQCQTLLRELETHI-EEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1552 RQVKQAEI-------EKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAEN 1624
Cdd:TIGR00618 763 HFNNNEEVtaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSA 842
|
570
....*....|.
gi 1988774682 1625 SREEAEKELEK 1635
Cdd:TIGR00618 843 TLGEITHQLLK 853
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4385-4423 |
5.16e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 54.26 E-value: 5.16e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1988774682 4385 FLEVQYLTGGLIEPDVEGRVSIDESIRKGTIDARTAQKL 4423
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2373-2586 |
5.22e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2373 AEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAtqekmtvVERLEFERLNTSKEADDLRKAIADLENEK 2452
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR-------IAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2453 ARLKKEAEELQNKSKEMADAQQKKIEHEKTVL----------------QQTFMTEKEMLLKKEKLIEDEKKRLESQFEEE 2516
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2517 VKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQK 2586
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
156-258 |
6.99e-09 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 56.71 E-value: 6.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 156 QSEDMTAKEKLLLWSQ-RMTDgyqgIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLG 233
Cdd:cd21315 11 DGKGPTPKQRLLGWIQsKVPD----LPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDaVKNAKEAMDLAEDWLD 86
|
90 100
....*....|....*....|....*
gi 1988774682 234 VTRLLDPEDVDVPHPDEKSIITYVS 258
Cdd:cd21315 87 VPQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1626-2385 |
7.43e-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: 7.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1626 REEAEKELEKWRQKANEaLRLRLQAEDEAHKK-------TLAQEEAEKQKEEAEREA-----KKRAKAEESALKQKEMAE 1693
Cdd:pfam15921 73 KEHIERVLEEYSHQVKD-LQRRLNESNELHEKqkfylrqSVIDLQTKLQEMQMERDAmadirRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1694 EELERQRKIAESTAQQKLT--------------AEQELIRLRADFDNAEQQRSLLEDELYRL--KNEVAAAQQQRKQLED 1757
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTqieqlrkmmlshegVLQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1758 ELAKVRSEM----DILIQLKTKAEKET----MSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQ 1829
Cdd:pfam15921 232 EISYLKGRIfpveDQLEALKSESQNKIelllQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1830 RAEAERILKEKLAAISEatrLKTEAEIALKEKEAENERLRRQ---AEDEAYQRKALEDQASQHKQEIEEKIvqlkkssea 1906
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQ---LRSELREAKRMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDDQL--------- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1907 emerQKAIVDdtLKQRrvvEEEirilklnfekassgkLDLELELNklKNIADETQQSKIRAEEEAEKLrklaleeekrrr 1986
Cdd:pfam15921 380 ----QKLLAD--LHKR---EKE---------------LSLEKEQN--KRLWDRDTGNSITIDHLRREL------------ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1987 eaeekvkkiaaaeeeaaRQRKAALEELERLRKkaeearKQKDEADKEAEKQIVVAQ---QAAQKCSAAEQQVQSV--LAQ 2061
Cdd:pfam15921 422 -----------------DDRNMEVQRLEALLK------AMKSECQGQMERQMAAIQgknESLEKVSSLTAQLESTkeMLR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2062 QIEDSITQKKLKEEyekakKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRK-EAEFEAA 2140
Cdd:pfam15921 479 KVVEELTAKKMTLE-----SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvQTECEAL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2141 KRAQAEAAALMQ--KQQADTEM---AKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDavkq 2215
Cdd:pfam15921 554 KLQMAEKDKVIEilRQQIENMTqlvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD---- 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2216 rgqVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKL--LAEEAENM-RKLAEDAARLSVEAQEAARLRQIAED 2292
Cdd:pfam15921 630 ---LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLkRNFRNKSEEMETTTNKLKMQLKSAQS 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2293 DLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE---DKQLMQQRLEEETEEYHKSLEVERKRQL 2369
Cdd:pfam15921 707 ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEamtNANKEKHFLKEEKNKLSQELSTVATEKN 786
|
810
....*....|....*.
gi 1988774682 2370 EIMAEAERLRLQVSQL 2385
Cdd:pfam15921 787 KMAGELEVLRSQERRL 802
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1481-1706 |
8.49e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 61.43 E-value: 8.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1481 RDRAAEAEKLRKLAQDEAEKLrKQVSEETQKKRQAEEELKRKSE------AEKEAAKQKQKALEDLEKLRMQAEeAERQV 1554
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERE-TEIAIAQANREAEEAELEQEREietariAEAEAELAKKKAEERREAETARAE-AEAAY 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1555 KQAEIEKEKQIKVAHEAAQKSAAAELQSKhmsfaektsKLEESLKQEHgAVLQLQQEAERLKKQQEdaensrEEAEKEle 1634
Cdd:COG2268 269 EIAEANAEREVQRQLEIAEREREIELQEK---------EAEREEAELE-ADVRKPAEAEKQAAEAE------AEAEAE-- 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 1635 kwrqkaneALRLRLQAEDEAHKKtlaqeeaekqKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAEST 1706
Cdd:COG2268 331 --------AIRAKGLAEAEGKRA----------LAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1422-1823 |
8.59e-09 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 61.90 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1422 LELQELKNLSEQQIKDKSQQVDealhSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAqDEAEKL 1501
Cdd:COG5185 184 LTLGLLKGISELKKAEPSGTVN----SIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTS-DKLEKL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1502 RKQVSE-ETQKKRQAEEELKRKSEAEKEAAKQ----KQKALEDLEKLRMQA--EEAERQVKQAEIEKEKQIKVAH-EAAQ 1573
Cdd:COG5185 259 VEQNTDlRLEKLGENAESSKRLNENANNLIKQfentKEKIAEYTKSIDIKKatESLEEQLAAAEAEQELEESKREtETGI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1574 KSAAAELQSKHMSFAEKTSKLEESLKQEHGAVL--QLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAE 1651
Cdd:COG5185 339 QNLTAEIEQGQESLTENLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1652 DEAHKKtlaqeeaekqkeeAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELI--RLRADFDNAEQ 1729
Cdd:COG5185 419 DRQIEE-------------LQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEInrSVRSKKEDLNE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1730 QRSLLEDELYRLKNEVaaaQQQRKQLEDELAKVRSEMDILIQLKTKAEKETmsNTEKSKQLLEAEAAKMKDLAEEASRLR 1809
Cdd:COG5185 486 ELTQIESRVSTLKATL---EKLRAKLERQLEGVRSKLDQVAESLKDFMRAR--GYAHILALENLIPASELIQASNAKTDG 560
|
410
....*....|....
gi 1988774682 1810 AISEEAKHQRQIAE 1823
Cdd:COG5185 561 QAANLRTAVIDELT 574
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
48-142 |
8.62e-09 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 56.19 E-value: 8.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 48 KTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMrfhkLQNVQIALDFLRHRQVKL 119
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1988774682 120 VNIRNDDIADGNPKLTLGLIWTI 142
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1420-1780 |
9.53e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 61.45 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1420 IQLELQElknlSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETT----EKQKYTAESELKQLRDRAAEAEKLRKLAQ 1495
Cdd:pfam07888 32 LQNRLEE----CLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1496 DEAEKLRKqvsEETQKKRQAEEELKRKSEAEKEAAKQKQKALE---DLEKLRMQAEEAERQVKQAEIEKEK-QIKV-AHE 1570
Cdd:pfam07888 108 ASSEELSE---EKDALLAQRAAHEARIRELEEDIKTLTQRVLEretELERMKERAKKAGAQRKEEEAERKQlQAKLqQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1571 AAQKSAAAELQSKHMSFAEKTSKLEE------SLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAL 1644
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQlqdtitTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1645 RLRLQAEDEAHKKTLAQEEAEKQKEEAE---REAKKRAKAEESALKQKEMAE--------EELERQRKIAESTAQQKLTA 1713
Cdd:pfam07888 265 AQRDRTQAELHQARLQAAQLTLQLADASlalREGRARWAQERETLQQSAEADkdrieklsAELQRLEERLQEERMEREKL 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774682 1714 EQELIRLRadfDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVrseMDILIQLKTKAEKET 1780
Cdd:pfam07888 345 EVELGREK---DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL---LEYIRQLEQRLETVA 405
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1594-1917 |
9.99e-09 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 60.85 E-value: 9.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1594 LEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEahKKTLAQEEAEKQKEEAER 1673
Cdd:pfam19220 25 LKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGE--LEELVARLAKLEAALREA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1674 EAKKRAKAeeSALKQKEMAEEELERQRKIAestAQQKLTAEQELIRLRADFDNAEQQRSLLEDELyrlknevAAAQQQRK 1753
Cdd:pfam19220 103 EAAKEELR--IELRDKTAQAEALERQLAAE---TEQNRALEEENKALREEAQAAEKALQRAEGEL-------ATARERLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1754 QLEDELAKVRSEMDiliqlktKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLraISEEAKHQRQIAEEEAARQRAEA 1833
Cdd:pfam19220 171 LLEQENRRLQALSE-------EQAAELAELTRRLAELETQLDATRARLRALEGQL--AAEQAERERAEAQLEEAVEAHRA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1834 ERI-LKEKLAAIS---EAT-RLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKksseaEM 1908
Cdd:pfam19220 242 ERAsLRMKLEALTaraAATeQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQ-----EM 316
|
....*....
gi 1988774682 1909 ERQKAIVDD 1917
Cdd:pfam19220 317 QRARAELEE 325
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1361-1531 |
1.09e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 61.33 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1361 RKKMAEMQAELDKQKQLAEAHAKAIAK-----AEKEAQELKLKMQEEVSKREiaavdaekqktniqLELQELknlsEQQI 1435
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKealleAKEEIHKLRNEFEKELRERR--------------NELQKL----EKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1436 KDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRA-AEAEKLRKLAQDEA-EKLRKQVSEETQKKR 1513
Cdd:PRK12704 92 LQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQlQELERISGLTAEEAkEILLEKVEEEARHEA 171
|
170 180
....*....|....*....|.
gi 1988774682 1514 QA---EEELKRKSEAEKEAAK 1531
Cdd:PRK12704 172 AVlikEIEEEAKEEADKKAKE 192
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2246-2612 |
1.21e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2246 RLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRqiaeDDLNQQRALAEKMLKEKmqaiQEASRLKAEAEML 2325
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIS----SELPELREELEKLEKEV----KELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2326 QKQKDLAQEQAQKLLEDKQLMQQRLEEeTEEYHKSLEVERKRQLEIMAEAERLRlqvsqlseaqaraeeEAKKFKKQADK 2405
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEE-LKKEIEELEEKVKELKELKEKAEEYI---------------KLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2406 VATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAE----------ELQNKSKEMADAQQK 2475
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyeeakakkeELERLKKRLTGLTPE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2476 KIEHEKTVLQqtfmTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQER----QKQQMEQEKKTLQATMDAALSK 2551
Cdd:PRK03918 388 KLEKELEELE----KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEYTAELKR 463
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2552 ----QKEAEEEMLRKQKEMQELERQRLEQERI-----LAEENQKLREKLQQLEDAQKDQHTRETDKVLHK 2612
Cdd:PRK03918 464 iekeLKEIEEKERKLRKELRELEKVLKKESELiklkeLAEQLKELEEKLKKYNLEELEKKAEEYEKLKEK 533
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2102-2558 |
1.22e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2102 QQAEEAERQKTAAEEEAANQAKAQEDAERLRKE-AEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQE 2180
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEElEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2181 LTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRG-QVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLl 2259
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2260 aEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQ--EQAQ 2337
Cdd:COG4717 230 -EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKeaEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2338 KLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSeaqaraeeeakKFKKQADKVATRLHETEIAT 2417
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE-----------ELEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2418 QEKMTVVERLEfERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEmaDAQQKKIEHEKTVLQQTfMTEKEMLLK 2497
Cdd:COG4717 378 EAGVEDEEELR-AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEEL-EEELEELRE 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 2498 KEKLIEDEKKRLESqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEE 2558
Cdd:COG4717 454 ELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1607-2061 |
1.24e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1607 QLQQEAERLKKQQEDAENSREEAEKElekwRQKAnEALRlRLQAEDEAHKKTlaqeeaeKQKEEAEREAKKRAKAEESAL 1686
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDA----REQI-ELLE-PIRELAERYAAA-------RERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1687 KQkEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLE-DELYRLKNEVAAAQQQRKQLEDELAKVRSE 1765
Cdd:COG4913 289 RL-ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1766 MDILiQLKTKAEKETMSNT-EKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERI---LKEKL 1841
Cdd:COG4913 368 LAAL-GLPLPASAEEFAALrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1842 AAISEATRLKTEA--------EIALKEKEAEN--ER-LRRQA-----EDEAYQR-----------------KALEDQASQ 1888
Cdd:COG4913 447 DALAEALGLDEAElpfvgeliEVRPEEERWRGaiERvLGGFAltllvPPEHYAAalrwvnrlhlrgrlvyeRVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1889 HKQEIEEK----IVQLKKSS-----EAEMERQKAIV----DDTLKQ--RRVVEEeiRILKLN---FEKASSGKL------ 1944
Cdd:COG4913 527 ERPRLDPDslagKLDFKPHPfrawlEAELGRRFDYVcvdsPEELRRhpRAITRA--GQVKGNgtrHEKDDRRRIrsryvl 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1945 ---------DLELELNKLKNIADETQQSKIRAEEEAEKL--RKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALE-- 2011
Cdd:COG4913 605 gfdnraklaALEAELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDAss 684
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 2012 -ELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQ 2061
Cdd:COG4913 685 dDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1453-1922 |
1.33e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.89 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1453 EEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAeklrKLAQDEAEKLRKQVS---EET--QKKRQAEEELKRKSEAEK 1527
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQL----KEQLQLLNKLLPQANllaDETlaDRLEELREELDAAQEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1528 EAAkQKQKALEDLEK----LR---MQAEEAERQVKQAEiEKEKQIKvaheaAQKSAAAEL--QSKHMSFAEKTSKLEESl 1598
Cdd:COG3096 911 FIQ-QHGKALAQLEPlvavLQsdpEQFEQLQADYLQAK-EQQRRLK-----QQIFALSEVvqRRPHFSYEDAVGLLGEN- 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1599 kqehgavlqlQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRlRLQAEDEAHkktlaqeeaekqkeeaereakkR 1678
Cdd:COG3096 983 ----------SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ-VLASLKSSR----------------------D 1029
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1679 AKAEESALKQKEMAEeelerqrkiaestaqqkltaeqelIRLRADfDNAEQQRSLLEDELYrlkNEVAAAQQQRKQLEDE 1758
Cdd:COG3096 1030 AKQQTLQELEQELEE------------------------LGVQAD-AEAEERARIRRDELH---EELSQNRSRRSQLEKQ 1081
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1759 LAKVRSEMDILIQLKTKAEKETMSNTEkskqllEAEAAKmkdlaEEASRLRAISEEAKHQRQIAEEEAARQRAeaerilk 1838
Cdd:COG3096 1082 LTRCEAEMDSLQKRLRKAERDYKQERE------QVVQAK-----AGWCAVLRLARDNDVERRLHRRELAYLSA------- 1143
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1839 EKLAAISEatrlktEAEIALKEKEAENERLR---RQAEDEAY-QRK-ALEDQASQHKQE-IEEKIVQLKKSSEA--EMER 1910
Cdd:COG3096 1144 DELRSMSD------KALGALRLAVADNEHLRdalRLSEDPRRpERKvQFYIAVYQHLRErIRQDIIRTDDPVEAieQMEI 1217
|
490
....*....|..
gi 1988774682 1911 QKAIVDDTLKQR 1922
Cdd:COG3096 1218 ELARLTEELTSR 1229
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1510-1779 |
1.42e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.51 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1510 QKKRQAEEELKRKSEAE---KEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEK-EKQIKVAHEAAQKSAaaelqsKHM 1585
Cdd:PRK04863 844 RRRVELERALADHESQEqqqRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEiREQLDEAEEAKRFVQ------QHG 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1586 SFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAEN---------------SREEAEKELEKwRQKANEALRLRL-Q 1649
Cdd:PRK04863 918 NALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafaltevvqrrahfSYEDAAEMLAK-NSDLNEKLRQRLeQ 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1650 AEDEAhkktlaqeeaekqkeeaeREAKKRAKAEESALKQKEMAEEELerqrKIAESTAQQKLT-AEQEL--IRLRADFdN 1726
Cdd:PRK04863 997 AEQER------------------TRAREQLRQAQAQLAQYNQVLASL----KSSYDAKRQMLQeLKQELqdLGVPADS-G 1053
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 1727 AEQQRSLLEDELYrlkNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKE 1779
Cdd:PRK04863 1054 AEERARARRDELH---ARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2250-2589 |
1.54e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 59.93 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2250 KDKDSTQKLLAEEAENMRKLAEdAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQK 2329
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMME-EERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2330 DLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQvsqlseaqaraeeeakKFKKQADKVATR 2409
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE----------------YLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2410 LHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADL---ENEKARLKKEAEELQNKSKEMADAQQkkiehektVLQQ 2486
Cdd:pfam13868 172 EAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLyqeEQERKERQKEREEAEKKARQRQELQQ--------AREE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2487 TFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKAlkdEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEM 2566
Cdd:pfam13868 244 QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE---EAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
|
330 340
....*....|....*....|...
gi 1988774682 2567 QELERQRleQERILAEENQKLRE 2589
Cdd:pfam13868 321 REEEAER--RERIEEERQKKLKE 341
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1507-1954 |
1.56e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 61.22 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1507 EETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEklrmqaeeaERQVKQAEIEKEKQI-----KVAHEAAQKSAAAELQ 1581
Cdd:PRK10929 24 DEKQITQELEQAKAAKTPAQAEIVEALQSALNWLE---------ERKGSLERAKQYQQVidnfpKLSAELRQQLNNERDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1582 SKHMSFAEKTSKLEESLKQEHGAVL----QLQQEAER----------LKKQQEDAENSREEAEKELE---KWRQKANEAL 1644
Cdd:PRK10929 95 PRSVPPNMSTDALEQEILQVSSQLLeksrQAQQEQDRareisdslsqLPQQQTEARRQLNEIERRLQtlgTPNTPLAQAQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1645 RLRLQAEDEAHKKTLaqeeaekqkeeaereakkrakaeesalkqkemaeEELErqrkiaesTAQQKLTAEQELIRLRAdf 1724
Cdd:PRK10929 175 LTALQAESAALKALV----------------------------------DELE--------LAQLSANNRQELARLRS-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1725 dnaeqqrslledELYrlknevaaaQQQRKQLEDELAKVRSemdiliQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEE 1804
Cdd:PRK10929 211 ------------ELA---------KKRSQQLDAYLQALRN------QLNSQRQREAERALESTELLAEQSGDLPKSIVAQ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1805 ASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAaiseatrLKTEAEIA--LKEKEAENERLRRQAEDEAYQRKAl 1882
Cdd:PRK10929 264 FKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQA-------LNTLREQSqwLGVSNALGEALRAQVARLPEMPKP- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1883 edqasqhkQEIEEKIVQLKKSS---EAEMERQ----KAIVDD----TLKQRRVVEEEIRILKLNFEKASSGKLDLELELN 1951
Cdd:PRK10929 336 --------QQLDTEMAQLRVQRlryEDLLNKQpqlrQIRQADgqplTAEQNRILDAQLRTQRELLNSLLSGGDTLILELT 407
|
...
gi 1988774682 1952 KLK 1954
Cdd:PRK10929 408 KLK 410
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
46-145 |
1.91e-08 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 55.20 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 46 QKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKG-----RMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 1988774682 121 NIRNDDIADGNPKLTLGLIWTIILH 145
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
161-263 |
2.58e-08 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 55.08 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 161 TAKEKLLLWSQRMTdgyQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLD 239
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQpVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1988774682 240 PEDVDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1349-1561 |
2.61e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 59.09 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1349 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAvdAEKQKtniqleLQELK 1428
Cdd:TIGR02794 78 EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAE--AERKA------KEEAA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1429 NLSEQQIKDKSQQvdealhsrtkieeeirliriqlettEKQKYTAESELKQLRDRAAEAEKLRKLAQDE----AEKLRKQ 1504
Cdd:TIGR02794 150 KQAEEEAKAKAAA-------------------------EAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKAK 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774682 1505 VSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDL--EKLRMQAEEAERQVKQAEIEK 1561
Cdd:TIGR02794 205 AAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLasGSNAEKQGGARGAAAGSEVDK 263
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1853-2489 |
2.62e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1853 EAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQH---KQEIEEKIVQLKKSSE--AEMERQKAIVDDTLKQRRVVEE 1927
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHeerREELETLEAEIEDLREtiAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1928 EIR------ILKLNFEKASSGKL-----DLELELNKLKNIADETQQSKIRAEEEAEKLRklaleeekrrreaeekvkkia 1996
Cdd:PRK02224 290 ELEeerddlLAEAGLDDADAEAVearreELEDRDEELRDRLEECRVAAQAHNEEAESLR--------------------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1997 aaeeeaarqrkaalEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSvLAQQIEDSITQKKLKEEY 2076
Cdd:PRK02224 349 --------------EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE-LRERFGDAPVDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2077 ekakklakeaeaakekaereAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRaqaeaaalmqkqqa 2156
Cdd:PRK02224 414 --------------------LEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQ-------------- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2157 DTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDEtdkqksvLDEELQRLKdevdDAVKQRGQVEEELFKVKVQMEELLKL 2236
Cdd:PRK02224 460 PVEGSPHVETIEEDRERVEELEAELEDLEEEVEE-------VEERLERAE----DLVEAEDRIERLEERREDLEELIAER 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2237 KNKIEEENQRLIKKDKDSTQklLAEEAENMRKLAEDAARLSVEAQEAArlrqiaeDDLNQQRAlaekMLKEKMQAIQEAS 2316
Cdd:PRK02224 529 RETIEEKRERAEELRERAAE--LEAEAEEKREAAAEAEEEAEEAREEV-------AELNSKLA----ELKERIESLERIR 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2317 RLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETeeyhkslevERKRQLEIMAEAERLrlqvsqlsEAQARAEEEA 2396
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREALAELNDERRERLAEKR---------ERKRELEAEFDEARI--------EEAREDKERA 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2397 KKFKKQADKVATRLHETEIATQEKMTVVERlEFERLntskeaDDLRKAIADLENEKARLK---KEAEELQNKSKEM-ADA 2472
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEIGAVEN-ELEEL------EELRERREALENRVEALEalyDEAEELESMYGDLrAEL 731
|
650
....*....|....*..
gi 1988774682 2473 QQKKIEHEKTVLQQTFM 2489
Cdd:PRK02224 732 RQRNVETLERMLNETFD 748
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1350-1582 |
2.98e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 59.09 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1350 EKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREiaavdAEKQKTNIQLELQELKN 1429
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1430 LSEQQIKDKSQQvDEALHSRTKIEEEIRliriQLETTEKQKYTAESELKqlrdrAAEAEKlrklaQDEAEKLRKqvsEET 1509
Cdd:TIGR02794 124 AKAKQAAEAKAK-AEAEAERKAKEEAAK----QAEEEAKAKAAAEAKKK-----AEEAKK-----KAEAEAKAK---AEA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774682 1510 QKKRQAeEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEI------EKEKQIKVAHEAAQKSAAAELQS 1582
Cdd:TIGR02794 186 EAKAKA-EEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELgdifglASGSNAEKQGGARGAAAGSEVDK 263
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1756-2379 |
3.03e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1756 EDELAKVRSEmdilIQLKTKAEKETMSNTEKSKQLLEAeaaKMKDLAEEASRLRAISEEakhqrqiaEEEAARQRAEAER 1835
Cdd:PRK03918 164 YKNLGEVIKE----IKRRIERLEKFIKRTENIEELIKE---KEKELEEVLREINEISSE--------LPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1836 ILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEdqasqhkqEIEEKIVQLK--KSSEAEMERQKA 1913
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE--------ELEEKVKELKelKEKAEEYIKLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1914 IVDDTLKQRRVVE-------EEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRR 1986
Cdd:PRK03918 301 FYEEYLDELREIEkrlsrleEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1987 EAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKdeadKEAEKQIVVAQQAAQKCsaaeqqvqSVLAQQIEDS 2066
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI----KELKKAIEELKKAKGKC--------PVCGRELTEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2067 iTQKKLKEEYEKAKKLAKEAEaakekaereaallrQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAE 2146
Cdd:PRK03918 449 -HRKELLEEYTAELKRIEKEL--------------KEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2147 AAALMQKQQADTEMAKHKKLA----------EQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQR 2216
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLiklkgeikslKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2217 GQVEEELFKvkvqmeELLKLKNkieeenqrlIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQ 2296
Cdd:PRK03918 594 LKELEPFYN------EYLELKD---------AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2297 QRalAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKqlmqqrleEETEEYHKSLEVERKrqleIMAEAE 2376
Cdd:PRK03918 659 EE--YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL--------EEREKAKKELEKLEK----ALERVE 724
|
...
gi 1988774682 2377 RLR 2379
Cdd:PRK03918 725 ELR 727
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1363-1542 |
3.06e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 57.63 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1363 KMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELklkmQEEVSKREIAAVDAEKQKTNIQLELQELknlsEQQIKDKSQQV 1442
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAAL----EARLEAAKTELEDLEKEIKRLELEIEEV----EARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1443 DEALHSRtkieeEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRK 1522
Cdd:COG1579 83 GNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170 180
....*....|....*....|
gi 1988774682 1523 seaEKEAAKQKQKALEDLEK 1542
Cdd:COG1579 158 ---LEELEAEREELAAKIPP 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1344-1711 |
3.07e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1344 RRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQ---------ELKLKMQEEVSK-REIAAVDA 1413
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaelperleELEERLEELRELeEELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1414 EKQKTNIQLE--LQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQ--KYTAESELKQLRDRAAEAE- 1488
Cdd:COG4717 171 ELAELQEELEelLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLKEARl 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1489 --------------------------------------------KLRKLAQDEAEKLRKQVSEETQKKRQAEEELKR--- 1521
Cdd:COG4717 251 llliaaallallglggsllsliltiagvlflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELLAAlgl 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1522 KSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQK----SAAAELQSKHMSFAEKTSKLEES 1597
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDeeelRAALEQAEEYQELKEELEELEEQ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1598 LKQEHGAVLQL--QQEAERLKKQQEDAENSREEAEKELEKWRQKanealrlrlQAEDEAHKKTLAQEEAEKQKEEAEREA 1675
Cdd:COG4717 411 LEELLGELEELleALDEEELEEELEELEEELEELEEELEELREE---------LAELEAELEQLEEDGELAELLQELEEL 481
|
410 420 430
....*....|....*....|....*....|....*.
gi 1988774682 1676 KKRAKAEESALKQKEMAEEELERQRKIAESTAQQKL 1711
Cdd:COG4717 482 KAELRELAEEWAALKLALELLEEAREEYREERLPPV 517
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1010-1912 |
3.50e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 60.45 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1010 RKPVEKEPLKEYIQKTTEQKKVQGELDGLKKDLDKVSVKTQEvlaspqpsasapvLRSELDLTVQKMDHAHMlssvylEK 1089
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEK-------------DNSELELKMEKVFQGTD------EQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1090 LKTVEmvirNTQGAEGVLKQYE--DCLREVHTVPSDVKEvetyrakLKKMRTEAEDEQPVFdSLEEELKKASAVSDKMVR 1167
Cdd:TIGR00606 303 LNDLY----HNHQRTVREKERElvDCQRELEKLNKERRL-------LNQEKTELLVEQGRL-QLQADRHQEHIRARDSLI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1168 VHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQAVPITDSKTLK 1247
Cdd:TIGR00606 371 QSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1248 EQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDyeLQLVAYKAQVEPLVSPLKKTKLDSAsdNIIQEYVTLRTRYSE 1327
Cdd:TIGR00606 451 KKQEELKFVIKELQQLEGSSDRILELDQELRKAERE--LSKAEKNSLTETLKKEVKSLQNEKA--DLDRKLRKLDQEMEQ 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1328 LMTLTSQYIKFITDTQRRLDDEEKaAEKLKAEERKKMAEMQAELDKQKQLAEAHAKaIAKAEKEAQELKLKMQEEVSKRE 1407
Cdd:TIGR00606 527 LNHHTTTRTQMEMLTKDKMDKDEQ-IRKIKSRHSDELTSLLGYFPNKKQLEDWLHS-KSKEINQTRDRLAKLNKELASLE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1408 IAAVDAEKQKTniQLELQELKnLSEQQIKDKSQQVDEALHSRTKieEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEA 1487
Cdd:TIGR00606 605 QNKNHINNELE--SKEEQLSS-YEDKLFDVCGSQDEESDLERLK--EEIEKSSKQRAMLAGATAVYSQFITQLTDENQSC 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1488 EKL-RKLAQDEAEkLRKQVSEETQKKRQAEEELKrksEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIK 1566
Cdd:TIGR00606 680 CPVcQRVFQTEAE-LQEFISDLQSKLRLAPDKLK---STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1567 VAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQ--QEDAENSREEAEKELEKWRQKANEal 1644
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKiaQQAAKLQGSDLDRTVQQVNQEKQE-- 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1645 rlrlqaEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADF 1724
Cdd:TIGR00606 834 ------KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1725 DNAEQ-QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMK-DLA 1802
Cdd:TIGR00606 908 KEQDSpLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNaQLE 987
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1803 EEASRLRAISEEAKHQRQIAEEEAARqraeaERILKEKLaaiseaTRLKTEAEIalkekeAENERLRRQAEDEAYQRKAL 1882
Cdd:TIGR00606 988 ECEKHQEKINEDMRLMRQDIDTQKIQ-----ERWLQDNL------TLRKRENEL------KEVEEELKQHLKEMGQMQVL 1050
|
890 900 910
....*....|....*....|....*....|
gi 1988774682 1883 edQASQHKQEIEEKIVQLKKSSEAEMERQK 1912
Cdd:TIGR00606 1051 --QMKQEHQKLEENIDLIKRNHVLALGRQK 1078
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2199-2603 |
5.12e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 59.45 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2199 DEELQRLKDEVDDAVKqrgqveeELFKVKVQMEELlklKNKIEEENQRLIKKDkDSTQKLLAeeaenMRKLAEDAARLSV 2278
Cdd:pfam10174 115 EENFRRLQSEHERQAK-------ELFLLRKTLEEM---ELRIETQKQTLGARD-ESIKKLLE-----MLQSKGLPKKSGE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2279 EAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRlkaeaeMLQKQKDLAQEQA-QKLLEDKQLMQQRLEEETEEY 2357
Cdd:pfam10174 179 EDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHR------RNQLQPDPAKTKAlQTVIEMKDTKISSLERNIRDL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2358 HKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLH--ETEIATQEKMTVVERLEFERLNTS 2435
Cdd:pfam10174 253 EDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLalQTKLETLTNQNSDCKQHIEVLKES 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2436 KEADDLRKAIADLENEKARLKKEAEE--LQNKSKEMADAQQkkiehEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQF 2513
Cdd:pfam10174 333 LTAKEQRAAILQTEVDALRLRLEEKEsfLNKKTKQLQDLTE-----EKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2514 EEEVKKAKALKDEQERQK--QQMEQEKKTLQATMDAALSkQKEAEEEMLRKQKEmqELERQRLEQERILAEENQKLREKL 2591
Cdd:pfam10174 408 EQLRDKDKQLAGLKERVKslQTDSSNTDTALTTLEEALS-EKERIIERLKEQRE--REDRERLEELESLKKENKDLKEKV 484
|
410
....*....|..
gi 1988774682 2592 QQLEDAQKDQHT 2603
Cdd:pfam10174 485 SALQPELTEKES 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2334-2607 |
5.35e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2334 EQAQKLLEDKQLMQQRLEEETEEYHKSLEVERK----RQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATR 2409
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEkreyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2410 LHETEIATQEKMTVVERL-EFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEKTVLQQTF 2488
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-LEAEIDKLLAEIEELEREI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2489 MTEKEMLLK-KEKLIEDEKKR--LESQFEEEVKKAKALKDEQERQKQQMEQ----------EKKTLQATMDAALSKQKEA 2555
Cdd:TIGR02169 346 EEERKRRDKlTEEYAELKEELedLRAELEEVDKEFAETRDELKDYREKLEKlkreinelkrELDRLQEELQRLSEELADL 425
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 2556 EEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETD 2607
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2238-2475 |
6.56e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2238 NKIEEENQRL--IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEA 2315
Cdd:COG4942 20 DAAAEAEAELeqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2316 SRLKAE-AEMLQKQKDLAQEQAQKLL---EDKQLMQQRLEeeteeYHKSLEVERKRQleimaeAERLRLQVSQLSEAQAR 2391
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLlspEDFLDAVRRLQ-----YLKYLAPARREQ------AEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2392 AEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMAD 2471
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....
gi 1988774682 2472 AQQK 2475
Cdd:COG4942 249 AALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2424-2601 |
7.05e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2424 VERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQ-------QTFMTEKEMLl 2496
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfSDFLDRLSAL- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2497 kkEKLIEDEKKRLESQfeeevkkaKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQ 2576
Cdd:COG3883 125 --SKIADADADLLEEL--------KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
170 180
....*....|....*....|....*
gi 1988774682 2577 ERILAEENQKLREKLQQLEDAQKDQ 2601
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
156-263 |
7.10e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 53.56 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 156 QSEDMTAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQ-QTNLENLEQAFSVAEKDLGV 234
Cdd:cd21313 3 DAKKQTPKQRLLGWIQ---NKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDpQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1988774682 235 TRLLDPEDVDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4033-4069 |
7.52e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 7.52e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1988774682 4033 IRLLEAQIATGGIIDPEESHRLPVEVAYNRGFFDEEM 4069
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1531-1713 |
7.80e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 58.35 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1531 KQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAhEAAQKSAAAELQSKhmsfaektskleeslkQEHGAVLQLQQ 1610
Cdd:COG2268 180 EDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIA-QANREAEEAELEQE----------------REIETARIAEA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1611 EAERLKKQQE---DAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALK 1687
Cdd:COG2268 243 EAELAKKKAEerrEAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAE 322
|
170 180
....*....|....*....|....*.
gi 1988774682 1688 QKEMAEEELERQRKIAESTAQQKLTA 1713
Cdd:COG2268 323 AEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1422-1580 |
9.38e-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: 56.09 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1422 LELQEL---KNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQD-- 1496
Cdd:COG1579 10 LDLQELdseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1497 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKL--RMQAEEAERQVKQAEIEKE-KQIKVAHEAAQ 1573
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELeaELEEKKAELDEELAELEAElEELEAEREELA 169
|
....*..
gi 1988774682 1574 KSAAAEL 1580
Cdd:COG1579 170 AKIPPEL 176
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2152-2526 |
1.04e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2152 QKQQADTEMAKHKKLAEQTLKQKF-----QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKV 2226
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQDWNKELkselkNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2227 KVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKlaedaarlsveaqeaarlrqiaedDLNQQRALAEKMLK 2306
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK------------------------DEQIKKLQQEKELL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2307 EKmqaiqEASRLKAEAEMLQKQ-KDLAQEQAQKLLEDKQLMQQR--LEEETEEYHKSLEVER------KRQLEI-MAEAE 2376
Cdd:TIGR04523 425 EK-----EIERLKETIIKNNSEiKDLTNQDSVKELIIKNLDNTResLETQLKVLSRSINKIKqnleqkQKELKSkEKELK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2377 RLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFE--RLNTSKEADDLRKAIADLENEKAR 2454
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKS 579
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 2455 LKKEAEELQNKSKEMADAQQ---KKIEhEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDE 2526
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKdliKEIE-EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1343-1540 |
1.14e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.51 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1343 QRRLDDEEKaaEKLKAEERKKMAEMQA--ELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKreiAAVDAEKQktni 1420
Cdd:PRK09510 100 QERLKQLEK--ERLAAQEQKKQAEEAAkqAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK---AAAEAKKK---- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1421 qlELQELKNLSEQQIKDKsqqvdealhsrtkieeeirliriqLETTEKQKYTAESELKQLRDRAAEAEKLRKlAQDEAEK 1500
Cdd:PRK09510 171 --AEAEAAKKAAAEAKKK------------------------AEAEAAAKAAAEAKKKAEAEAKKKAAAEAK-KKAAAEA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1988774682 1501 LRKQVSEETQKKRQAEEELKRKSeAEKEAAKQKQKALEDL 1540
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKA-AEKAAAAKAAAEVDDL 262
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2199-2384 |
1.17e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2199 DEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSV 2278
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2279 EAQEAARLRQIAE--------DDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRL 2350
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|....
gi 1988774682 2351 EEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQ 2384
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2340-2601 |
1.22e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 57.24 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2340 LEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLheteiatqe 2419
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ--------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2420 kmtvvERLEFERLNTSKEADDLRKAIADLENEKARLK--KEAEELQNKSKEMaDAQQKKIEHEKTVLQQTFMTEKEMLLK 2497
Cdd:pfam13868 99 -----EREQMDEIVERIQEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKEL-EKEEEREEDERILEYLKEKAEREEERE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2498 KEKL-IEDEKKRLESQFEEEVKKAKALKDEQE---------------RQKQQMEQEKK-TLQATMDAALSKQKEAEEEML 2560
Cdd:pfam13868 173 AEREeIEEEKEREIARLRAQQEKAQDEKAERDelraklyqeeqerkeRQKEREEAEKKaRQRQELQQAREEQIELKERRL 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1988774682 2561 RKQKEMQELERQRL-----EQERILAEENQKLREKLQQLEDAQKDQ 2601
Cdd:pfam13868 253 AEEAEREEEEFERMlrkqaEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1349-1709 |
1.33e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 57.65 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1349 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQL--ELQE 1426
Cdd:pfam15709 172 ERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERNLEVaaELSG 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1427 LKNLSEQQIKDKSQQVDEALHSRT-------KIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAE 1499
Cdd:pfam15709 252 PDVINSKETEDASERGAFSSDSVVedpwlssKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1500 K-LRKQVSEETQKKRQAEEELKRKSEAEKEaaKQKQKALEDLEKLRMQAEEaERQVKQAEIEKEKQiKVAHEAAQKSAAA 1578
Cdd:pfam15709 332 KaSRDRLRAERAEMRRLEVERKRREQEEQR--RLQQEQLERAEKMREELEL-EQQRRFEEIRLRKQ-RLEEERQRQEEEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1579 ELQSKHMSFAEKTSKLEEslKQEHGAVLQLQQeaerlKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEahkkt 1658
Cdd:pfam15709 408 RKQRLQLQAAQERARQQQ--EEFRRKLQELQR-----KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE----- 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 1659 laqeEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQ 1709
Cdd:pfam15709 476 ----RLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1340-1631 |
1.36e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 57.57 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1340 TDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHA---KAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQ 1416
Cdd:pfam02029 52 PSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIAdekESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1417 KTNIQlelqeLKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQD 1496
Cdd:pfam02029 132 ETEIR-----EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1497 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQvkqaEIEKEKQikvaheaAQKSA 1576
Cdd:pfam02029 207 VKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESE----EFEKLRQ-------KQQEA 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 1577 AAELQSKHMSFAEKTSKLEESLKQEHgavlqlQQEAERLKKQQEDAENSREEAEK 1631
Cdd:pfam02029 276 ELELEELKKKREERRKLLEEEEQRRK------QEEAERKLREEEEKRRMKEEIER 324
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1421-1757 |
1.46e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.22 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1421 QLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKlrklaqdEAEK 1500
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE-------ELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1501 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAEL 1580
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1581 QSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLA 1660
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1661 QEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYR 1740
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330
....*....|....*..
gi 1988774682 1741 LKNEVAAAQQQRKQLED 1757
Cdd:COG4372 325 AKKLELALAILLAELAD 341
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
41-148 |
1.60e-07 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 53.08 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 41 ERDRVQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 111
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnkvNKPPYPKLGANMK--KLENCNYAVEL 93
|
90 100 110
....*....|....*....|....*....|....*...
gi 1988774682 112 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21331 94 GKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2155-2357 |
1.78e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2155 QADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELL 2234
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2235 K-----------------------------LKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEdaarLSVEAQEAAR 2285
Cdd:COG3883 93 RalyrsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 2286 LRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEY 2357
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2269-2611 |
2.01e-07 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 57.04 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2269 LAEDAARLSVEAQEAARLRQIAEDDLNQQRA-------LAEKMLKEKMQAIQEA-----------SRLKAEAEMLQKQKD 2330
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAkfkelylAKEEDLKRQNAVLQEAqveldalqnqlALARAEMENIKAVAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2331 LAQEQAQKLLED------------KQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAER----LRLQVSQlSEAQARAEE 2394
Cdd:pfam03528 86 VSENTKQEAIDEvksqwqeevaslQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEReiadLRRRLSE-GQEEENLED 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2395 EAKKFKKQADKVATRL--HETEIAT--------QEKMTVVERLEFERLNTSKEAD-----DLRKAIADLENEKARLKKEA 2459
Cdd:pfam03528 165 EMKKAQEDAEKLRSVVmpMEKEIAAlkaklteaEDKIKELEASKMKELNHYLEAEkscrtDLEMYVAVLNTQKSVLQEDA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2460 EELQNKSKEMADA-QQKKIEHekTVLQQTFMTEKEMLLKKEKLIEDEKKRLESqfeeevkkakALKDEQERQKQQmeqek 2538
Cdd:pfam03528 245 EKLRKELHEVCHLlEQERQQH--NQLKHTWQKANDQFLESQRLLMRDMQRMES----------VLTSEQLRQVEE----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2539 ktlqatmdaaLSKQKEAEEEMLRKQKEMQELERQRLEQERILA-------EENQKLREKLQQLEDAQKDQHTRETDKVLH 2611
Cdd:pfam03528 308 ----------IKKKDQEEHKRARTHKEKETLKSDREHTVSIHAvfspagvETSAPLSNVEEQINSAHGSVHSLDTDVVLG 377
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2232-2595 |
2.10e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2232 ELLKLKNKIEEENQRLIkkdkdSTQKLLAEEAENMRKLAED----AARLSVeAQEAARLR-QI--AEDDLNqqrALAEKm 2304
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLV-----EMARELAELNEAESDLEQDyqaaSDHLNL-VQTALRQQeKIerYQADLE---ELEER- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2305 LKEKMQAIQEASRlkaEAEMLQKQKDLAQEQAQKLleDKQL--MQQRLEEETE---EYHKSLE-VERKRQLeimaeaerl 2378
Cdd:PRK04863 364 LEEQNEVVEEADE---QQEENEARAEAAEEEVDEL--KSQLadYQQALDVQQTraiQYQQAVQaLERAKQL--------- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2379 rLQVSQLSeaqaraeeeakkfkkqADKVATRLHEteIATQEKMTVVERLEFE-RLNTSKEADD--------LRKAIADLE 2449
Cdd:PRK04863 430 -CGLPDLT----------------ADNAEDWLEE--FQAKEQEATEELLSLEqKLSVAQAAHSqfeqayqlVRKIAGEVS 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2450 NEKA------------RLKKEAEELQNKSKEMADAQQKKIEHEKTV-LQQTFMTEKEMLLKKEKLIEDEKKRLESQFE-- 2514
Cdd:PRK04863 491 RSEAwdvarellrrlrEQRHLAEQLQQLRMRLSELEQRLRQQQRAErLLAEFCKRLGKNLDDEDELEQLQEELEARLEsl 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2515 -EEVKKAKALKDEQERQKQQMEQEKKTLQA------TMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKL 2587
Cdd:PRK04863 571 sESVSEARERRMALRQQLEQLQARIQRLAArapawlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
....*...
gi 1988774682 2588 REKLQQLE 2595
Cdd:PRK04863 651 AARKQALD 658
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1432-1746 |
2.14e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1432 EQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQK 1511
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1512 KRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKT 1591
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1592 SKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEA 1671
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 1672 EREAKKRAKAEESALKQKEMAEEELERQRKIaesTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVA 1746
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALE---DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDV 355
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1474-1862 |
2.28e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 56.83 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1474 ESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQkqkALEDLEKLRMQAEEAERQ 1553
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ---SREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1554 vkQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKtskleeslkqehgaVLQLQQEAERLKKQQEDAENSREEAEKEl 1633
Cdd:pfam07888 110 --SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQR--------------VLERETELERMKERAKKAGAQRKEEEAE- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1634 ekwrqkaNEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEeelerQRKIAESTAqqkltA 1713
Cdd:pfam07888 173 -------RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA-----HRKEAENEA-----L 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1714 EQELIRLRADFDNAEQQRSLLEDELyrlknEVAAAQQQRKQLEDELAKVRS-EMDILIQLKTKAEKETMSNTEKSKQLL- 1791
Cdd:pfam07888 236 LEELRSLQERLNASERKVEGLGEEL-----SSMAAQRDRTQAELHQARLQAaQLTLQLADASLALREGRARWAQERETLq 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774682 1792 ---EAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEklaAISEATRLKTEAEIALKEKE 1862
Cdd:pfam07888 311 qsaEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSE---SRRELQELKASLRVAQKEKE 381
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1434-1715 |
2.31e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 57.27 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1434 QIKDKSQQVDEAlhsrtKIEEEIRLIRIQlettekqkytaeselkqlRDRAAEAEKLRKLAQDEAEKLRKQVSE--ETQK 1511
Cdd:PRK05035 440 AIEQEKKKAEEA-----KARFEARQARLE------------------REKAAREARHKKAAEARAAKDKDAVAAalARVK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1512 KRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAElqskhmsfAEKT 1591
Cdd:PRK05035 497 AKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQ--------QAAN 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1592 SKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKwRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEA 1671
Cdd:PRK05035 569 AEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDP-KKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA 647
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1988774682 1672 EREAKKRAKAEESALKQKEMAEEELERQRKIAESTA----QQKLTAEQ 1715
Cdd:PRK05035 648 VAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAiaraKAKKAAQQ 695
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1413-1595 |
2.36e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.39 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1413 AEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETtEKQKYTAESELKQLRDRAAEAEKLRk 1492
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAA-EKAAKQAEQAAKQAEEKQKQAEEAK- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1493 lAQDEAEKLRKqvsEETQKKRQAEEELKRKSEAE---KEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKvah 1569
Cdd:TIGR02794 126 -AKQAAEAKAK---AEAEAERKAKEEAAKQAEEEakaKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKA--- 198
|
170 180
....*....|....*....|....*.
gi 1988774682 1570 EAAQKSAAAELQSKHMSFAEKTSKLE 1595
Cdd:TIGR02794 199 EAAKAKAAAEAAAKAEAEAAAAAAAE 224
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1474-1913 |
2.47e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 57.06 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1474 ESELKQLRDRAAEAEKLRKLAQDEAEK----LRKQVSEETQKKRQAEEELK--RKSEAEKEAAKQKQKaleDLEKLRMQA 1547
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKkasaLKRQLDRESDRNQELQKRIRllEKREAEAEEALREQA---ELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1548 EEAERQVKQaeiEKEKQIKVAHE--AAQKSAAAEL----QSKHMSFAEKTSKLEEsLKQEHGAVLQLQQEAERLKKQQED 1621
Cdd:pfam05557 85 LEALNKKLN---EKESQLADAREviSCLKNELSELrrqiQRAELELQSTNSELEE-LQERLDLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1622 AENSREEAE---KELEKWRQKAN-----------EALRL-RLQAEDEAHK------------KTLAQEEAEKQKEEAERE 1674
Cdd:pfam05557 161 QQSSLAEAEqriKELEFEIQSQEqdseivknsksELARIpELEKELERLRehnkhlnenienKLLLKEEVEDLKRKLERE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1675 AKKRAKAEESALKqKEMAEEELERQRKIAESTA-----------------QQKLTAEQELIRLRADFDNAEQQRSLLEDE 1737
Cdd:pfam05557 241 EKYREEAATLELE-KEKLEQELQSWVKLAQDTGlnlrspedlsrrieqlqQREIVLKEENSSLTSSARQLEKARRELEQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1738 LYRLKNEVAAAQQQRKQ-------LEDELAKVRSEMDILIQLKTKAEKEtMSNTEKSKQLLEaeaaKMKDLAEEASRLRA 1810
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRhkalvrrLQRRVLLLTKERDGYRAILESYDKE-LTMSNYSPQLLE----RIEEAEDMTQKMQA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1811 ISEEAKHQRQIAEEEAARQRAEA---ERILK-----EKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQrkaL 1882
Cdd:pfam05557 395 HNEEMEAQLSVAEEELGGYKQQAqtlERELQalrqqESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEME---L 471
|
490 500 510
....*....|....*....|....*....|..
gi 1988774682 1883 EDQASQHKQEIEE-KIVQLKKSSEAEMERQKA 1913
Cdd:pfam05557 472 ERRCLQGDYDPKKtKVLHLSMNPAAEAYQQRK 503
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
989-1551 |
2.48e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 989 SELKDLRLRIEDCEAG-TVARIRKPVEKEPLKEYIQKTTEQKKVQGELDGLKKDL-----------DKVSVKTQEVLAsp 1056
Cdd:PRK02224 213 SELAELDEEIERYEEQrEQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaeterereelaEEVRDLRERLEE-- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1057 qpsasapvLRSELDltvqkmdhaHMLSSVYLEKL--KTVEMVIRNTQGAEgvlKQYEDCLREVHTVPSDV-KEVETYRAK 1133
Cdd:PRK02224 291 --------LEEERD---------DLLAEAGLDDAdaEAVEARREELEDRD---EELRDRLEECRVAAQAHnEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1134 LKKMRTEAEDEQPVFDSLEEELKKASAVSDkmvrvhsERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLgrqlgy 1213
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVE-------DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL------ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1214 yRESYDwlirwiaDAKQRQEKIQAvpitDSKTLKEQLAQEKKLLEEieqnkDKVDECQKYAK--AYIDTIKDYELQ---L 1288
Cdd:PRK02224 418 -REERD-------ELREREAELEA----TLRTARERVEEAEALLEA-----GKCPECGQPVEgsPHVETIEEDRERveeL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1289 VAYKAQVEPLVSPLKKtKLDSASDniiqeYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLkaeeRKKMAEMQ 1368
Cdd:PRK02224 481 EAELEDLEEEVEEVEE-RLERAED-----LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL----RERAAELE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1369 AEldkqkqlAEAHAKAIAKAEKEAQElklkmqeevsKREIAAvDAEKQKTNIQLELQELKNLSEQQ--IKDKSQQVDEAL 1446
Cdd:PRK02224 551 AE-------AEEKREAAAEAEEEAEE----------AREEVA-ELNSKLAELKERIESLERIRTLLaaIADAEDEIERLR 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1447 HSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKlrklaqDEAEKLRKQVSEETQKKRQAEEELK------ 1520
Cdd:PRK02224 613 EKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDK------ERAEEYLEQVEEKLDELREERDDLQaeigav 686
|
570 580 590
....*....|....*....|....*....|....*
gi 1988774682 1521 RKSEAEKEAAKQKQKALED----LEKLRMQAEEAE 1551
Cdd:PRK02224 687 ENELEELEELRERREALENrveaLEALYDEAEELE 721
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1686-1919 |
2.55e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1686 LKQKEMAEEELERQRKIAESTAQQKLTAEQElirlradfdnAEQQRsLLEDELYRLknevaAAQQQRKQLEDelakvrse 1765
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQA----------AEQER-LKQLEKERL-----AAQEQKKQAEE-------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1766 mdiliQLKTKAEKETMSNTEKSKQlleAEAAKMKdLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILK-EKLAAI 1844
Cdd:PRK09510 123 -----AAKQAALKQKQAEEAAAKA---AAAAKAK-AEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKaEAEAAA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 1845 SEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDqasqhKQEIEEKIVQLKKSSEAEMERQKAIVDDTL 1919
Cdd:PRK09510 194 KAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAE-----AKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2172-2593 |
2.63e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2172 KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQM----EELLKLKNKIEEENQRL 2247
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVedrrEEIEELEEEIEELRERF 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2248 --IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAE---------------------DDLNQQRALAEKM 2304
Cdd:PRK02224 401 gdAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpvegsphvETIEEDRERVEEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2305 LKEKMQAIQEASRLKAEAEMLQKQKDLAQEqAQKLLEDKQLMQQRLEEETEEyhksleVERKRQleimaEAERLRLQVSQ 2384
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVEAEDR-IERLEERREDLEELIAERRET------IEEKRE-----RAEELRERAAE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2385 LSEAQARAEEEAKKFKKQADKVATRLHETEiatQEKMTVVERLefERLNTSKEADDlrkAIADLENEKARLKKEAEELQN 2464
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELN---SKLAELKERI--ESLERIRTLLA---AIADAEDEIERLREKREALAE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2465 KSKEmadaqqkkiehektvlqqtfmtekemllKKEKLIE--DEKKRLESQFEEE-VKKAKALKDEQERQKQQME------ 2535
Cdd:PRK02224 621 LNDE----------------------------RRERLAEkrERKRELEAEFDEArIEEAREDKERAEEYLEQVEekldel 672
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 2536 -QEKKTLQATMDAALSKQKEAEEemLRKQKEMQELERQRLEQERILAEENQ----KLREKLQQ 2593
Cdd:PRK02224 673 rEERDDLQAEIGAVENELEELEE--LRERREALENRVEALEALYDEAEELEsmygDLRAELRQ 733
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2004-2356 |
2.66e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 56.83 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2004 RQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKcsaAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLA 2083
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ---SREKHEELEEKYKELSASSEELSEEKDALLAQR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2084 KEAEAAKEKAEREAALLRQQAEEAERQktaaeeeAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKH 2163
Cdd:pfam07888 125 AAHEARIRELEEDIKTLTQRVLERETE-------LERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2164 KKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQR-----------------LKDEVDDAVKQRGQVEEELFKV 2226
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrslqerlnaserkvegLGEELSSMAAQRDRTQAELHQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2227 KVQMEEL---LKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEK 2303
Cdd:pfam07888 278 RLQAAQLtlqLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRV 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 2304 MLKEKMQAIQEasrLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEE 2356
Cdd:pfam07888 358 QLSESRRELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1125-1558 |
2.84e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 57.36 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1125 KEVETYRAKLKKMRTEAEDEQpvfDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQREL 1204
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKL---KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1205 EQLGRQLGyyresydwlirwIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTI-KD 1283
Cdd:TIGR00606 768 EEQETLLG------------TIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQeKQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1284 YELQLVAYKAQVeplvsplkKTKLDSASDNIIQEYvtlrtrYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKaeerkK 1363
Cdd:TIGR00606 836 HELDTVVSKIEL--------NRKLIQDQQEQIQHL------KSKTNELKSEKLQIGTNLQRRQQFEEQLVELST-----E 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1364 MAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNL----SEQQIKDKS 1439
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgKDDYLKQKE 976
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1440 Q-------QVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKK 1512
Cdd:TIGR00606 977 TelntvnaQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEH 1056
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1988774682 1513 RQAEEELKRKSEAEKEAAKQkQKALEDlEKLRMQAEEAERQVKQAE 1558
Cdd:TIGR00606 1057 QKLEENIDLIKRNHVLALGR-QKGYEK-EIKHFKKELREPQFRDAE 1100
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1592-1916 |
3.05e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 56.44 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1592 SKLEESLkQEHGAVLQLQQEAERlkkqqeDAENSREEAEKELEKWRQKANEaLRLRLQAEDEAHKKTLAQEEAEKQKEEA 1671
Cdd:pfam07888 34 NRLEECL-QERAELLQAQEAANR------QREKEKERYKRDREQWERQRRE-LESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1672 EREAKKRAKAEESAL-KQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1750
Cdd:pfam07888 106 LSASSEELSEEKDALlAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1751 QRKQLEDELAKVRSEMD----ILIQLKTKAEKETMSNTEKSKQLLEAEAAKmKDLAEEASRLrAISEEAKH--QRQIAEE 1824
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALL-EELRSLQERL-NASERKVEglGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1825 EAARQRAEAEriLKEKLAAISEATRLKTEAEIALKEkeaenERLRRQAEDEAYQRKALEDQasQHKQEIEEKIVQLKKS- 1903
Cdd:pfam07888 264 AAQRDRTQAE--LHQARLQAAQLTLQLADASLALRE-----GRARWAQERETLQQSAEADK--DRIEKLSAELQRLEERl 334
|
330
....*....|...
gi 1988774682 1904 SEAEMERQKAIVD 1916
Cdd:pfam07888 335 QEERMEREKLEVE 347
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1436-1855 |
3.28e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1436 KDKSQQVDEALHSR--------TKIEEEIRLIRIQ--LETTEKQKYTAESELKQLRDRAAeaeklrkLAQdeaEKLRKQv 1505
Cdd:PRK04863 279 NERRVHLEEALELRrelytsrrQLAAEQYRLVEMAreLAELNEAESDLEQDYQAASDHLN-------LVQ---TALRQQ- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1506 seetQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVK----------QAEIEKEKQIKVAHEAAQKS 1575
Cdd:PRK04863 348 ----EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDelksqladyqQALDVQQTRAIQYQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1576 AAAELQSKHMSFAEKtsKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAlrLRLQAEDEAh 1655
Cdd:PRK04863 424 ERAKQLCGLPDLTAD--NAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEV--SRSEAWDVA- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1656 kktlaqeeaekqkeeaeREAKKRAKaeesalKQKEMAEEELERQRKIAEstAQQKLTAEQELIRLRADF----------- 1724
Cdd:PRK04863 499 -----------------RELLRRLR------EQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFckrlgknldde 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1725 DNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELakvrSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEE 1804
Cdd:PRK04863 554 DELEQLQEELEARLESLSESVSEARERRMALRQQL----EQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDV 629
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 1805 ASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAE 1855
Cdd:PRK04863 630 TEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1368-1830 |
3.54e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 56.69 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1368 QAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQktniqleLQELKNLSEQQIKDKSQQVDEA-L 1446
Cdd:pfam09731 81 EPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKA-------LEEVLKEAISKAESATAVAKEAkD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1447 HSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAE--AEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKrKSE 1524
Cdd:pfam09731 154 DAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEklKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLD-NVE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1525 AEKEAAKQKQKALEDLEKLrmqaEEAERQVKQAEIEKekqikvaheaAQKSAAAELQSKHMSFAEKTSKLEESLKQEhga 1604
Cdd:pfam09731 233 EKVEKAQSLAKLVDQYKEL----VASERIVFQQELVS----------IFPDIIPVLKEDNLLSNDDLNSLIAHAHRE--- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1605 VLQLQQEAERLKKQ-QEDAENSREEAEKELEKwrqkANEALRLRLQAEDEAHKKTLaqeeaekqkeeaerEAKKRAKAEE 1683
Cdd:pfam09731 296 IDQLSKKLAELKKReEKHIERALEKQKEELDK----LAEELSARLEEVRAADEAQL--------------RLEFEREREE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1684 SALKQKEMAEEELERQRKIAESTAQQKL-TAEQEL-IRLRADFDNA-EQQRSLLE---DELYRLKNEVAAAQQQRKQLED 1757
Cdd:pfam09731 358 IRESYEEKLRTELERQAEAHEEHLKDVLvEQEIELqREFLQDIKEKvEEERAGRLlklNELLANLKGLEKATSSHSEVED 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774682 1758 ELAKVRSemdilIQLKTKAEKETM--SNTEKSKQLLEAEAAKMKDLAEE----ASRLRAISEEAKhQRQIAEEEAARQR 1830
Cdd:pfam09731 438 ENRKAQQ-----LWLAVEALRSTLedGSADSRPRPLVRELKALKELASDdevvKAALASLPEEAY-QRGVYTEAALRER 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1341-1578 |
3.65e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1341 DTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELklkmqeevsKREIAAVDAEKQKTNI 1420
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL---------QAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1421 QLElqelKNLSEQQIKDKSQQVDEALHSRTKIEEEIRliriQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 1500
Cdd:COG3883 87 ELG----ERARALYRSGGSVSYLDVLLGSESFSDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774682 1501 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAA 1578
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1683-2315 |
3.92e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1683 ESALKQKEMAEEELERQRKIAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKV 1762
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARERL---AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1763 RSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEE-ASRLRAISEEAKHQRQIAEE---EAARQRAEAERILK 1838
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARlEALLAALGLPLPASAEEFAAlraEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1839 EKLAAISEATRLKTEAEIALKEKEAENERLRRQAE--DEAYQ--RKALEDQASQHKQEI----EEkiVQLKkssEAEMER 1910
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKSniPARLLalRDALAEALGLDEAELpfvgEL--IEVR---PEEERW 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1911 QKAI------------VDDTLKQ--RRVVEEEIRILKLNFEKASSGKLDLELE-------LNKLkniadETQQSKIRAEE 1969
Cdd:COG4913 477 RGAIervlggfaltllVPPEHYAaaLRWVNRLHLRGRLVYERVRTGLPDPERPrldpdslAGKL-----DFKPHPFRAWL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1970 EAEKLRKLALEeekrrreaeekvkkiaaaeeeaarqRKAALEELERLRK--------KAEEARKQKDEADKEAEKQiVVA 2041
Cdd:COG4913 552 EAELGRRFDYV-------------------------CVDSPEELRRHPRaitragqvKGNGTRHEKDDRRRIRSRY-VLG 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2042 QQAAQKCSAAEQQvqsvlAQQIEDSITQkklkeeyekakklakeaeaakekaereaalLRQQAEEAERQKtaaeeeaanq 2121
Cdd:COG4913 606 FDNRAKLAALEAE-----LAELEEELAE------------------------------AEERLEALEAEL---------- 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2122 AKAQEDAERLRKEAEFeaakraqaeaaalmQKQQADTEMAkHKKLAEqtlkqkfqVEQELTKvklkLDETDKQKSVLDEE 2201
Cdd:COG4913 641 DALQERREALQRLAEY--------------SWDEIDVASA-EREIAE--------LEAELER----LDASSDDLAALEEQ 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2202 LQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLknkIEEENQRLIKKDKDSTQKLLAEeaenmrkLAEDAARLSVEAQ 2281
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEE---LDELQDRLEAAEDLARLELRAL-------LEERFAAALGDAV 763
|
650 660 670
....*....|....*....|....*....|....*.
gi 1988774682 2282 EAARLRQIAE--DDLNQQRALAEKMLKEKMQAIQEA 2315
Cdd:COG4913 764 ERELRENLEEriDALRARLNRAEEELERAMRAFNRE 799
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1673-2110 |
4.35e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 56.07 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1673 REAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 1752
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1753 KQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAE 1832
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1833 AERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQK 1912
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1913 AIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKV 1992
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1993 KKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKL 2072
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430
....*....|....*....|....*....|....*...
gi 1988774682 2073 KEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQ 2110
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAA 519
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1379-1736 |
4.44e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.03 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1379 EAHAKAIAKA-EKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSeqqikDKSQQVDEALHSRTKIEEEIR 1457
Cdd:pfam02029 1 IEDEEEAARErRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG-----QGGLDEEEAFLDRTAKREERR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1458 LIRIQlETTEKQKytaESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE-----AAKQ 1532
Cdd:pfam02029 76 QKRLQ-EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQEnkwstEVRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1533 KQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKhmSFAEKTSKLEESLKQEHGAVLQLQQEA 1612
Cdd:pfam02029 152 AEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKR--GHPEVKSQNGEEEVTKLKVTTKRRQGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1613 ERLKKQQEDAENSREEAEKELEKWRQKANEALRlrlqAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEEsalkQKEMA 1692
Cdd:pfam02029 230 LSQSQEREEEAEVFLEAEQKLEELRRRRQEKES----EEFEKLRQKQQEAELELEELKKKREERRKLLEEE----EQRRK 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1988774682 1693 EEELERQRKIAESTAQQKltaeQELIRLRAdfDNAEQQRSLLED 1736
Cdd:pfam02029 302 QEEAERKLREEEEKRRMK----EEIERRRA--EAAEKRQKLPED 339
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1472-1708 |
6.67e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1472 TAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKrkseaekeaakQKQKALEDLEKlrmQAEEAE 1551
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-----------ALQAEIDKLQA---EIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1552 RQVKQAEIEKEKQIKVAHEAAQKSAAAE--LQSKHMS-FAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREE 1628
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYLDvlLGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1629 AEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQ 1708
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1230-1652 |
6.80e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.52 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1230 QRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAY---KAQVEPLVSPLKK-T 1305
Cdd:pfam05557 121 QRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQeqdSEIVKNSKSELARiP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1306 KLDSASDNIIQEYVTLRTRYSELMTLTSQyikfITDTQRRLDDEEKAAEKLKAEERKKmAEMQAELDKQKQLAEAHAKAI 1385
Cdd:pfam05557 201 ELEKELERLREHNKHLNENIENKLLLKEE----VEDLKRKLEREEKYREEAATLELEK-EKLEQELQSWVKLAQDTGLNL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1386 AKAEKEAQELKLKMQEE-VSKREIAAVDAE-KQKTNIQLELQE-----LKNLSEQQIKDKSQqvdEALHSRTK-----IE 1453
Cdd:pfam05557 276 RSPEDLSRRIEQLQQREiVLKEENSSLTSSaRQLEKARRELEQelaqyLKKIEDLNKKLKRH---KALVRRLQrrvllLT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1454 EEIRLIRIQLETTEKQKYTAESELKQLRdRAAEAEKLRKLAQDEAEKLRKQVS----EETQKKRQA-----EEELKRKSE 1524
Cdd:pfam05557 353 KERDGYRAILESYDKELTMSNYSPQLLE-RIEEAEDMTQKMQAHNEEMEAQLSvaeeELGGYKQQAqtlerELQALRQQE 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1525 AEKEAAKQKQKALE---DLEKLRMQAEEAERQVKQAEIEKEKqikvaHEAAQKSAAAELQSKHMSfAEKTSKLEESLKQE 1601
Cdd:pfam05557 432 SLADPSYSKEEVDSlrrKLETLELERQRLREQKNELEMELER-----RCLQGDYDPKKTKVLHLS-MNPAAEAYQQRKNQ 505
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 1602 HGavlQLQQEAERLKKQQEDAENSREEAEKELEKWRQKAN-EALRLRLQAED 1652
Cdd:pfam05557 506 LE---KLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFkEVLDLRKELES 554
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4136-4164 |
6.96e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.48 E-value: 6.96e-07
10 20
....*....|....*....|....*....
gi 1988774682 4136 IVDPETGKEMTVYEAYRKGLIDHQTYLEL 4164
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1674-1930 |
7.91e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.47 E-value: 7.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1674 EAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRadfdnaeQQRSLLEDELYRLKNEVAAAQQQRK 1753
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQK-------ELEQRAAAEKAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1754 QLEDELAKVRSEMDILIQLKTKAEKETMSNTEKskqllEAEAAKMKDLAEEASRlraiseEAKHQRQIAEEEAaRQRAEA 1833
Cdd:TIGR02794 118 QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK-----QAEEEAKAKAAAEAKK------KAEEAKKKAEAEA-KAKAEA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1834 ERILK-EKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQK 1912
Cdd:TIGR02794 186 EAKAKaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYA 265
|
250
....*....|....*...
gi 1988774682 1913 AIVDDTLKQRRVVEEEIR 1930
Cdd:TIGR02794 266 AIIQQAIQQNLYDDPSFR 283
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1347-1592 |
7.94e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1347 DDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEevSKREIAAVDAEKQKTNIQLElqe 1426
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK--LQAEIAEAEAEIEERREELG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1427 lKNLSEQQIKDKSQQVDEALHSRTKIEEEIRliRIQLettekqkytaeseLKQLRDRAAEAEKLRKLAQDEAEKLRKQVS 1506
Cdd:COG3883 90 -ERARALYRSGGSVSYLDVLLGSESFSDFLD--RLSA-------------LSKIADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1507 EETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMS 1586
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
....*.
gi 1988774682 1587 FAEKTS 1592
Cdd:COG3883 234 AAAAAA 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2321-2599 |
8.08e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2321 EAEMLQKQKDLAQE---QAQKLLED-KQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRlqvsQLSEAQARAEEEA 2396
Cdd:PTZ00121 1078 DFDFDAKEDNRADEateEAFGKAEEaKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR----KAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2397 KKFKKQADKvATRLHETEIATQEKMTVVER--LEFERLNTSKEADDLRKAIADLENEKARLKKE---------------A 2459
Cdd:PTZ00121 1154 VEIARKAED-ARKAEEARKAEDAKKAEAARkaEEVRKAEELRKAEDARKAEAARKAEEERKAEEarkaedakkaeavkkA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2460 EELQNKSKEMADAQQKKIEHEKTVLQQTFM---TEKEMLLKKE--------KLIEDEKKRLESQFEEEVKKAKALKDEQE 2528
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMahfARRQAAIKAEearkadelKKAEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2529 RQKQQMEQEKKTLQATMDAALSKQK---------------EAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQ 2593
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKaeeakkaaeaakaeaEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
....*.
gi 1988774682 2594 LEDAQK 2599
Cdd:PTZ00121 1393 ADEAKK 1398
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1725-1973 |
8.19e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.47 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1725 DNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLE-AEAAKMKDLAE 1803
Cdd:TIGR02794 29 PEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQrAAAEKAAKQAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1804 EASRL-RAISEEAKHQRQIAEEEAARQR-AEAERILKEKLAAISEATRLKTEAEIALKEKEAEnerlRRQAEDEAyqrKA 1881
Cdd:TIGR02794 109 QAAKQaEEKQKQAEEAKAKQAAEAKAKAeAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEA----KKKAEAEA---KA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1882 ledqasqhKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvvEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQ 1961
Cdd:TIGR02794 182 --------KAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEA--EAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGG 251
|
250
....*....|..
gi 1988774682 1962 QSKIRAEEEAEK 1973
Cdd:TIGR02794 252 ARGAAAGSEVDK 263
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1265-1526 |
8.73e-07 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 55.01 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1265 DKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKKTKLD--------SASDNIIQEYVTLRTRYSELMTLTSQYI 1336
Cdd:pfam05262 79 DHILNLRRILAGYLMAAYGYERSDAETIAKFITIYNAVYRGDLDyfkefykeVVTKSLTKENAGLARRYDQWPGKTQIVI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1337 KF--------ITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREI 1408
Cdd:pfam05262 159 PLkknilsgnVSDVDTDSISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADF 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1409 AAVDAEKQKTNIQLELQELKNlSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTaESELKQLRDRAAEAE 1488
Cdd:pfam05262 239 AQDNADKQRDEVRQKQQEAKN-LPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAK-DHKAFDLKQESKASE 316
|
250 260 270
....*....|....*....|....*....|....*...
gi 1988774682 1489 KLRKLAQDEAEKLRKQVSEETQKKRQAEEElKRKSEAE 1526
Cdd:pfam05262 317 KEAEDKELEAQKKREPVAEDLQKTKPQVEA-QPTSLNE 353
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2154-2607 |
8.81e-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: 55.50 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2154 QQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEE- 2232
Cdd:pfam05483 102 KQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREEt 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2233 ---LLKLKNKIEE------------ENQRL-----IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAarlrqiaED 2292
Cdd:pfam05483 182 rqvYMDLNNNIEKmilafeelrvqaENARLemhfkLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEK-------EN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2293 DLNQQRALAEKMlKEKMQAIQEASRLKAE--AEMLQKQKDLAQEqaqklLEDKQLMQQR-------LEEETEEYHKS--- 2360
Cdd:pfam05483 255 KMKDLTFLLEES-RDKANQLEEKTKLQDEnlKELIEKKDHLTKE-----LEDIKMSLQRsmstqkaLEEDLQIATKTicq 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2361 LEVERKRQLEIMAEAERLR-LQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEAD 2439
Cdd:pfam05483 329 LTEEKEAQMEELNKAKAAHsFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2440 DLRKAIAD---LENEKARLKKEAEELQNKSKEMADA-QQKKIEHEKTVLQQTFMTEKEMLLKKEklIEDEKKRLESQfee 2515
Cdd:pfam05483 409 ELKKILAEdekLLDEKKQFEKIAEELKGKEQELIFLlQAREKEIHDLEIQLTAIKTSEEHYLKE--VEDLKTELEKE--- 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2516 evkKAKALKDEQERQKQQMEQEKKTLQAT-MDAALSKQKE-------AEEEMLRKQKEMQELERQ-RLEQERILAEENQK 2586
Cdd:pfam05483 484 ---KLKNIELTAHCDKLLLENKELTQEASdMTLELKKHQEdiinckkQEERMLKQIENLEEKEMNlRDELESVREEFIQK 560
|
490 500
....*....|....*....|.
gi 1988774682 2587 LREKLQQLEDAQKDQHTRETD 2607
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYE 581
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2477-2675 |
8.82e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 55.60 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2477 IEHEKTVLQqtfmTEKEMLlkkEKLIED-EKKRLESqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEA 2555
Cdd:PRK00409 504 IEEAKKLIG----EDKEKL---NELIASlEELEREL--EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2556 EEEMLRKQKEMQEL---ERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDIIHLTtiETTKTVYNGQNv 2632
Cdd:PRK00409 575 AQQAIKEAKKEADEiikELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVG--DEVKYLSLGQK- 651
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1988774682 2633 GDVVDGIDKKPDPLAFDGIRDKVPASRLHELGVLPKKEFDKLK 2675
Cdd:PRK00409 652 GEVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPK 694
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1452-1761 |
9.00e-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: 54.54 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1452 IEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDE-AEKLRKQVsEETQKKRQAEEELKRKseaEKEAA 1530
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyRQELEEQI-EEREQKRQEEYEEKLQ---EREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1531 KQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAV-LQLQ 1609
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIeEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1610 QEAERLKKQQEDAENSREEAEKELEKWRQKANEAlRLRLQAEDEAHKKtlaqeeaeKQKEEAEREAKKRAKAEESALKQK 1689
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDELRAKLYQEEQER-KERQKEREEAEKK--------ARQRQELQQAREEQIELKERRLAE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 1690 EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAK 1761
Cdd:pfam13868 255 EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2170-2577 |
9.88e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.90 E-value: 9.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2170 TLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIK 2249
Cdd:pfam07888 8 TLEEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2250 KDKDSTQKLlaEEAENMRKLAEDA---------ARLSVEAQEAARLRQIAEDdlnqQRALAEKMLKEKMqaiqEASRLKA 2320
Cdd:pfam07888 88 ELRQSREKH--EELEEKYKELSASseelseekdALLAQRAAHEARIRELEED----IKTLTQRVLERET----ELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2321 EAEMLQKQKdlAQEQAQKllEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLseaqaraeeeakkfK 2400
Cdd:pfam07888 158 RAKKAGAQR--KEEEAER--KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL--------------T 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2401 KQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIE-- 2478
Cdd:pfam07888 220 QKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgr 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2479 ----HEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKE 2554
Cdd:pfam07888 300 arwaQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKE 379
|
410 420
....*....|....*....|....*
gi 1988774682 2555 AEEEMLRKQKEMQELER--QRLEQE 2577
Cdd:pfam07888 380 KEQLQAEKQELLEYIRQleQRLETV 404
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1859-2297 |
1.06e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.13 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1859 KEKEAENERLRRQAEDEAyqrkaledqasqHKQEIEEKIVQLKKSSEAEMERQKAIVDDtlkQRRVVEEEIRilklnfek 1938
Cdd:pfam17380 292 KFEKMEQERLRQEKEEKA------------REVERRRKLEEAEKARQAEMDRQAAIYAE---QERMAMERER-------- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1939 assgkldlelELNKLKNIADETQQSKIRAEE---EAEKLRKLaleeekrrreaeekvkkiaaAEEEAARQRKAaleelER 2015
Cdd:pfam17380 349 ----------ELERIRQEERKRELERIRQEEiamEISRMREL--------------------ERLQMERQQKN-----ER 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2016 LRKKAEEARKQKDEadkEAEKQIVVAQQAAQKCSAAEQQVQsvlAQQIEdsitQKKLKEEyekakklakeaeaakekaeR 2095
Cdd:pfam17380 394 VRQELEAARKVKIL---EEERQRKIQQQKVEMEQIRAEQEE---ARQRE----VRRLEEE-------------------R 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2096 EAALLRQQAEEAERQKtaaeeeaANQAKAQEDAERLRKEAEfeaakraqaeaaalMQKQQADtemakhKKLAEQtlKQKF 2175
Cdd:pfam17380 445 AREMERVRLEEQERQQ-------QVERLRQQEEERKRKKLE--------------LEKEKRD------RKRAEE--QRRK 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2176 QVEQELTKVKLKLDETDKQKSVLDEElqrlkdevddavkqrgqveeelfkvkvqMEEllkLKNKIEEENQRLIKKDKDST 2255
Cdd:pfam17380 496 ILEKELEERKQAMIEEERKRKLLEKE----------------------------MEE---RQKAIYEEERRREAEEERRK 544
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1988774682 2256 QKLLAEE---AENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQ 2297
Cdd:pfam17380 545 QQEMEERrriQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1343-1600 |
1.16e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.95 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1343 QRRLDDEekaaeKLKAEERKKMAEmqAELDKQKQLAEAHAKAIAKAEKEAQElklkmqeevskREIAAVDAEKQKTNIQL 1422
Cdd:PRK05035 459 QARLERE-----KAAREARHKKAA--EARAAKDKDAVAAALARVKAKKAAAT-----------QPIVIKAGARPDNSAVI 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1423 ELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRliRIQLETTEKQKYTAESELKQLRDRAAEAEklrKLAQDEAEKLR 1502
Cdd:PRK05035 521 AAREARKAQARARQAEKQAAAAADPKKAAVAAAIA--RAKAKKAAQQAANAEAEEEVDPKKAAVAA---AIARAKAKKAA 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1503 KQVSEETQKKRQAEEELKrKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVK-QAEIEKEKQIKVAHEAAQKSAAAELQ 1581
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPK-KAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAvAAAIARAKARKAAQQQANAEPEEAED 674
|
250
....*....|....*....
gi 1988774682 1582 SKHMSFAEKTSKLEESLKQ 1600
Cdd:PRK05035 675 PKKAAVAAAIARAKAKKAA 693
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1474-1713 |
1.17e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 54.60 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1474 ESELKQLRDRAAEAEKlrKLAQDE-AEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQK--QKALEDLEKLRMQAEEA 1550
Cdd:PRK07735 4 EKDLEDLKKEAARRAK--EEARKRlVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRaaAAAKAKAAALAKQKREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1551 ERQVKQAEIEKEKqiKVAHEAAQKSAAAELQSKHMSFAEKTSklEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAE 1630
Cdd:PRK07735 82 TEEVTEEEKAKAK--AKAAAAAKAKAAALAKQKREGTEEVTE--EEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1631 KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKK-----RAKAEESAL-KQKEM-----AEEELERQ 1699
Cdd:PRK07735 158 EETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKakaaaAAKAKAAALaKQKASqgngdSGDEDAKA 237
|
250
....*....|....
gi 1988774682 1700 RKIAESTAQQKLTA 1713
Cdd:PRK07735 238 KAIAAAKAKAAAAA 251
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1611-2044 |
1.17e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 55.02 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1611 EAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQK- 1689
Cdd:NF033838 56 QKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTl 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1690 EMAEEELERQRKIAEstAQQKLTAEQElirlradfdnaEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVrsemdil 1769
Cdd:NF033838 136 EPGKKVAEATKKVEE--AEKKAKDQKE-----------EDRRNYPTNTYKTLELEIAESDVEVKKAELELVKE------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1770 iqlktkaEKETMSNTEKSKQlleaEAAKMKDLAEEASRLraisEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATR 1849
Cdd:NF033838 196 -------EAKEPRDEEKIKQ----AKAKVESKKAEATRL----EKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1850 LKTEAEIALKEKEAENERLRRQAE--DEAYQRKALEDQASQHKQ---EIEEKIVQLKKSSEAEMERQKaivddtlkqRRV 1924
Cdd:NF033838 261 PKRRAKRGVLGEPATPDKKENDAKssDSSVGEETLPSPSLKPEKkvaEAEKKVEEAKKKAKDQKEEDR---------RNY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1925 VEEEIRILKLNFEKASSGKLDLELELNK--LKNIADETQQSKIRAEEEAEKlrklaleeekrrreaeekvkkiaaaeeea 2002
Cdd:NF033838 332 PTNTYKTLELEIAESDVKVKEAELELVKeeAKEPRNEEKIKQAKAKVESKK----------------------------- 382
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1988774682 2003 arQRKAALEELERLRKKAEEARKQK-DEADKEAEKQIVVAQQA 2044
Cdd:NF033838 383 --AEATRLEKIKTDRKKAEEEAKRKaAEEDKVKEKPAEQPQPA 423
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1335-1916 |
1.20e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.91 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1335 YIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKqlaeaHAKAIAKAEKEAQELKLKMQEEVSKreiaavdAE 1414
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYN-----NLKSALNELSSLEDMKNRYESEIKT-------AE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1415 KQKTNIQLELQELKNLSEQQIKDKSqqvDEALHSRTKIEEEIRLIRiQLETTEKQKYTAESELKQLRDraaeaeKLRKLA 1494
Cdd:PRK01156 263 SDLSMELEKNNYYKELEERHMKIIN---DPVYKNRNYINDYFKYKN-DIENKKQILSNIDAEINKYHA------IIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1495 QDEAEKlrkqvsEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQ--AEIEKEKQIKVAHEAA 1572
Cdd:PRK01156 333 VLQKDY------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERmsAFISEILKIQEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1573 QKSAAAELQSKHMSFAEKTSKLEESLK---------QEHGAVLQLQ------------QEAERLKKQQEDAENSREEAEK 1631
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRalrenldelSRNMEMLNGQsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1632 ELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEEL-ERQRKIAESTAQQK 1710
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIkNRYKSLKLEDLDSK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1711 ltaeqelirlRADFDNAEQQRSLLE-DELYRLKNEVaaaQQQRKQLEDELAKVRSEMDiliqlktkaekETMSNTEKSKQ 1789
Cdd:PRK01156 567 ----------RTSWLNALAVISLIDiETNRSRSNEI---KKQLNDLESRLQEIEIGFP-----------DDKSYIDKSIR 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1790 LLEAEAAKMKDLAEEASRLRAISEEAKhqrqiaeeeaarqraEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLR 1869
Cdd:PRK01156 623 EIENEANNLNNKYNEIQENKILIEKLR---------------GKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSR 687
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1870 RQAED---EAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVD 1916
Cdd:PRK01156 688 KALDDakaNRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGD 737
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1372-1657 |
1.34e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 54.22 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1372 DKQKQLAEAHAKAIAKAEKEAQELKLKMQEEvskrEIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTK 1451
Cdd:PRK07735 2 DPEKDLEDLKKEAARRAKEEARKRLVAKHGA----EISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1452 IEEEIRliriqlETTEKQKYTAESelkqlrdRAAEAEKLRklaqdeAEKLRKQVSEETQkkrQAEEELKRKSEAeKEAAK 1531
Cdd:PRK07735 78 KREGTE------EVTEEEKAKAKA-------KAAAAAKAK------AAALAKQKREGTE---EVTEEEKAAAKA-KAAAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1532 QKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQE 1611
Cdd:PRK07735 135 AKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAK 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1988774682 1612 AERLKKQQEdaenSREEAEKELEKWRQKANEALRLRLQAEDEAHKK 1657
Cdd:PRK07735 215 AAALAKQKA----SQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTK 256
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1474-1574 |
1.42e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.83 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1474 ESELKQLRDRAAEAEKLRKlaqdEAEKLRKQVSEetQKKRQAEEELKRKSEAEKEAAKQ----KQKALEDLEKLR-MQAE 1548
Cdd:PRK00409 526 EELERELEQKAEEAEALLK----EAEKLKEELEE--KKEKLQEEEDKLLEEAEKEAQQAikeaKKEADEIIKELRqLQKG 599
|
90 100
....*....|....*....|....*.
gi 1988774682 1549 EAERQVKQAEIEKEKQIKVAHEAAQK 1574
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEK 625
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1727-1897 |
1.50e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.62 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1727 AEQQRSLLEdeLYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtMSNTEKSKQLLEAEAAKMKDLAEEA- 1805
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLELEIEEVEARIKKYe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1806 SRLRAIS--EEAKH-QRQIaeEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAL 1882
Cdd:COG1579 80 EQLGNVRnnKEYEAlQKEI--ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....*
gi 1988774682 1883 EDQASQHKQEIEEKI 1897
Cdd:COG1579 158 LEELEAEREELAAKI 172
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1349-1646 |
1.75e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 54.09 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1349 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELK 1428
Cdd:pfam06160 87 ALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1429 NLSEQQIKDKSQQVDEALHSRTkIEEEIRLIRI-----QLETT---------------EKQKYT-----AESELKQLRDR 1483
Cdd:pfam06160 167 ELTESGDYLEAREVLEKLEEET-DALEELMEDIpplyeELKTElpdqleelkegyremEEEGYAlehlnVDKEIQQLEEQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1484 AAEAEK-LRKLAQDEAEKLRKQVSEETQK-----------KRQAEEELKRKSEAEKEAAKQKQKALEDLEKL----RMQA 1547
Cdd:pfam06160 246 LEENLAlLENLELDEAEEALEEIEERIDQlydllekevdaKKYVEKNLPEIEDYLEHAEEQNKELKEELERVqqsyTLNE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1548 EEAERqvkQAEIEKE-KQIKVAHEAAQKsaaaELQSKHMSFAEKTSKLEESLKQehgaVLQLQQEAERLKKQQEDAENSR 1626
Cdd:pfam06160 326 NELER---VRGLEKQlEELEKRYDEIVE----RLEEKEVAYSELQEELEEILEQ----LEEIEEEQEEFKESLQSLRKDE 394
|
330 340
....*....|....*....|
gi 1988774682 1627 EEAEKELEKWRQKANEALRL 1646
Cdd:pfam06160 395 LEAREKLDEFKLELREIKRL 414
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
165-260 |
1.80e-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: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 165 KLLL-WSQRMTDGYqGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNL-----------------------EN 220
Cdd:cd21224 3 SLLLkWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 221 LEQAFSVAEK-----------DLG-VTRLLDPEDVDVPHPDEKSIITYVSSL 260
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1254-1921 |
1.88e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 54.67 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1254 KKLLEEIEQNKDKVDECQKYAKAY--IDTIKDYELQlvaYKAQVEPLVSPLKKtkLDSASDNIIQEYVTLRTRySElmtl 1331
Cdd:TIGR01612 1073 KEILEEAEINITNFNEIKEKLKHYnfDDFGKEENIK---YADEINKIKDDIKN--LDQKIDHHIKALEEIKKK-SE---- 1142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1332 tsqyiKFITDTQRRLDDEEKAAEKLKAEE-----RKKMAEMQAELDKQKQLAEAHAK---AIAKAEK------EAQELKL 1397
Cdd:TIGR01612 1143 -----NYIDEIKAQINDLEDVADKAISNDdpeeiEKKIENIVTKIDKKKNIYDEIKKllnEIAEIEKdktsleEVKGINL 1217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1398 KMQEEVSKREIAAVDAEKQKTNIQLELQE--LKNLSEqqIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAES 1475
Cdd:TIGR01612 1218 SYGKNLGKLFLEKIDEEKKKSEHMIKAMEayIEDLDE--IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKK 1295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1476 ELKQLRDRaaeAEKLRKLAQDEAEK---------LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQK-QKALEDLEKLRM 1545
Cdd:TIGR01612 1296 HDENISDI---REKSLKIIEDFSEEsdindikkeLQKNLLDAQKHNSDINLYLNEIANIYNILKLNKiKKIIDEVKEYTK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1546 QAEEAERQVKQAEIEKEKQIKVAHEaaqksaaaelqskHMSFAEKTSKLEESL--KQEHGAVLQLQQEAERLKKQQEDA- 1622
Cdd:TIGR01612 1373 EIEENNKNIKDELDKSEKLIKKIKD-------------DINLEECKSKIESTLddKDIDECIKKIKELKNHILSEESNId 1439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1623 ---ENSREEAE------KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAER-EAKKRAKAEEsalKQKEMA 1692
Cdd:TIGR01612 1440 tyfKNADENNEnvlllfKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKdEADKNAKAIE---KNKELF 1516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1693 EeelerQRKIAESTAQQKLTAeqelIRLRADFDNAEQQRSLLEDELYRLKN----EVAAAQQQRKQLEDElaKVRSEMDI 1768
Cdd:TIGR01612 1517 E-----QYKKDVTELLNKYSA----LAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEKSEQKIKEIKKE--KFRIEDDA 1585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1769 liqLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASrlRAISEEAKHQRQIAEEEAARQRAEaeriLKEKLAAISEat 1848
Cdd:TIGR01612 1586 ---AKNDKSNKAAIDIQLSLENFENKFLKISDIKKKIN--DCLKETESIEKKISSFSIDSQDTE----LKENGDNLNS-- 1654
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774682 1849 rLKTEAEiALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIE----EKIVQLKKSSEAEMERQKAIVDDTLKQ 1921
Cdd:TIGR01612 1655 -LQEFLE-SLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEigiiEKIKEIAIANKEEIESIKELIEPTIEN 1729
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1358-1813 |
2.07e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1358 AEERKKMAEMQAEL-----DKQKQLAEAHAKAIAKAEkeaqELklkmqEEVSKREiAAVDAEKQKTNIQLELqeLKNLSE 1432
Cdd:COG3096 277 ANERRELSERALELrrelfGARRQLAEEQYRLVEMAR----EL-----EELSARE-SDLEQDYQAASDHLNL--VQTALR 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1433 QQIKDKSQQVD-EALHSRTKIEEEIRliriqlettekqkytaeselKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEetqk 1511
Cdd:COG3096 345 QQEKIERYQEDlEELTERLEEQEEVV--------------------EEAAEQLAEAEARLEAAEEEVDSLKSQLAD---- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1512 KRQAEEELKRKseaekeaAKQKQKALEDLEKLRMQAEEAERQVKQAEiekekqikvAHEAAQKSAAAELQSKHMSFAEKT 1591
Cdd:COG3096 401 YQQALDVQQTR-------AIQYQQAVQALEKARALCGLPDLTPENAE---------DYLAAFRAKEQQATEEVLELEQKL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1592 SkLEESLKQEHGAVLQLQQEAerlkkqqeDAENSREEAekelekWrQKANEALR----LRLQAEDEAHKKTlaqeEAEKQ 1667
Cdd:COG3096 465 S-VADAARRQFEKAYELVCKI--------AGEVERSQA------W-QTARELLRryrsQQALAQRLQQLRA----QLAEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1668 KEEAEREAKKRAKAEESALKQK------EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRL 1741
Cdd:COG3096 525 EQRLRQQQNAERLLEEFCQRIGqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAW 604
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774682 1742 KNEVAAAQQQRKQLEDELAKVRSEMDILIQLktkAEKETMSNTEKS-----KQLLEAEAAKMKDLA-EEASRLRAISE 1813
Cdd:COG3096 605 LAAQDALERLREQSGEALADSQEVTAAMQQL---LEREREATVERDelaarKQALESQIERLSQPGgAEDPRLLALAE 679
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1317-1773 |
2.20e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.06 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1317 EYVTLRTRyseLMTLTSQYikfiTDTQRRLddeEKAAEKLKAEErKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL- 1395
Cdd:pfam10174 304 ELLALQTK---LETLTNQN----SDCKQHI---EVLKESLTAKE-QRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLt 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1396 --KLKMQEEVSKREiAAVDAEKQKTNIqleLQE-LKNLSEQqIKDKSQQVDEalhsrtkieeeirlIRIQLETTEKQKYT 1472
Cdd:pfam10174 373 eeKSTLAGEIRDLK-DMLDVKERKINV---LQKkIENLQEQ-LRDKDKQLAG--------------LKERVKSLQTDSSN 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1473 AESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEK----LRMQAE 1548
Cdd:pfam10174 434 TDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEhassLASSGL 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1549 EAERQVKQAEIEKEK----------QIKVAHEAAQKSAAAElqskhmSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQ 1618
Cdd:pfam10174 514 KKDSKLKSLEIAVEQkkeecsklenQLKKAHNAEEAVRTNP------EINDRIRLLEQEVARYKEESGKAQAEVERLLGI 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1619 QEDAENSREEAEKELEKWRQKAneALRLRLQAEDEAHKKTLAQEEAEKQKEEAErEAKKRAKAEESALKQKEMAE--EEL 1696
Cdd:pfam10174 588 LREVENEKNDKDKKIAELESLT--LRQMKEQNKKVANIKHGQQEMKKKGAQLLE-EARRREDNLADNSQQLQLEElmGAL 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1697 ERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAA---------------QQQRKQLEDELAK 1761
Cdd:pfam10174 665 EKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAaisekdaniallelsSSKKKKTQEEVMA 744
|
490
....*....|...
gi 1988774682 1762 VRSEMDILI-QLK 1773
Cdd:pfam10174 745 LKREKDRLVhQLK 757
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2450-2595 |
2.28e-06 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 52.67 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2450 NEKARLKKEAEELQNKSKEMADAQQKKIEhEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLEsqfeEEVKKAKALKDEQER 2529
Cdd:pfam02841 155 EERDKLEAKYNQVPRKGVKAEEVLQEFLQ-SKEAVEEAILQTDQALTAKEKAIEAERAKAE----AAEAEQELLREKQKE 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2530 QKQQMEQEKKTLQATMdAALSKQKEAEEEMLRKQKEMQeLERQRLEQERILAE----ENQKLREKLQQLE 2595
Cdd:pfam02841 230 EEQMMEAQERSYQEHV-KQLIEKMEAEREQLLAEQERM-LEHKLQEQEELLKEgfktEAESLQKEIQDLK 297
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1849-2342 |
2.31e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1849 RLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKivqlkKSSEAEMERQKAIVDDTLKQRRVVEEE 1928
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL-----EELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1929 IRILKLNFEKASsgkldLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKA 2008
Cdd:COG4717 125 LQLLPLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2009 ALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSIT--QKKLKEEYEKAKKLAKEA 2086
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLalLGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2087 EAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKL 2166
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2167 AEQTLKQKFQVEQE--LTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELfKVKVQMEELLKLKNKIEEEN 2244
Cdd:COG4717 360 EEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL-EELLEALDEEELEEELEELE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2245 QRlikkdkdstqklLAEEAENMRKLAEDAARLSveaqeaARLRQIAEDDLNQQRALAEKMLKEKMQ-AIQEASRLKAEAE 2323
Cdd:COG4717 439 EE------------LEELEEELEELREELAELE------AELEQLEEDGELAELLQELEELKAELReLAEEWAALKLALE 500
|
490 500
....*....|....*....|
gi 1988774682 2324 MLQK-QKDLAQEQAQKLLED 2342
Cdd:COG4717 501 LLEEaREEYREERLPPVLER 520
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1367-1549 |
2.35e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1367 MQAELDKQKQLAEAHAKaIAKAEKEAQELklkmQEEVSKREIAAVDAEKQKTNIQLELQELknlsEQQIKDKSQQVDEAL 1446
Cdd:COG1579 2 MPEDLRALLDLQELDSE-LDRLEHRLKEL----PAELAELEDELAALEARLEAAKTELEDL----EKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1447 HSRTKIEEEIRLIRiqletTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAE 1526
Cdd:COG1579 73 ARIKKYEEQLGNVR-----NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
170 180
....*....|....*....|...
gi 1988774682 1527 KEAAKQKQKALEDLEKLRMQAEE 1549
Cdd:COG1579 148 DEELAELEAELEELEAEREELAA 170
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3920-3956 |
2.37e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.71 E-value: 2.37e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1988774682 3920 RYLQGTGCIAGVFLESTKERLSIYQAMKKNMIRPGTA 3956
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1339-1824 |
2.37e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 54.04 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1339 ITDTQRRLDDEEKAAEKLKAEErkkMAEMQAELDKQK----QLAEAHAKAIAKAEKEAQelklkMQEEvskreIAAVDAE 1414
Cdd:PRK10246 389 LTHAEQKLNALPAITLTLTADE---VAAALAQHAEQRplrqRLVALHGQIVPQQKRLAQ-----LQVA-----IQNVTQE 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1415 KQKTNIQLELQElknlseQQIKDKSQQVDEAlhsRTKIEEEIRL-----IRIQLE---------TTEK---QKYTAeSEL 1477
Cdd:PRK10246 456 QTQRNAALNEMR------QRYKEKTQQLADV---KTICEQEARIkdleaQRAQLQagqpcplcgSTSHpavEAYQA-LEP 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1478 KQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQA 1557
Cdd:PRK10246 526 GVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQ 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1558 EiEKEKQIKvaheaaQKSAAAELQSKHMSFAEKTSKLEESLKQEHgAVLQLQQEAERLKKQQEDAENS-REEAEKELEKW 1636
Cdd:PRK10246 606 E-EHERQLR------LLSQRHELQGQIAAHNQQIIQYQQQIEQRQ-QQLLTALAGYALTLPQEDEEASwLATRQQEAQSW 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1637 RQKANEALRLRLQ-AEDEAHKKTLAQEEAEKQKEEAE-----REAKKRAKAEESALkQKEMAEEELERQRkIAESTAQ-- 1708
Cdd:PRK10246 678 QQRQNELTALQNRiQQLTPLLETLPQSDDLPHSEETValdnwRQVHEQCLSLHSQL-QTLQQQDVLEAQR-LQKAQAQfd 755
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1709 QKLTA---EQELIRLRADFDNA-----EQQRSLLEDELYRLK-------NEVAAAQQQRKQLEDELAKVRSEMDILIQLK 1773
Cdd:PRK10246 756 TALQAsvfDDQQAFLAALLDEEtltqlEQLKQNLENQRQQAQtlvtqtaQALAQHQQHRPDGLDLTVTVEQIQQELAQLA 835
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 1774 TKAEKETMSNTEKSKQLleaeaakmKDLAEEASRLRAISEEAKHQRQIAEE 1824
Cdd:PRK10246 836 QQLRENTTRQGEIRQQL--------KQDADNRQQQQALMQQIAQATQQVED 878
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2467-2599 |
2.68e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.63 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2467 KEMADAQQKKIEHE-KTVLQQTfmtEKEM-LLKKEKLIE--DEKKRLESQFEEEVKKAKalkDEQERQKQQMEQEKKTLQ 2542
Cdd:PRK12704 26 KKIAEAKIKEAEEEaKRILEEA---KKEAeAIKKEALLEakEEIHKLRNEFEKELRERR---NELQKLEKRLLQKEENLD 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774682 2543 ATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLrEKLQQL--EDAQK 2599
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLtaEEAKE 157
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1471-1917 |
2.74e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.49 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1471 YTAESELKQLRDRAAEaeklrKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEA----EKEAAKQKQKALEDLEKLRMQ 1546
Cdd:pfam05667 91 YPNEPDIRKILMFLVE-----KLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAApwlpPECKPHQRRQGSRALRPFHTQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1547 A-EEAERQVKQAEIEKEkqikvaheaaqksaAAELQSKHMSFAE----KTSKLEESLKQEHGAVLQLQQEAERLKKQQED 1621
Cdd:pfam05667 166 TlVLPGRKGKTLKNSKE--------------LKEFYSEYLPPVTaqpsSRASVVPSLLERNAAELAAAQEWEEEWNSQGL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1622 AENSREEAEK--ELEKWRQKANEALRLRLQAEDEAHkktlaqeeaekqkeeaeREAKKRAKAEESALKQKEMAEEELERQ 1699
Cdd:pfam05667 232 ASRLTPEEYRkrKRTKLLKRIAEQLRSAALAGTEAT-----------------SGASRSAQDLAELLSSFSGSSTTDTGL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1700 RKIAESTAQQKLTAEQELIRLRADFDNAEQQrslLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILI----QLKTK 1775
Cdd:pfam05667 295 TKGSRFTHTEKLQFTNEAPAATSSPPTKVET---EEELQQQREEELEELQEQLEDLESSIQELEKEIKKLEssikQVEEE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1776 AEKETMSNTEKSKQ----------LLEAEA--AKMKDLAEEAS-RLRAISEE-AKHQRQIAEE------EAARQRAEAER 1835
Cdd:pfam05667 372 LEELKEQNEELEKQykvkkktldlLPDAEEniAKLQALVDASAqRLVELAGQwEKHRVPLIEEyralkeAKSNKEDESQR 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1836 I------LKEKLAAISEATRLKTEaeiALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIE-EKIVQLKKSSEAEM 1908
Cdd:pfam05667 452 KleeikeLREKIKEVAEEAKQKEE---LYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEiTKILSDTKSLQKEI 528
|
490
....*....|....*.
gi 1988774682 1909 -------ERQKAIVDD 1917
Cdd:pfam05667 529 nsltgklDRTFTVTDE 544
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1486-1843 |
2.77e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.42 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1486 EAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQI 1565
Cdd:pfam15709 164 TPASISHAERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERNL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1566 KVAHEAAQK----SAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQ---------EDAENSREEAEKE 1632
Cdd:pfam15709 244 EVAAELSGPdvinSKETEDASERGAFSSDSVVEDPWLSSKYDAEESQVSIDGRSSPTQtfvvtgnmeSEEERSEEDPSKA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1633 LEKWRQKANEAlRLRLQAEdEAHKKTLAQeeaekqkeeaerEAKKRAKAEESALKQkemaeEELERQRKIAE--STAQQK 1710
Cdd:pfam15709 324 LLEKREQEKAS-RDRLRAE-RAEMRRLEV------------ERKRREQEEQRRLQQ-----EQLERAEKMREelELEQQR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1711 LTAEqelIRLRADFDNAEQQRSllEDELYRLKNEVAAAQQQRKQLEDELAKVrsemdiLIQLKTKAEKETMSNTEKSKQL 1790
Cdd:pfam15709 385 RFEE---IRLRKQRLEEERQRQ--EEEERKQRLQLQAAQERARQQQEEFRRK------LQELQRKKQQEEAERAEAEKQR 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 1791 LEAEAAKmkdLAEEASRLRAISEEAK--HQRQIAEEEAARQRAEAERILKEKLAA 1843
Cdd:pfam15709 454 QKELEMQ---LAEEQKRLMEMAEEERleYQRQKQEAEEKARLEAEERRQKEEEAA 505
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
2424-2594 |
3.06e-06 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 53.30 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2424 VERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKsKEMADAQQKKIEHEKTVLQQTFMTEKEmllKKEKLIE 2503
Cdd:pfam15066 372 VEELIEDKYNVILEKNDINKTLQNLQEILANTQKHLQESRKE-KETLQLELKKIKVNYVHLQERYITEMQ---QKNKSVS 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2504 D--EKKRLESQFEEEVKKAKALKDEQERqkqqmeqekktlqATMDA--ALSKQKEA-EEEMLRKQKEMQELERQRLeqer 2578
Cdd:pfam15066 448 QclEMDKTLSKKEEEVERLQQLKGELEK-------------ATTSAldLLKREKETrEQEFLSLQEEFQKHEKENL---- 510
|
170
....*....|....*.
gi 1988774682 2579 ilaEENQKLREKLQQL 2594
Cdd:pfam15066 511 ---EERQKLKSRLEKL 523
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1684-1888 |
3.23e-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: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1684 SALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAK-- 1761
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1762 --------VRSEMDILIQLK---------------TKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKH- 1817
Cdd:COG3883 93 ralyrsggSVSYLDVLLGSEsfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAe 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 1818 -QRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQ 1888
Cdd:COG3883 173 lEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3721-3755 |
3.44e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.44e-06
10 20 30
....*....|....*....|....*....|....*
gi 1988774682 3721 LLEAQAATGFIVDPLKNETLTVDEAVRKGVVGPEI 3755
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1116-1724 |
3.45e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1116 EVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAvsdkmvrvHSERDVELDHFRQQLSSLqDRWKAvFT 1195
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAER--------YAAARERLAELEYLRAAL-RLWFA-QR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1196 QIDLRQRELEQLgrqlgyyRESYDWLIRWIADAKQRQEKIQAvpitDSKTLKEQLAQ-----EKKLLEEIEQNKDKVDEC 1270
Cdd:COG4913 289 RLELLEAELEEL-------RAELARLEAELERLEARLDALRE----ELDELEAQIRGnggdrLEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1271 QKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLK--KTKLDSASDNIIQEYVTLRTRYSELmtltsqyikfiTDTQRRLDD 1348
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDL-----------RRELRELEA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1349 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIA-----KAEKEA-----------QELKLKMQEEVSKREIAAVD 1412
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGelievRPEEERwrgaiervlggFALTLLVPPEHYAAALRWVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1413 AEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTK-----IEEEI--RLIRIQLETTEkqkytaesELKQLRdRAA 1485
Cdd:COG4913 507 RLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHpfrawLEAELgrRFDYVCVDSPE--------ELRRHP-RAI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1486 EAEKLRKLAQDEAEK-LRKQVSEE-------TQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQA 1557
Cdd:COG4913 578 TRAGQVKGNGTRHEKdDRRRIRSRyvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1558 eiekEKQIKVAheaaqkSAAAELqskhmsfAEKTSKLEEsLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWR 1637
Cdd:COG4913 658 ----WDEIDVA------SAEREI-------AELEAELER-LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1638 QKANEALRLRLQAEDEAHkktlaqEEAEKQKEEAEREAKKRAKAEESALKQKEMAeEELERQRKIAESTAQQkltAEQEL 1717
Cdd:COG4913 720 KELEQAEEELDELQDRLE------AAEDLARLELRALLEERFAAALGDAVERELR-ENLEERIDALRARLNR---AEEEL 789
|
....*..
gi 1988774682 1718 IRLRADF 1724
Cdd:COG4913 790 ERAMRAF 796
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1695-1839 |
3.55e-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: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1695 ELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRS---------E 1765
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyealqkE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774682 1766 MDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKE 1839
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2418-2591 |
3.59e-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: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2418 QEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQ---NKSKEMADAQQKKIEHEKTvLQQTFMTEKEM 2494
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEkeiKRLELEIEEVEARIKKYEE-QLGNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2495 L-LKKEklIEDEKKRLeSQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAalsKQKEAEEEMLRKQKEMQELERQR 2573
Cdd:COG1579 92 EaLQKE--IESLKRRI-SDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAER 165
|
170
....*....|....*...
gi 1988774682 2574 LEQERILAEENQKLREKL 2591
Cdd:COG1579 166 EELAAKIPPELLALYERI 183
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1744-1899 |
3.97e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.95 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1744 EVAAAQQQRKQledELAKVRSEMDILIQLKTKAEKETmsntEKSKQLLEAEAAKMKDLAEEASRLRAIS---------EE 1814
Cdd:COG2268 213 EIAIAQANREA---EEAELEQEREIETARIAEAEAEL----AKKKAEERREAETARAEAEAAYEIAEANaerevqrqlEI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1815 AKHQRQI--AEEEAARQRAEAERILKEKLAAISEATRLKTEAE----IALKEKEAENERLRRQAEdEAYQRKALEDQASQ 1888
Cdd:COG2268 286 AEREREIelQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEaeaiRAKGLAEAEGKRALAEAW-NKLGDAAILLMLIE 364
|
170
....*....|.
gi 1988774682 1889 HKQEIEEKIVQ 1899
Cdd:COG2268 365 KLPEIAEAAAK 375
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1678-1853 |
4.29e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1678 RAKAEESALKQKEMAEEELERQRKIAESTAQQKLT-AEQELIRLRADFDNAEQQRsllEDELYRLKNEVaaaQQQRKQLE 1756
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRER---RNELQKLEKRL---LQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1757 DELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDL-------AEEASR--LRAISEEAKHQRQI----AE 1823
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisgltAEEAKEilLEKVEEEARHEAAVlikeIE 179
|
170 180 190
....*....|....*....|....*....|.
gi 1988774682 1824 EEAarqRAEAERILKEKLA-AIseaTRLKTE 1853
Cdd:PRK12704 180 EEA---KEEADKKAKEILAqAI---QRCAAD 204
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1837-2609 |
4.34e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.51 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1837 LKEKLAAISEATRLKTEAEIALKEKEAENERLRrqaedEAYQRKALEDQASQHKQEIEEKIV--QLKKSSEAEMERQKAI 1914
Cdd:TIGR00606 171 LKQKFDEIFSATRYIKALETLRQVRQTQGQKVQ-----EHQMELKYLKQYKEKACEIRDQITskEAQLESSREIVKSYEN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1915 VDDTLKQRRVVEEEIRilklnfekasSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLrklaleeekrRREAEEKVKK 1994
Cdd:TIGR00606 246 ELDPLKNRLKEIEHNL----------SKIMKLDNEIKALKSRKKQMEKDNSELELKMEKV----------FQGTDEQLND 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1995 IAAAEEEAARQRKAAL----EELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQK 2070
Cdd:TIGR00606 306 LYHNHQRTVREKERELvdcqRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2071 KLKEeyekakklakeaeaaKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfEAAKRAQAEAAAL 2150
Cdd:TIGR00606 386 PFSE---------------RQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKK-GLGRTIELKKEIL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2151 MQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSV---LDEE--LQRLKDEVDDAVKQRGQVEEELFK 2225
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTetlKKEVksLQNEKADLDRKLRKLDQEMEQLNH 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2226 VKVQMEELLKLKNKIEEENQRLIKKDKDSTQKL--LAEEAENMRKLAEDAARLSVEAQ-----------EAARLRQIAED 2292
Cdd:TIGR00606 530 HTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELtsLLGYFPNKKQLEDWLHSKSKEINqtrdrlaklnkELASLEQNKNH 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2293 DLNQQRALAEKMLK--EKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYH-------KSLEV 2363
Cdd:TIGR00606 610 INNELESKEEQLSSyeDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqRVFQT 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2364 ERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRK 2443
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2444 AIADLENEKARLKKeAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEML------LKKEKLIEDEKKRLESQFEEEV 2517
Cdd:TIGR00606 770 QETLLGTIMPEEES-AKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLdrtvqqVNQEKQEKQHELDTVVSKIELN 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2518 KKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELER---QRLEQERILAEENQKLREKLQQL 2594
Cdd:TIGR00606 849 RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIReikDAKEQDSPLETFLEKDQQEKEEL 928
|
810
....*....|....*
gi 1988774682 2595 EDAQKDQHTRETDKV 2609
Cdd:TIGR00606 929 ISSKETSNKKAQDKV 943
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1722-2071 |
4.53e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.42 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1722 ADF-DNAEQQRSLLEDELyRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMK- 1799
Cdd:COG3096 271 ADYmRHANERRELSERAL-ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKi 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1800 -----DLAEEASRLRA---ISEEAKHQRQIAEEEAARQRAEAERiLKEKLA---------------------AISEATRL 1850
Cdd:COG3096 350 eryqeDLEELTERLEEqeeVVEEAAEQLAEAEARLEAAEEEVDS-LKSQLAdyqqaldvqqtraiqyqqavqALEKARAL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1851 KTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQ---ASQHKQEIEeKIVQLKKSSEAEMERQKAivDDTLKQrrvVEE 1927
Cdd:COG3096 429 CGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKlsvADAARRQFE-KAYELVCKIAGEVERSQA--WQTARE---LLR 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1928 EIRILKLNFEKASSGKLDL-ELE-----LNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEE 2001
Cdd:COG3096 503 RYRSQQALAQRLQQLRAQLaELEqrlrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSE 582
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 2002 AARQRKAALEELERLRKKAEEARKQKDEADKEAEkQIVVAQQAAQKCSAAEQQV--QSVLAQQIEDSITQKK 2071
Cdd:COG3096 583 LRQQLEQLRARIKELAARAPAWLAAQDALERLRE-QSGEALADSQEVTAAMQQLleREREATVERDELAARK 653
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1524-1891 |
4.53e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.95 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1524 EAEKEAAKQK-QKALEDLEKLRmQAEEAERQVKQAEIEKEKQIkVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQeh 1602
Cdd:pfam02029 2 EDEEEAARERrRRAREERRRQK-EEEEPSGQVTESVEPNEHNS-YEEDSELKPSGQGGLDEEEAFLDRTAKREERRQK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1603 gavlQLQQEAERLKKQQED--------AENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTlaqeeaekqkeeaeRE 1674
Cdd:pfam02029 78 ----RLQEALERQKEFDPTiadekesvAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIRE--------------KE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1675 AKKRAKAEEsalkQKEMAEEELERQRKIAESTAQQKltaeqelirlraDFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQ 1754
Cdd:pfam02029 140 YQENKWSTE----VRQAEEEGEEEEDKSEEAEEVPT------------ENFAKEEVKDEKIKKEKKVKYESKVFLDQKRG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1755 LEDELAKVRSEMDILIQLKTKAEKETMSNT----EKSKQLLEAEAAKmkdlaEEASRLRAISE----EAKHQRQiaeEEA 1826
Cdd:pfam02029 204 HPEVKSQNGEEEVTKLKVTTKRRQGGLSQSqereEEAEVFLEAEQKL-----EELRRRRQEKEseefEKLRQKQ---QEA 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 1827 ARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERL------RRQAEDEAYQRKALEDQASQHKQ 1891
Cdd:pfam02029 276 ELELEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRmkeeieRRRAEAAEKRQKLPEDSSSEGKK 346
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
38-142 |
4.64e-06 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 48.81 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 38 RKDERDRVQKKTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGETLPREKG--RMRFHKLQNVQIALDFLR 113
Cdd:cd21285 3 SWEAENGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLA 82
|
90 100
....*....|....*....|....*....
gi 1988774682 114 HRQVKLVNIRNDDIADGNPKLTLGLIWTI 142
Cdd:cd21285 83 AKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1386-1657 |
4.66e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 52.39 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1386 AKAEKEAQELKlKMQEEVSKREIAAVDAEKQKTNIQLELQElknlSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLET 1465
Cdd:PRK11637 40 AHASDNRDQLK-SIQQDIAAKEKSVRQQQQQRASLLAQLKK----QEEAISQASRKLRETQNTLNQLNKQIDELNASIAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1466 TEKQKYTAESELKQLRDRAaeaeklrkLAQDEAEKLRKQVS-EETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLR 1544
Cdd:PRK11637 115 LEQQQAAQERLLAAQLDAA--------FRQGEHTGLQLILSgEESQRGERILAYFGYLNQARQETIAELKQTREELAAQK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1545 MQAEEAERQVKQAEIEKEKQ---IKVAHEAAQKSAAAelqskhmsfaektskLEESLKQEHGAVLQLQQEAERLKKQQED 1621
Cdd:PRK11637 187 AELEEKQSQQKTLLYEQQAQqqkLEQARNERKKTLTG---------------LESSLQKDQQQLSELRANESRLRDSIAR 251
|
250 260 270
....*....|....*....|....*....|....*..
gi 1988774682 1622 AE-NSREEAEKElekwrqkANEALRLRlQAEDEAHKK 1657
Cdd:PRK11637 252 AErEAKARAERE-------AREAARVR-DKQKQAKRK 280
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1343-1571 |
4.67e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.23 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1343 QRRLDDEEKAAEKLKA--EERKKMAEMQAELDKQ-KQLAEAHAKAIAKAEKEAQELKLKMQEEVSK---REIAAVDAEKQ 1416
Cdd:pfam13868 65 EERKEERKRYRQELEEqiEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKLEKQRQLREeidEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1417 KTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESElkQLRDRAAEAEKLRKLAQD 1496
Cdd:pfam13868 145 LEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERD--ELRAKLYQEEQERKERQK 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 1497 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEA 1571
Cdd:pfam13868 223 EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK 297
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1604-1843 |
5.14e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1604 AVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEE 1683
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1684 SALKQKEMAEEELERQRKIAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVR 1763
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQ---PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1764 SEMDILIQLKT--KAEKETMSNTEKSKQLLEAEAAkmKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKL 1841
Cdd:COG4942 171 AERAELEALLAelEEERAALEALKAERQKLLARLE--KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
..
gi 1988774682 1842 AA 1843
Cdd:COG4942 249 AA 250
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1501-1680 |
5.26e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1501 LRKQVSEetQKKRQAEEELKR-KSEAEKEAAKQKQKAL----EDLEKLRmqaEEAERQVKQAEIE---KEKQIKVAHEA- 1571
Cdd:PRK12704 24 VRKKIAE--AKIKEAEEEAKRiLEEAKKEAEAIKKEALleakEEIHKLR---NEFEKELRERRNElqkLEKRLLQKEENl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1572 AQKSAAAELQSKHMsfaektSKLEESLKQEHGAVLQLQQEAERLKKQQED-----AENSREEAEKE-LEKWRQKA-NEAL 1644
Cdd:PRK12704 99 DRKLELLEKREEEL------EKKEKELEQKQQELEKKEEELEELIEEQLQeleriSGLTAEEAKEIlLEKVEEEArHEAA 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 1988774682 1645 RLRLQAEDEAHKktlaqeeaekqkeeaerEAKKRAK 1680
Cdd:PRK12704 173 VLIKEIEEEAKE-----------------EADKKAK 191
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2499-2604 |
5.40e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2499 EKLIEDEKKRLESQFEEEVKKAKalkDEQERQKQQMEQEKKTLQATMdAALSKQKEAEEEMLRKQKEMQELERQRLE-QE 2577
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEALLEAK---EEIHKLRNEFEKELRERRNEL-QKLEKRLLQKEENLDRKLELLEKREEELEkKE 116
|
90 100
....*....|....*....|....*..
gi 1988774682 2578 RILAEENQKLREKLQQLEDAQKDQHTR 2604
Cdd:PRK12704 117 KELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2251-2465 |
5.81e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2251 DKDSTQKLLAEEAENMRKLaEDAARLSVEAQE-AARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQK 2329
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL-ERAHEALEDAREqIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2330 DLAQEQAQKLLEDKQLMQQRLEEETEEYhksLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATR 2409
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREEL---DELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2410 LHETEIATQEK----MTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNK 2465
Cdd:COG4913 375 LPASAEEFAALraeaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
621-713 |
6.06e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.71 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 621 HAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDIQALGDRLVRDGHPGKKTVESFTA 700
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1988774682 701 ALQTQWSWILQLC 713
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1374-1566 |
6.43e-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: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1374 QKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREiAAVDAEKQKTNIqLELQELKNLSEQQIKDKSQQVDEALHSRTKIE 1453
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAE-AALEEFRQKNGL-VDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1454 EEIRLIRIQLETTEKQKYT--AESELKQLRDRAAEAE-KLRKLAQD------EAEKLRKQVSEETQKKRQAEEELKRKSE 1524
Cdd:COG3206 240 ARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEaELAELSARytpnhpDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1988774682 1525 AEKEAAKQKQKALED-LEKLRMQAEE-AERQVKQAEIEKEKQIK 1566
Cdd:COG3206 320 AELEALQAREASLQAqLAQLEARLAElPELEAELRRLEREVEVA 363
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1424-1834 |
6.47e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 52.38 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1424 LQELKNLSEQQIK---DKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 1500
Cdd:pfam05622 26 LQEEKNSLQQENKklqERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1501 LRKQVSEETQKK------RQAEEELKrKSEAEKEAAKQKqkaLEDLEKLRMQA---EEAERQVKQAEIEKEKQIKVA--- 1568
Cdd:pfam05622 106 LTSLAEEAQALKdemdilRESSDKVK-KLEATVETYKKK---LEDLGDLRRQVkllEERNAEYMQRTLQLEEELKKAnal 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1569 --HEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQedaENSREeaekelekwrqkANEALRL 1646
Cdd:pfam05622 182 rgQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIER---DTLRE------------TNEELRC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1647 RLQAEDEAHKKTLAQEEAEKQKEEAEREakkrakaeesaLKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDN 1726
Cdd:pfam05622 247 AQLQQAELSQADALLSPSSDPGDNLAAE-----------IMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLED 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1727 AEQQRSLLEDELyRLKNE-VAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEketmsntEKSKQLLEAEAAKMKdlAEEA 1805
Cdd:pfam05622 316 ANRRKNELETQN-RLANQrILELQQQVEELQKALQEQGSKAEDSSLLKQKLE-------EHLEKLHEAQSELQK--KKEQ 385
|
410 420
....*....|....*....|....*....
gi 1988774682 1806 SRLRAISEEAKHQRQIAEEEAARQRAEAE 1834
Cdd:pfam05622 386 IEELEPKQDSNLAQKIDELQEALRKKDED 414
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3921-3959 |
6.97e-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: 6.97e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1988774682 3921 YLQGTGCIAGVFLESTKERLSIYQAMKKNMIRPGTAFEL 3959
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2197-2468 |
7.05e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2197 VLDEelQRLKDEVDDAVKQRGQ---VEEELFKVKVQMEELLKlknkIEEENQRLikkdkdstqkllAEEAENMRKLAEDA 2273
Cdd:COG4913 217 MLEE--PDTFEAADALVEHFDDlerAHEALEDAREQIELLEP----IRELAERY------------AAARERLAELEYLR 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2274 ARLSV-EAQEAARLRQIAEDDLNQQRALAEKmlkEKMQAIQEASRLKAEAEMLQKQKDLAQ----EQAQKLLEDKQLMQQ 2348
Cdd:COG4913 279 AALRLwFAQRRLELLEAELEELRAELARLEA---ELERLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2349 RLEEETEEYHKSLeveRKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLE 2428
Cdd:COG4913 356 ERERRRARLEALL---AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1988774682 2429 FERLNTSKEADDLRKAIAD-LENEKARLKKEAEELQNKSKE 2468
Cdd:COG4913 433 RRKSNIPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1431-1702 |
7.25e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1431 SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQ 1510
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1511 KKRQAEEELKRKSEAEKEAA------KQKQKALEDLEKlRMQAE----EAERQV--KQAEIEKE-KQIKVAHEAAQK--- 1574
Cdd:COG1340 86 KLNELREELDELRKELAELNkaggsiDKLRKEIERLEW-RQQTEvlspEEEKELveKIKELEKElEKAKKALEKNEKlke 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1575 --SAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRlRLQAED 1652
Cdd:COG1340 165 lrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK-ELRELR 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1653 EAHKKTLAQEeaekqkeeaerEAKKRAKAEESALKQKEMAEEELERQRKI 1702
Cdd:COG1340 244 KELKKLRKKQ-----------RALKREKEKEELEEKAEEIFEKLKKGEKL 282
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1449-1977 |
7.30e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1449 RTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKlAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE 1528
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKS-SNLELENIKKQIADDEKSHSITLKEIERLSIEYNN 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1529 AAKQKQKALEDLEKLRMQAEEAERqvkqaeiekekqikvaHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQL 1608
Cdd:PRK01156 230 AMDDYNNLKSALNELSSLEDMKNR----------------YESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1609 QQEAERLKKQQEDAENSREEAEKelekwrqkaneaLRLRLQAEDEAHKKtLAQEEAEKQKEEAEREAKKRAKAEESALKQ 1688
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSN------------IDAEINKYHAIIKK-LSVLQKDYNDYIKKKSRYDDLNNQILELEG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1689 KEMAEEELER-----QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLED---ELYRLKNEVAAAQQQRKQLEDELA 1760
Cdd:PRK01156 361 YEMDYNSYLKsieslKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEinvKLQDISSKVSSLNQRIRALRENLD 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1761 KVRSEMDILIQLKTKAEKETMSNTEKSKQLLEaeaakmkDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEK 1840
Cdd:PRK01156 441 ELSRNMEMLNGQSVCPVCGTTLGEEKSNHIIN-------HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1841 LAAISEATRLKTEAE-----IALKEKEAENERLRRQAEDEAYQRKALEDQASQHkqeiEEKIVQLKKSSEAEMERQKAIV 1915
Cdd:PRK01156 514 INKSINEYNKIESARadledIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKR----TSWLNALAVISLIDIETNRSRS 589
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774682 1916 DDTLKQRRVVEEEIRILKLNFEKASS----GKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKL 1977
Cdd:PRK01156 590 NEIKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNY 655
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1683-1916 |
7.43e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1683 ESALKQKEMAEEELERQRKIAEsTAQQKLTA---EQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDEL 1759
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1760 AKVRSEMDILIQLKTKAEKETmsntekskQLLEAEAakmkDLAEEASRLRaiseeAKHQRQIAeeeAARQRAEAERILKE 1839
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRA--------QLAELEA----ELAELSARYT-----PNHPDVIA---LRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1840 KLAAISEAtrLKTEAEiALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIE--EKIVQ--LKKSSEAEMERQKAIV 1915
Cdd:COG3206 310 EAQRILAS--LEAELE-ALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEvaRELYEslLQRLEEARLAEALTVG 386
|
.
gi 1988774682 1916 D 1916
Cdd:COG3206 387 N 387
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
36-153 |
7.91e-06 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 48.50 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 36 DGRKDERDRVQKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKL 102
Cdd:cd21323 15 EGTQHSYSEEEKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTIS 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 103 QNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 153
Cdd:cd21323 95 ENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2436-2595 |
8.27e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2436 KEADDLRKAIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEktvlqqtfmtekemLLKKEKLIEDEKKRLESqfee 2515
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELE--------------IEEVEARIKKYEEQLGN---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2516 eVKKAKALK------DEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLRE 2589
Cdd:COG1579 85 -VRNNKEYEalqkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*.
gi 1988774682 2590 KLQQLE 2595
Cdd:COG1579 164 EREELA 169
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1120-1294 |
8.85e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 49.75 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1120 VPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEElkkasavSDKMVRVHSERDVELdhfRQQLSSLQDRWKAVFTQIDL 1199
Cdd:cd00176 28 YGDDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHPDAEEI---QERLEELNQRWEELRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1200 RQRELEQLGRQLGYYRESYDwLIRWIADAKQRQEKIQavPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYID 1279
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLE 174
|
170
....*....|....*
gi 1988774682 1280 TIKDYELQLVAYKAQ 1294
Cdd:cd00176 175 EGHPDADEEIEEKLE 189
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1462-1888 |
9.28e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.83 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1462 QLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLE 1541
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1542 KLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQED 1621
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1622 AENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRK 1701
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1702 IAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDElyrlknevAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETM 1781
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAE--------AVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEAL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1782 SNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEK 1861
Cdd:COG5278 423 ELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLA 502
|
410 420
....*....|....*....|....*..
gi 1988774682 1862 EAENERLRRQAEDEAYQRKALEDQASQ 1888
Cdd:COG5278 503 LALAALLLAAAEAALAAALAAALASAE 529
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1247-1895 |
1.02e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1247 KEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKK-----TKLDSASDNIIQEyvtl 1321
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKnkdkiNKLNSDLSKINSE---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1322 rtryselmtltsqyIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL---KLK 1398
Cdd:TIGR04523 112 --------------IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELeneLNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1399 MQEEVSKREIAAVDAEKQKTNIQLELQELKNLsEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELK 1478
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK-IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1479 QLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAE---EELKRKSEAE-----KEAAKQKQKALEDLEKLRMQAEEA 1550
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKseiSDLNNQKEQDwnkelKSELKNQEKKLEEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1551 ERQVKQaEIEKEKQikvaheaaqksaaaELQSKHMSFAEKTSKLEESlkqehgavlqlQQEAERLKKQQEDAENSREEAE 1630
Cdd:TIGR04523 337 ISQLNE-QISQLKK--------------ELTNSESENSEKQRELEEK-----------QNEIEKLKKENQSYKQEIKNLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1631 KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 1710
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1711 LTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMS-------- 1782
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDledelnkd 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1783 NTEKSKQLLEAEaakMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEklaaISEATRLKTEAEIALKEKE 1862
Cdd:TIGR04523 551 DFELKKENLEKE---IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE----IEEKEKKISSLEKELEKAK 623
|
650 660 670
....*....|....*....|....*....|...
gi 1988774682 1863 AENERLRRQAEDEAYQRKALEDQASQHKQEIEE 1895
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1404-1576 |
1.08e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.70 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1404 SKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDksqqvdEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQlrdr 1483
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKE------EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1484 aaeaeKLRKLaqdeaEKLRKQVSEETQKKRQAEEELKRKseaEKEAAKQKQKALEDLEKL-RMQAEEAERQV-----KQA 1557
Cdd:PRK12704 101 -----KLELL-----EKREEELEKKEKELEQKQQELEKK---EEELEELIEEQLQELERIsGLTAEEAKEILlekveEEA 167
|
170
....*....|....*....
gi 1988774682 1558 EIEKEKQIKVAHEAAQKSA 1576
Cdd:PRK12704 168 RHEAAVLIKEIEEEAKEEA 186
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2499-2607 |
1.10e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.70 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2499 EKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTlqatmdaalskqkEAEEEMLRKQKEMQELERQRLEQER 2578
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRN-------------EFEKELRERRNELQKLEKRLLQKEE 96
|
90 100
....*....|....*....|....*....
gi 1988774682 2579 ILAEENQKLREKLQQLEDAQKDQHTRETD 2607
Cdd:PRK12704 97 NLDRKLELLEKREEELEKKEKELEQKQQE 125
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2006-2461 |
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 1988774682 2006 RKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSvLAQQIEDSITQKKLKEEYEKAKKLAKE 2085
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2086 AEAAKEKAEReaalLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfeaakraqaeaaalmqkqqadtemAKHKK 2165
Cdd:COG4717 127 LLPLYQELEA----LEAELAELPERLEELEERLEELRELEEELEELEAELA------------------------ELQEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2166 LAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELfkvkvqmeELLKLKNKIEEENQ 2245
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL--------EAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2246 RLI------------KKDKDSTQK----------LLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRA---- 2299
Cdd:COG4717 251 LLLiaaallallglgGSLLSLILTiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalgl 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2300 ---LAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKlledKQLMQQRLEEETEEYHKSLEVERKRQlEIMAEAE 2376
Cdd:COG4717 331 ppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI----AALLAEAGVEDEEELRAALEQAEEYQ-ELKEELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2377 RLRLQVSQLSEAQARAEEEAKKF--KKQADKVATRLHETEIATQEKMTVVERLEfERLNTSKEADDLRKAIADLENEKAR 2454
Cdd:COG4717 406 ELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELE-AELEQLEEDGELAELLQELEELKAE 484
|
....*..
gi 1988774682 2455 LKKEAEE 2461
Cdd:COG4717 485 LRELAEE 491
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2236-2598 |
1.22e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2236 LKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEdaARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEA 2315
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLH--GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2316 SRLKAEAEMLQKQKDLAQEQAQKlleDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSeaqaraeee 2395
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKK---QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVT--------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2396 akKFKKQADKVATRLheteiatQEKMTVVERLEFERLNTSKEADDL---RKAIADLENEKARLKKEAEElQNKSKEMADA 2472
Cdd:TIGR00618 304 --QIEQQAQRIHTEL-------QSKMRSRAKLLMKRAAHVKQQSSIeeqRRLLQTLHSQEIHIRDAHEV-ATSIREISCQ 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2473 QQKKIEHEKTVLQQtfmteKEMLLKKEKLIedekKRLESQFEEEVKKAKALKDEQERQKQQMeqekktlqatmdAALSKQ 2552
Cdd:TIGR00618 374 QHTLTQHIHTLQQQ-----KTTLTQKLQSL----CKELDILQREQATIDTRTSAFRDLQGQL------------AHAKKQ 432
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1988774682 2553 KEAEEEMLRKQKEMQELERQRLEQERILAEE-NQKLREKLQQLEDAQ 2598
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIHLQEsAQSLKEREQQLQTKE 479
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1687-1974 |
1.22e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1687 KQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEM 1766
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1767 DILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQ----IAEEEAARQRAEAERILKEKLA 1842
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaaLEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1843 AISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQR 1922
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 1923 RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKL 1974
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2435-2568 |
1.28e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2435 SKEADDLRKAIADLENEKARLKKEAEELQNKSKEmadAQQKKiehektvlqqtfmteKEMLLKKEKLIEDEKK---RLES 2511
Cdd:PRK00409 512 GEDKEKLNELIASLEELERELEQKAEEAEALLKE---AEKLK---------------EELEEKKEKLQEEEDKlleEAEK 573
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 2512 QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDA-----ALSKQKEAEEEMLRKQKEMQE 2568
Cdd:PRK00409 574 EAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELiearkRLNKANEKKEKKKKKQKEKQE 635
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1343-1557 |
1.29e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1343 QRRLDDEEKAAEKLKAEERKKMAEMQaelDKQKQLAEAHAKAIAKAEKEAQElKLKMqeevSKREIAAVDAEKQktniQL 1422
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELE---EKKEKLQEEEDKLLEEAEKEAQQ-AIKE----AKKEADEIIKELR----QL 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1423 ELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYtaeSELKQlrdraaEAEKLRKLAQDEAeklr 1502
Cdd:PRK00409 597 QKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVKY---LSLGQ------KGEVLSIPDDKEA---- 663
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 1503 kQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEK------LR-MQAEEAERQVKQA 1557
Cdd:PRK00409 664 -IVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTvsleldLRgMRYEEALERLDKY 724
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
41-149 |
1.30e-05 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 47.29 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 41 ERDRVQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEV---------LSGETLPREKGRMRfhKLQNVQIALDF 111
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1988774682 112 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2285-2612 |
1.31e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.55 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2285 RLRQIAEDDLNQQRALAEKMLKEKMQAIQE---ASRLKAEAEMLQKQKDLAqEQAQKLLEDKQLMQQRLEEETEEY---- 2357
Cdd:NF033838 92 KLSDIKTEYLYELNVLKEKSEAELTSKTKKeldAAFEQFKKDTLEPGKKVA-EATKKVEEAEKKAKDQKEEDRRNYptnt 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2358 HKSLEVERKRQLEIMAEAERlrlqvsQLSEAQARAEEEAKKFKKQADKVATRlheteiatQEKMTVVERLEFERlntsKE 2437
Cdd:NF033838 171 YKTLELEIAESDVEVKKAEL------ELVKEEAKEPRDEEKIKQAKAKVESK--------KAEATRLEKIKTDR----EK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2438 ADDLRKAIADLENEKARLKKEAEELQNKSKEMA--------DAQQKKIEHEKT----VLQQTFMTEKemlLKKEKLI-ED 2504
Cdd:NF033838 233 AEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAkrgvlgepATPDKKENDAKSsdssVGEETLPSPS---LKPEKKVaEA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2505 EKKRLESQfeeevKKAKALKDEQERQKQQMEQekKTLQATMDAALSKQKEAEEEMLRKQ-KEMQELERQRLEQERILAEE 2583
Cdd:NF033838 310 EKKVEEAK-----KKAKDQKEEDRRNYPTNTY--KTLELEIAESDVKVKEAELELVKEEaKEPRNEEKIKQAKAKVESKK 382
|
330 340 350
....*....|....*....|....*....|...
gi 1988774682 2584 NQKLR-EKLQQLEDAQKDQHTR---ETDKVLHK 2612
Cdd:NF033838 383 AEATRlEKIKTDRKKAEEEAKRkaaEEDKVKEK 415
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1431-1977 |
1.32e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1431 SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQdEAEKLRKQVSEETQ 1510
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIK-TAESDLSMELEKNN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1511 KKRQAEEELKRkseAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAeiekEKQIKVAHEAAQKsaAAELQSKHMSFAEK 1590
Cdd:PRK01156 274 YYKELEERHMK---IINDPVYKNRNYINDYFKYKNDIENKKQILSNI----DAEINKYHAIIKK--LSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1591 TSKLEE------SLKQEHGAVLQLQQEAERLKKQqedaensREEAEKELEKWRQKANEALRLRLQAEDE--AHKKTLAQE 1662
Cdd:PRK01156 345 KSRYDDlnnqilELEGYEMDYNSYLKSIESLKKK-------IEEYSKNIERMSAFISEILKIQEIDPDAikKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1663 EAEKQKEEAEREAKKRakaeesALKQKEMaeeELERQRKIAESTAQQKLT----AEQELIRLRADFDNaeqQRSLLEDEL 1738
Cdd:PRK01156 418 LQDISSKVSSLNQRIR------ALRENLD---ELSRNMEMLNGQSVCPVCgttlGEEKSNHIINHYNE---KKSRLEEKI 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1739 YRLKNEVAAAQQQRKQLE--------DELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRA 1810
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKkrkeylesEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1811 ISEE---AKHQRQIAEEEAARQRAEaerilkEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAY----QRKALE 1883
Cdd:PRK01156 566 KRTSwlnALAVISLIDIETNRSRSN------EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANnlnnKYNEIQ 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1884 DQASQhKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQS 1963
Cdd:PRK01156 640 ENKIL-IEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDR 717
|
570
....*....|....
gi 1988774682 1964 KIRAEEEAEKLRKL 1977
Cdd:PRK01156 718 INDINETLESMKKI 731
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2254-2597 |
1.33e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2254 STQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQ-QRALAekmLKEKMQAIQE-----ASRLkAEAEMLQK 2327
Cdd:COG3096 296 GARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLvQTALR---QQEKIERYQEdleelTERL-EEQEEVVE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2328 QKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQ------LEIMAEAERLrLQVSQLSEAQARAEEEAkkFKK 2401
Cdd:COG3096 372 EAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyqqaVQALEKARAL-CGLPDLTPENAEDYLAA--FRA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2402 QADKV-------ATRLHETEIATQE---KMTVVERL--EFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEM 2469
Cdd:COG3096 449 KEQQAteevlelEQKLSVADAARRQfekAYELVCKIagEVERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2470 AdaQQKKIEHEKTVLQQTFMTEkemlLKKEKLIEDEKKRLESQFEE---EVKKAKALKDEQERQKQQMEQEKKTLQA--- 2543
Cdd:COG3096 529 R--QQQNAERLLEEFCQRIGQQ----LDAAEELEELLAELEAQLEEleeQAAEAVEQRSELRQQLEQLRARIKELAArap 602
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774682 2544 ---TMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDA 2597
Cdd:COG3096 603 awlAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQ 659
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
45-146 |
1.40e-05 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 47.41 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 45 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRF----HKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1988774682 121 NIRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1575-1834 |
1.46e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1575 SAAAELQSKHMSFAEKTSKLEESLKQehgaVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAlrlrlQAEDEA 1654
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-----EAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1655 HKKTLaqeeaekqkeeaereaKKRAKAE-------------------ESALKQKEMAEEELERQRKIAESTAQQKLTAEQ 1715
Cdd:COG3883 84 RREEL----------------GERARALyrsggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1716 ELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEA 1795
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 1988774682 1796 AKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAE 1834
Cdd:COG3883 228 AAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1125-1653 |
1.58e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.33 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1125 KEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKA--------------SAVSDKM----VRVHSERD---VELDHFRQQL 1183
Cdd:pfam01576 517 RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLqrelealtqqleekAAAYDKLektkNRLQQELDdllVDLDHQRQLV 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1184 SSLQDRWKavftQIDLRQRELEQLGRQLGYYRESydwlirwiADAKQRQEKIQAVPITdsktlkeqlaqekKLLEEIEQN 1263
Cdd:pfam01576 597 SNLEKKQK----KFDQMLAEEKAISARYAEERDR--------AEAEAREKETRALSLA-------------RALEEALEA 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1264 KDKVDECQKYAKAYIDtikdyelQLVAYKAQVEPLVSPLKKTKldSASDNIIQEyvtLRTRYSElmtltsqyikfitdtq 1343
Cdd:pfam01576 652 KEELERTNKQLRAEME-------DLVSSKDDVGKNVHELERSK--RALEQQVEE---MKTQLEE---------------- 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1344 rrLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKA-EKEAQELKLKMQEEVSKREIAAvdAEKQKtnIQL 1422
Cdd:pfam01576 704 --LEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQlVKQVRELEAELEDERKQRAQAV--AAKKK--LEL 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1423 ELQELknlsEQQIKDKSQQVDEALHSRTKIE----------EEIRLIR----IQLETTEKQKYTAESELKQLRDRAAEAE 1488
Cdd:pfam01576 778 DLKEL----EAQIDAANKGREEAVKQLKKLQaqmkdlqrelEEARASRdeilAQSKESEKKLKNLEAELLQLQEDLAASE 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1489 KLRKLAQDEAEKLRKQVSEETQKKRQAEEElKRKSEAEkeaAKQKQKALEDLE-KLRMQAEEAERQVKQAE-IEKEKQIK 1566
Cdd:pfam01576 854 RARRQAQQERDELADEIASGASGKSALQDE-KRRLEAR---IAQLEEELEEEQsNTELLNDRLRKSTLQVEqLTTELAAE 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1567 VAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEH-GAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALr 1645
Cdd:pfam01576 930 RSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFkSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVL- 1008
|
....*...
gi 1988774682 1646 lrLQAEDE 1653
Cdd:pfam01576 1009 --LQVEDE 1014
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1326-1583 |
1.66e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 51.37 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1326 SELMTLTSQYIKFITD---TQRRLDDEEKAaeklkAEERKKMaemqaELDKQKQLAeahakAIAKAEKEAQELKLKMQEE 1402
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERA-----EADRQRL-----EQEKQQQLA-----AISGSQSQLESTDQNALET 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1403 VSKREIAAVDAEKQKTNIQLE--LQELKNLSEQQ-----------------IKDKSQ-QVDEA-LHSRTKIEEeirliri 1461
Cdd:NF012221 1603 NGQAQRDAILEESRAVTKELTtlAQGLDALDSQAtyagesgdqwrnpfaggLLDRVQeQLDDAkKISGKQLAD------- 1675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1462 qlettEKQKYTAesELKQLRDRAAEAEKlrklAQDEAEKLRKQVSEETQKKR-QAEeelKRKSEA---EKEAAKQKQKAL 1537
Cdd:NF012221 1676 -----AKQRHVD--NQQKVKDAVAKSEA----GVAQGEQNQANAEQDIDDAKaDAE---KRKDDAlakQNEAQQAESDAN 1741
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1988774682 1538 EDLEKLRMQaeeAERQVKQAEIEKEKqikvaheaAQKSAAAELQSK 1583
Cdd:NF012221 1742 AAANDAQSR---GEQDASAAENKANQ--------AQADAKGAKQDE 1776
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2310-2598 |
1.73e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2310 QAIQEASRLKAEAEMLqKQKDLAQEQAQKLLEDKQLMQQRLEEET--EEYHKSLEVERKRQLEIM---------AEAERL 2378
Cdd:COG3206 75 SLSASDSPLETQIEIL-KSRPVLERVVDKLNLDEDPLGEEASREAaiERLRKNLTVEPVKGSNVIeisytspdpELAAAV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2379 ------RLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEkmtvverleFER----LNTSKEADDLRKAIADL 2448
Cdd:COG3206 154 analaeAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE---------FRQknglVDLSEEAKLLLQQLSEL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2449 ENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEkemLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQE 2528
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774682 2529 RQKQQMEQEKKTLQATMDAALSKQKeAEEEMLRKQ--------KEMQELERQRLEQERILAEENQKLREKLQQLEDAQ 2598
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAELEALQ-AREASLQAQlaqlearlAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
36-154 |
1.75e-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: 47.75 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 36 DGRKDERDRVQKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKL 102
Cdd:cd21325 15 EGTQHSYSEEEKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQ 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 103 QNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 154
Cdd:cd21325 95 ENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1343-1568 |
1.83e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 50.14 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1343 QRRLDDEEKAAEKLK----AEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEevskreiaavdAEKQKT 1418
Cdd:pfam09787 17 ARILQSKEKLIASLKegsgVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE-----------LEAQQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1419 NIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRiqlETTEKQKYTAESELKQLrdraaeaeklrklaQDEA 1498
Cdd:pfam09787 86 EEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLE---EELRRSKATLQSRIKDR--------------EAEI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774682 1499 EKLRKQVSEETQKKRQaEEELKRKSEAEKEAAKQKQKALEDL--EK--LRMQAEEAERQVKQAEIEKEKQIKVA 1568
Cdd:pfam09787 149 EKLRNQLTSKSQSSSS-QSELENRLHQLTETLIQKQTMLEALstEKnsLVLQLERMEQQIKELQGEGSNGTSIN 221
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1453-1643 |
1.86e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1453 EEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQ 1532
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1533 KQKALEDLEKL--------------RMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsFAEKTSKLEESL 1598
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1988774682 1599 KQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEA 1643
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2270-2481 |
1.91e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2270 AEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQR 2349
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2350 LEEETEEYhksleVERKRQLEIMAEAERLRLQVSQ------------LSEAQARAEEEAKKFKKQADKVATRLHETEIAT 2417
Cdd:COG4942 99 LEAQKEEL-----AELLRALYRLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774682 2418 QEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEK 2481
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
2278-2585 |
1.95e-05 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 51.10 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2278 VEAQEAARLRQIAEDDLNQQRAlaekmlkekmQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE--DKQLMQQR--LEEE 2353
Cdd:pfam15818 10 LEALEELRMRREAETQYEEQIG----------KIIVETQELKWQKETLQNQKETLAKQHKEAMAvfKKQLQMKMcaLEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2354 TEEYHKSLEVERKrqlEIMAEAERLR-LQVSQLSEAQARAEEEAKKfkkQADKVATRLHETEIATQEK--MTVVERLEFE 2430
Cdd:pfam15818 80 KGKYQLATEIKEK---EIEGLKETLKaLQVSKYSLQKKVSEMEQKL---QLHLLAKEDHHKQLNEIEKyyATITGQFGLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2431 RLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEhEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLE 2510
Cdd:pfam15818 154 KENHGKLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIK-SKVTCQYKMGEENINLTIKEQKFQELQERLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2511 SQFEEEVKKAKALKDEQERQK---------QQMEQEKKTLQATMDAALSKQKEaEEEMLRKQKEMQElERQRLEQERILA 2581
Cdd:pfam15818 233 MELELNKKINEEITHIQEEKQdiiisfqhmQQLLQQQTQANTEMEAELKALKE-NNQTLERDNELQR-EKVKENEEKFLN 310
|
....
gi 1988774682 2582 EENQ 2585
Cdd:pfam15818 311 LQNE 314
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1508-1825 |
1.98e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 50.36 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1508 ETQKKRQAE--EELKRKSEAEKEAAKQKQKALEDLEKlrmqaeeAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHM 1585
Cdd:PRK07735 8 EDLKKEAARraKEEARKRLVAKHGAEISKLEEENREK-------EKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1586 SFAEKTSklEESLKQEHGAVLQLQQEAERLKKQQEdaENSREEAEKELEKWRQKANEALRLRLQAedeahkktlaqeeae 1665
Cdd:PRK07735 81 GTEEVTE--EEKAKAKAKAAAAAKAKAAALAKQKR--EGTEEVTEEEKAAAKAKAAAAAKAKAAA--------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1666 kqkeeaerEAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQqrslleDELYRLKNEV 1745
Cdd:PRK07735 142 --------LAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTE------EEKAKAKAKA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1746 AAAQQQRKQledELAKvrsemdiliQLKTKAEKETMSNTEKSKQlleAEAAKMKdlAEEASRLRAISEEAKHQRQIAEEE 1825
Cdd:PRK07735 208 AAAAKAKAA---ALAK---------QKASQGNGDSGDEDAKAKA---IAAAKAK--AAAAARAKTKGAEGKKEEEPKQEE 270
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1348-1600 |
2.00e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.72 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1348 DEEKAAEKLKAEERKKMAEMQAELDKQKQLAEahakaiAKAEKEAQELKLKMQEEvskreiaavdaekqktniqLELqel 1427
Cdd:pfam15709 329 EQEKASRDRLRAERAEMRRLEVERKRREQEEQ------RRLQQEQLERAEKMREE-------------------LEL--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1428 knlsEQQikdksqqvdealhsrtKIEEEIRLIRIQLEttEKQKYTAESELKQLRDRAAEAEKLRKlaqdEAEKLRKQVSE 1507
Cdd:pfam15709 381 ----EQQ----------------RRFEEIRLRKQRLE--EERQRQEEEERKQRLQLQAAQERARQ----QQEEFRRKLQE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1508 ETQKKRQAEEElkrKSEAEKEAAKQKQKALEDLEKLRMQAEEAER----QVKQAEIEKEKQikvahEAAQKSAAAELQSK 1583
Cdd:pfam15709 435 LQRKKQQEEAE---RAEAEKQRQKELEMQLAEEQKRLMEMAEEERleyqRQKQEAEEKARL-----EAEERRQKEEEAAR 506
|
250
....*....|....*..
gi 1988774682 1584 hMSFAEKTSKLEESLKQ 1600
Cdd:pfam15709 507 -LALEEAMKQAQEQARQ 522
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1226-1542 |
2.05e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.07 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1226 ADAKQRQEKI--QAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQ-VEPLVSPL 1302
Cdd:PRK11281 39 ADVQAQLDALnkQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDnDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1303 KKT-------KLDSASDNIIQEYVTLRTRYSELMTLTSQYI---KFITDTQRR-------LDDEEKAAEKLKAEERKKMA 1365
Cdd:PRK11281 119 STLslrqlesRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraqAALYANSQRlqqirnlLKGGKVGGKALRPSQRVLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1366 EMQAELDKQ-------------------KQLAEAHAKaIAKAEKEAQEL-------KLKMQEEVSKREIAAVDAEKQKTN 1419
Cdd:PRK11281 199 AEQALLNAQndlqrkslegntqlqdllqKQRDYLTAR-IQRLEHQLQLLqeainskRLTLSEKTVQEAQSQDEAARIQAN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1420 --IQLEL--------------QELKNLSEQQIKDKsQQVDEALHSRTKIEEEIR-------LIRIQLEttEKQKYTAESE 1476
Cdd:PRK11281 278 plVAQELeinlqlsqrllkatEKLNTLTQQNLRVK-NWLDRLTQSERNIKEQISvlkgsllLSRILYQ--QQQALPSADL 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 1477 LKQLRDRAAeaeKLRkLAQDEAEKLRKQVSE-----ETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEK 1542
Cdd:PRK11281 355 IEGLADRIA---DLR-LEQFEINQQRDALFQpdayiDKLEAGHKSEVTDEVRDALLQLLDERRELLDQLNK 421
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2424-2613 |
2.07e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2424 VERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMAD-------AQQKKIEHEKTVLQQTFMTEKEMLL 2496
Cdd:PHA02562 236 IEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2497 KKEKLIEDEKKRLESQFEEEVKKAKALKDeqerqkqQMEQEKKTLQATMDAALskqkeaeeemlRKQKEMQELERQRLEQ 2576
Cdd:PHA02562 316 EKLDTAIDELEEIMDEFNEQSKKLLELKN-------KISTNKQSLITLVDKAK-----------KVKAAIEELQAEFVDN 377
|
170 180 190
....*....|....*....|....*....|....*..
gi 1988774682 2577 ERILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKD 2613
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1722-2173 |
2.22e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.68 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1722 ADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKE---TMSNTEKSKQLLEAeaakM 1798
Cdd:COG5278 79 EPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEaalALVRSGEGKALMDE----I 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1799 KDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQ 1878
Cdd:COG5278 155 RARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1879 RKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAD 1958
Cdd:COG5278 235 LAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1959 ETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQI 2038
Cdd:COG5278 315 AAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2039 VVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEA 2118
Cdd:COG5278 395 IAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAAL 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 2119 ANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQ 2173
Cdd:COG5278 475 AALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAE 529
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1613-1857 |
2.28e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.26 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1613 ERLKKQQEDAENSREEAEKELEKWRQKANealrlRLQAEDEAHKKtlaqeeaekqkeeaeREAKKRAKAEESALKQKEMA 1692
Cdd:COG2268 192 RKIAEIIRDARIAEAEAERETEIAIAQAN-----REAEEAELEQE---------------REIETARIAEAEAELAKKKA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1693 EEELERQRKIAESTAQQKLtaeqelirlradfdnaeqqrslledelyrlknevaAAQQQRKQLEDELAKVRSEMDILIQL 1772
Cdd:COG2268 252 EERREAETARAEAEAAYEI-----------------------------------AEANAEREVQRQLEIAEREREIELQE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1773 KTKAEKEtmsNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKhqrqiAEEEAARQRAEAERILKEklAAISEAtRLKT 1852
Cdd:COG2268 297 KEAEREE---AELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGL-----AEAEGKRALAEAWNKLGD--AAILLM-LIEK 365
|
....*
gi 1988774682 1853 EAEIA 1857
Cdd:COG2268 366 LPEIA 370
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2452-2624 |
2.65e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.34 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2452 KARLKKEAEELQNKSKEMADAQQKKIEhektvLQQTFMTEkEMLLKKEKLiEDEKKRLEsqfEEEVKKAKALKDEQERQK 2531
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELE-----LEQQRRFE-EIRLRKQRL-EEERQRQE---EEERKQRLQLQAAQERAR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2532 QQMEQEKKTLQatmDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAE--ENQKLREKLQQLEDAQKDQHTRETDKV 2609
Cdd:pfam15709 423 QQQEEFRRKLQ---ELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEmaEEERLEYQRQKQEAEEKARLEAEERRQ 499
|
170
....*....|....*
gi 1988774682 2610 LHKDIIHLTTIETTK 2624
Cdd:pfam15709 500 KEEEAARLALEEAMK 514
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2167-2338 |
2.67e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2167 AEQTLkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELL------KLKNKI 2240
Cdd:COG3206 194 AEAAL-EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLqspviqQLRAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2241 EEENQRLIKKDKDST------QKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQE 2314
Cdd:COG3206 273 AELEAELAELSARYTpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
170 180 190
....*....|....*....|....*....|..
gi 1988774682 2315 ASRLKAEAE--------MLQKQKDLAQEQAQK 2338
Cdd:COG3206 353 LRRLEREVEvarelyesLLQRLEEARLAEALT 384
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1126-2036 |
2.70e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.82 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1126 EVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRW-KAVFTQIDLRQREL 1204
Cdd:TIGR01612 780 ELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFlNKVDKFINFENNCK 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1205 EQLGRQlgyyRESYDWLIRWI-ADAKQRQEKIQAVPITDSKTLkeqLAQEKKLLEEIEQNKD---KVDECQKYAKAYIDT 1280
Cdd:TIGR01612 860 EKIDSE----HEQFAELTNKIkAEISDDKLNDYEKKFNDSKSL---INEINKSIEEEYQNINtlkKVDEYIKICENTKES 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1281 IKDYELQLVAYKAQVEPLVSPLKKTkldsasdNIIQEyvtlrtryselmTLTSQYIKFITDTQRRLDDEEKAAEkLKAEE 1360
Cdd:TIGR01612 933 IEKFHNKQNILKEILNKNIDTIKES-------NLIEK------------SYKDKFDNTLIDKINELDKAFKDAS-LNDYE 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1361 RKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAqelklkmQEEVSKREIAAVDAEKQKTNIQLELQ-ELKNLSEQQIKDKS 1439
Cdd:TIGR01612 993 AKNNELIKYFNDLKANLGKNKENMLYHQFDEK-------EKATNDIEQKIEDANKNIPNIEIAIHtSIYNIIDEIEKEIG 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1440 QQVdEALHSRTKIEEEIRLIRIQlETTEKQKYTAESELKQlRDRAAEAEKLRKLAQDeaeklRKQVSEETQKKRQAEEEL 1519
Cdd:TIGR01612 1066 KNI-ELLNKEILEEAEINITNFN-EIKEKLKHYNFDDFGK-EENIKYADEINKIKDD-----IKNLDQKIDHHIKALEEI 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1520 KRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAE-----IEKEKQI-----KVAHEAAQ----KSAAAELQSKHM 1585
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIEnivtkIDKKKNIydeikKLLNEIAEiekdKTSLEEVKGINL 1217
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1586 SFAEKTSKL------EESLKQEH--GAVLQLQQEAERLKKQQEDAENsreeaEKELEKWRQKANEALRLRlQAEDEAHKK 1657
Cdd:TIGR01612 1218 SYGKNLGKLflekidEEKKKSEHmiKAMEAYIEDLDEIKEKSPEIEN-----EMGIEMDIKAEMETFNIS-HDDDKDHHI 1291
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1658 TLAQEEAEKQKEEAEREAKKRAKAEESALK--QKEMAEEELERQRKIAE-STAQQKLTAEQELIRL---RADFDNAEQQR 1731
Cdd:TIGR01612 1292 ISKKHDENISDIREKSLKIIEDFSEESDINdiKKELQKNLLDAQKHNSDiNLYLNEIANIYNILKLnkiKKIIDEVKEYT 1371
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1732 SLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKM-------KDLAEE 1804
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIdtyfknaDENNEN 1451
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1805 ASRLRAISEEAKHQRQ-IAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEaENERLRRQAEDEA------Y 1877
Cdd:TIGR01612 1452 VLLLFKNIEMADNKSQhILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIE-KNKELFEQYKKDVtellnkY 1530
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1878 QRKALEDQASQHKQEIEEKIVQLKKSS-----EAEMERQKaiVDDTLKQRRVVEEEIRilklNFEKASSGKLDLELEL-- 1950
Cdd:TIGR01612 1531 SALAIKNKFAKTKKDSEIIIKEIKDAHkkfilEAEKSEQK--IKEIKKEKFRIEDDAA----KNDKSNKAAIDIQLSLen 1604
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1951 --NKLKNIAD-ETQQSKIRAEEEA--EKLRKLALEEEKRRreaeekvkkiAAAEEEAARQRKAALEELERLRKKAEEARK 2025
Cdd:TIGR01612 1605 feNKFLKISDiKKKINDCLKETESieKKISSFSIDSQDTE----------LKENGDNLNSLQEFLESLKDQKKNIEDKKK 1674
|
970
....*....|.
gi 1988774682 2026 QKDEADKEAEK 2036
Cdd:TIGR01612 1675 ELDELDSEIEK 1685
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2232-2606 |
2.95e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 50.57 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2232 ELLKLKNKIEEENQRLIKKDKDSTQ-KLLAEEAENMRKLAEDAARL----------SVEaQEAARLRQIAEDDLNQQRAL 2300
Cdd:PRK10246 455 EQTQRNAALNEMRQRYKEKTQQLADvKTICEQEARIKDLEAQRAQLqagqpcplcgSTS-HPAVEAYQALEPGVNQSRLD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2301 AekMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDkqlmQQRLEEETEEYHKSLEVERKRQLEI---MAEAER 2377
Cdd:PRK10246 534 A--LEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQE----EQALTQQWQAVCASLNITLQPQDDIqpwLDAQEE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2378 LRLQVSQLSeaqaraeeeaKKFKKQADKVATRLHETEIATQekmtvverLEFERLNTSKEADDLRKAIADLENEKARL-- 2455
Cdd:PRK10246 608 HERQLRLLS----------QRHELQGQIAAHNQQIIQYQQQ--------IEQRQQQLLTALAGYALTLPQEDEEASWLat 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2456 -KKEAEELQNKSKEMADAQQKKieHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfeeevkkAKALKDEQERQKQQM 2534
Cdd:PRK10246 670 rQQEAQSWQQRQNELTALQNRI--QQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQ-------CLSLHSQLQTLQQQD 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2535 EQEKKTL---QATMDAALSKQ----KEA-------EEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKD 2600
Cdd:PRK10246 741 VLEAQRLqkaQAQFDTALQASvfddQQAflaalldEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDL 820
|
....*.
gi 1988774682 2601 QHTRET 2606
Cdd:PRK10246 821 TVTVEQ 826
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1451-1601 |
3.06e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1451 KIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKS------- 1523
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyea 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1524 -EAEKEAAKQKQKALEDLEK-LRMQAEEAERQVK--QAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLK 1599
Cdd:COG1579 94 lQKEIESLKRRISDLEDEILeLMERIEELEEELAelEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
..
gi 1988774682 1600 QE 1601
Cdd:COG1579 174 PE 175
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2496-2600 |
3.13e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.68 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2496 LKKEKLIEDEKKRLESQFEEevkkAKALKDEQERQKQQMEQEKKTLQAtmdaALSKQKEAEEEMLRKQKEMQELERQRLE 2575
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQ----TLALLDKIDRQKEETEQLKQQLAQ----APAKLRQAQAELEALKDDNDEETRETLS 119
|
90 100
....*....|....*....|....*
gi 1988774682 2576 QERiLAEENQKLREKLQQLEDAQKD 2600
Cdd:PRK11281 120 TLS-LRQLESRLAQTLDQLQNAQND 143
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4129-4157 |
3.15e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 3.15e-05
10 20
....*....|....*....|....*....
gi 1988774682 4129 VRKRRVVIVDPETGKEMTVYEAYRKGLID 4157
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2150-2603 |
3.24e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.12 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2150 LMQKQQADTEMAKHKKLAEQTLKQKFqveqeLTKVKLKLDETDKQKSVLDEELQRLKDEVDD----AVKQRGQVEEELFK 2225
Cdd:pfam05557 59 LLEKREAEAEEALREQAELNRLKKKY-----LEALNKKLNEKESQLADAREVISCLKNELSElrrqIQRAELELQSTNSE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2226 VKVQMEELLKLKNKIEEENQRliKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEA----ARLRQIAEDDLNQQRALA 2301
Cdd:pfam05557 134 LEELQERLDLLKAKASEAEQL--RQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVknskSELARIPELEKELERLRE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2302 E-KMLKEkmqAIQEASRLKAEAEMLQKQKDlAQEQAQKLLEDKQLMQQRLEEETEEYHK----------SLEVERKRQLE 2370
Cdd:pfam05557 212 HnKHLNE---NIENKLLLKEEVEDLKRKLE-REEKYREEAATLELEKEKLEQELQSWVKlaqdtglnlrSPEDLSRRIEQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2371 IMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLEN 2450
Cdd:pfam05557 288 LQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDK 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2451 E---------KARLKKEAEEL----QNKSKEMaDAQQKKIEHEKTVL-QQTFMTEKEMLLKKEKLIEDEKKRLESQFEEE 2516
Cdd:pfam05557 368 EltmsnyspqLLERIEEAEDMtqkmQAHNEEM-EAQLSVAEEELGGYkQQAQTLERELQALRQQESLADPSYSKEEVDSL 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2517 VKKAKALKDEQERQKQQ-----MEQEKKTLQATMDAALSKQkeaeeeMLRKQKEMQELERQRLEQERILAEENQKLREKL 2591
Cdd:pfam05557 447 RRKLETLELERQRLREQkneleMELERRCLQGDYDPKKTKV------LHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLL 520
|
490
....*....|..
gi 1988774682 2592 QQLEDAQKDQHT 2603
Cdd:pfam05557 521 KKLEDDLEQVLR 532
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2279-2601 |
3.36e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.87 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2279 EAQEAAR-LRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDkqlMQQRLEEETEEY 2357
Cdd:pfam02029 3 DEEEAAReRRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDR---TAKREERRQKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2358 HKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKV---ATRLHETEIATQEKMTVVERLEfERLNT 2434
Cdd:pfam02029 80 QEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYkeeETEIREKEYQENKWSTEVRQAE-EEGEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2435 SKEADDLRKAI--ADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQ 2512
Cdd:pfam02029 159 EEDKSEEAEEVptENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2513 FEEEVKKAKALKDEQERQKQQME-QEKKTLQatmdaalSKQKEAE---EEMLRKQKE---MQELERQRLEQERILA---- 2581
Cdd:pfam02029 239 EAEVFLEAEQKLEELRRRRQEKEsEEFEKLR-------QKQQEAElelEELKKKREErrkLLEEEEQRRKQEEAERklre 311
|
330 340
....*....|....*....|...
gi 1988774682 2582 -EENQKLREKLQ--QLEDAQKDQ 2601
Cdd:pfam02029 312 eEEKRRMKEEIErrRAEAAEKRQ 334
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1449-1542 |
3.58e-05 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 46.28 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1449 RTKIEEEIRLIRIQLETTEKQKYTAESELKQLRdraAEAEKLRKLAQDEAEKLRKQVseetqkKRQAEEELKR-KSEAEK 1527
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEI------LAEAKEEAERiLEQAKA 102
|
90
....*....|....*
gi 1988774682 1528 EAAKQKQKALEDLEK 1542
Cdd:cd06503 103 EIEQEKEKALAELRK 117
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1134-1640 |
3.69e-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: 50.02 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1134 LKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQlgrqlgy 1213
Cdd:TIGR04523 234 IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1214 yresyDWlirwiadakqrqekiqavpitdSKTLKEQLAQEKKLLEEIEqnkDKVDECQKYAKAYIDTIKDyelqlvayka 1293
Cdd:TIGR04523 307 -----DW----------------------NKELKSELKNQEKKLEEIQ---NQISQNNKIISQLNEQISQ---------- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1294 qveplvspLKKTKLDSASDNiiqeyvtlRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKkmaemqaeLDK 1373
Cdd:TIGR04523 347 --------LKKELTNSESEN--------SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK--------IQN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1374 QKQLAEAHAKAIAKAEKEAQEL-----KLKMQEEVSKREIAavDAEKQKTNIQLELQELKNLSEQQikdkSQQVDEalhs 1448
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLekeieRLKETIIKNNSEIK--DLTNQDSVKELIIKNLDNTRESL----ETQLKV---- 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1449 rtkIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKlrklaqdEAEKLRKQVSEETQKKRQAEEElkrKSEAEKE 1528
Cdd:TIGR04523 473 ---LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE-------KVKDLTKKISSLKEKIEKLESE---KKEKESK 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1529 AAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQehgaVLQL 1608
Cdd:TIGR04523 540 ISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK----ISSL 615
|
490 500 510
....*....|....*....|....*....|..
gi 1988774682 1609 QQEAERLKKQQEDAENSREEAEKELEKWRQKA 1640
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1341-1634 |
3.84e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 49.59 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1341 DTQRRLDD-EEKAAEKLKAEERKKMAEMQAElDKQKQLAEAHAKAIAKAEKEAQELklkmqEEVSKREIAAVDAEKQKTN 1419
Cdd:PRK07735 2 DPEKDLEDlKKEAARRAKEEARKRLVAKHGA-EISKLEEENREKEKALPKNDDMTI-----EEAKRRAAAAAKAKAAALA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1420 IQLELQELKNLSEQQIKDKSQQVDEAlhsrtkieeeirliRIQLETTEKQKYTAESELKQlRDRAAEAEKLRKLAQDEAE 1499
Cdd:PRK07735 76 KQKREGTEEVTEEEKAKAKAKAAAAA--------------KAKAAALAKQKREGTEEVTE-EEKAAAKAKAAAAAKAKAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1500 KLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVaheAAQKSAAAE 1579
Cdd:PRK07735 141 ALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAA---AAAKAKAAA 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 1580 LQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKkqQEDAENSREEAEKELE 1634
Cdd:PRK07735 218 LAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAK--TKGAEGKKEEEPKQEE 270
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2169-2593 |
4.27e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 49.64 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2169 QTLKQKFQVEQELTKVKlkldetdkqksvldEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEEL-LKLKNKIEEENQRl 2247
Cdd:pfam05701 32 QTVERRKLVELELEKVQ--------------EEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELkLNLERAQTEEAQA- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2248 iKKDKDstqklLAE-EAENMRKLAEDAARLSVEAQ-EAARLRQIAeddlnqqrALAE-KMLKEKMQAIQEasrlkaEAEM 2324
Cdd:pfam05701 97 -KQDSE-----LAKlRVEEMEQGIADEASVAAKAQlEVAKARHAA--------AVAElKSVKEELESLRK------EYAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2325 LQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEY---HKSLEVERKRQLEimAEAERLRLQVSqlseaqaraeeeakkfkK 2401
Cdd:pfam05701 157 LVSERDIAIKRAEEAVSASKEIEKTVEELTIELiatKESLESAHAAHLE--AEEHRIGAALA-----------------R 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2402 QADKVAtrlHETEIATQEKmtvverlEFERLNtskeaDDLRKAiadlENEKARLKKEAEELQNKSKEMADAQQKKIEHEK 2481
Cdd:pfam05701 218 EQDKLN---WEKELKQAEE-------ELQRLN-----QQLLSA----KDLKSKLETASALLLDLKAELAAYMESKLKEEA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2482 TVLQQTFMTE---KEMLLKKEKLIEDEKKRLESQfEEEVK----KAKALKDEQERQK------QQ-----------MEQE 2537
Cdd:pfam05701 279 DGEGNEKKTStsiQAALASAKKELEEVKANIEKA-KDEVNclrvAAASLRSELEKEKaelaslRQregmasiavssLEAE 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2538 KKTLQATMDAALSKQKEAEEEMLRKQKEMQElERQRLEQERILA----EENQKLREKLQQ 2593
Cdd:pfam05701 358 LNRTKSEIALVQAKEKEAREKMVELPKQLQQ-AAQEAEEAKSLAqaarEELRKAKEEAEQ 416
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1447-1618 |
4.29e-05 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 50.04 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1447 HSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAE-AEKLRKlAQDEAEKLRKQVSEETQKKRQAEEELkrkSEA 1525
Cdd:pfam10168 554 LAREEIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKlAEKYEE-IKDKQEKLMRRCKKVLQRLNSQLPVL---SDA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1526 EKEAAKQkqkaledLEKLRMQAEEAERQVKQAEIEKEKQIKvaHEAAQKSAAaelQSKHMSFAEKTSK-LEESLKQEHGA 1604
Cdd:pfam10168 630 EREMKKE-------LETINEQLKHLANAIKQAKKKMNYQRY--QIAKSQSIR---KKSSLSLSEKQRKtIKEILKQLGSE 697
|
170
....*....|....
gi 1988774682 1605 VLQLQQEAERLKKQ 1618
Cdd:pfam10168 698 IDELIKQVKDINKH 711
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
2502-2636 |
4.45e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.86 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2502 IEDEKKRLeSQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATmdaaLSKQKEAEEEMLRKQKEMQELER--QRLEQERI 2579
Cdd:COG2433 408 LTEEEEEI-RRLEEQVERLEAEVEELEAELEEKDERIERLERE----LSEARSEERREIRKDREISRLDReiERLERELE 482
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774682 2580 -LAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDIIHLTTIETTKTVYnGQNVGDVV 2636
Cdd:COG2433 483 eERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEY-GLKEGDVV 539
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2287-2595 |
4.58e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.15 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2287 RQIAEDDLNQQRALAEKMLKEKMQAIQEasRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERK 2366
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEE--EEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2367 RQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKvatrlheteiatQEKMTVVERLEFERLNTSKEADdlrkaia 2446
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE------------EEREEDERILEYLKEKAEREEE------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2447 dLENEKARLKKEAEELQNKskemADAQQKKIEHEKTvlqqtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDE 2526
Cdd:pfam13868 171 -REAEREEIEEEKEREIAR----LRAQQEKAQDEKA--------ERDELRAKLYQEEQERKERQKEREEAEKKARQRQEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2527 QERQKQQMEQEKKTLQATMDaalsKQKEAEEEMLRKQKEMQELERQRLEQERI-----------LAEENQKLREKLQQLE 2595
Cdd:pfam13868 238 QQAREEQIELKERRLAEEAE----REEEEFERMLRKQAEDEEIEQEEAEKRRMkrlehrrelekQIEEREEQRAAEREEE 313
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3996-4027 |
4.91e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.91e-05
10 20 30
....*....|....*....|....*....|..
gi 1988774682 3996 KLLSAERAVTGYRDPYTGKTISLFQAMKKGLI 4027
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1339-1536 |
5.01e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1339 ITDTQRRLDDEEKAAEKLKAEER---KKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEvsKREIAAVDAEK 1415
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAaleRRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ--KEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1416 QKTNIQLELQELKNLSE-QQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDR---------AA 1485
Cdd:COG4942 114 YRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEleeeraaleAL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 1486 EAEKLRKLAQDEAEKlrKQVSEETQKKRQAEEELKRK-SEAEKEAAKQKQKA 1536
Cdd:COG4942 194 KAERQKLLARLEKEL--AELAAELAELQQEAEELEALiARLEAEAAAAAERT 243
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1608-2061 |
5.15e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 49.64 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1608 LQQEAERLKKQQEDAENSREEAEKELEKWRqKANEALRLRL---QAEDEAHKK--TLAQEEAEKQKEEAEREAKKRAKAE 1682
Cdd:pfam05701 47 VQEEIPEYKKQSEAAEAAKAQVLEELESTK-RLIEELKLNLeraQTEEAQAKQdsELAKLRVEEMEQGIADEASVAAKAQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1683 --------ESALKQKEMAEEELERQRKIAESTAQQK-----------------------LTAE-----QELIRLRADFDN 1726
Cdd:pfam05701 126 levakarhAAAVAELKSVKEELESLRKEYASLVSERdiaikraeeavsaskeiektveeLTIEliatkESLESAHAAHLE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1727 AEQQR------------------SLLEDELYRLKNEVAAAQQQRKQLE---DELAKVRSEMDILIQLKTKAEKETMSNTE 1785
Cdd:pfam05701 206 AEEHRigaalareqdklnwekelKQAEEELQRLNQQLLSAKDLKSKLEtasALLLDLKAELAAYMESKLKEEADGEGNEK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1786 KSKQLLEAEAAKMKDLAEEasrLRAISEEAKHQRQIAEEEAARQRAEAErilKEKlAAISEATRLKTEAEIALKEKEAEN 1865
Cdd:pfam05701 286 KTSTSIQAALASAKKELEE---VKANIEKAKDEVNCLRVAAASLRSELE---KEK-AELASLRQREGMASIAVSSLEAEL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1866 ERLRrqAEDEAYQRKALEDQasqhkqeieEKIVQL-KKSSEAEMErqkaiVDDTLKQRRVVEEEIRILKLNFEKASSGKL 1944
Cdd:pfam05701 359 NRTK--SEIALVQAKEKEAR---------EKMVELpKQLQQAAQE-----AEEAKSLAQAAREELRKAKEEAEQAKAAAS 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1945 DLELELnklkniadETQQSKIRAEEEAEKLRKLALEEEKRRREAEEkvkkiAAAEEEAARQRKAALEELERLRKKAEEAR 2024
Cdd:pfam05701 423 TVESRL--------EAVLKEIEAAKASEKLALAAIKALQESESSAE-----STNQEDSPRGVTLSLEEYYELSKRAHEAE 489
|
490 500 510
....*....|....*....|....*....|....*..
gi 1988774682 2025 KQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQ 2061
Cdd:pfam05701 490 ELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEE 526
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3094-3130 |
5.20e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 5.20e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1988774682 3094 KLLSAERAVTGYRDPYTGKTVSLFQAMKKDLIPKEQG 3130
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1360-2574 |
5.29e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.05 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1360 ERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELK---LKMQEEVSK---REIAAVDAEKQKTNIQLELQE-LKNLSe 1432
Cdd:TIGR01612 535 KAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENedsIHLEKEIKDlfdKYLEIDDEIIYINKLKLELKEkIKNIS- 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1433 qqikDKSQQVDEALHSRTKIEEEIRLIRiqlETTEKQKYTAESELKQlRDRAAEAEK--LRKLAQDEAEKLRKQVSEETQ 1510
Cdd:TIGR01612 614 ----DKNEYIKKAIDLKKIIENNNAYID---ELAKISPYQVPEHLKN-KDKIYSTIKseLSKIYEDDIDALYNELSSIVK 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1511 KKRQAEEELKRKSEAEKEAAKQKQKALEDleklrMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSaaaelqskHMSFAEK 1590
Cdd:TIGR01612 686 ENAIDNTEDKAKLDDLKSKIDKEYDKIQN-----METATVELHLSNIENKKNELLDIIVEIKKHI--------HGEINKD 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1591 TSKLEESLKQEhgavlqlqqeaerlKKQQEDAENSREEAEKELEKWRQKANEalrLRLQAEDEAHKKTLAQEEAEKQKEE 1670
Cdd:TIGR01612 753 LNKILEDFKNK--------------EKELSNKINDYAKEKDELNKYKSKISE---IKNHYNDQINIDNIKDEDAKQNYDK 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1671 AEREAKKRAKAEESALK----QKEMAEEELERQRKIA--ESTAQQKLTAEQELI-----RLRADFdnAEQQRSLLEDEL- 1738
Cdd:TIGR01612 816 SKEYIKTISIKEDEIFKiineMKFMKDDFLNKVDKFInfENNCKEKIDSEHEQFaeltnKIKAEI--SDDKLNDYEKKFn 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1739 --YRLKNEVAAAQQQRKQLEDELAKVRSEMDIliqlkTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLraiseEAK 1816
Cdd:TIGR01612 894 dsKSLINEINKSIEEEYQNINTLKKVDEYIKI-----CENTKESIEKFHNKQNILKEILNKNIDTIKESNLI-----EKS 963
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1817 HQRQIaEEEAARQRAEAERILKEklAAISEATRLKTEAeiaLKEKEAENERLRRQAEDEAYQRKaleDQASQHKQEIEEK 1896
Cdd:TIGR01612 964 YKDKF-DNTLIDKINELDKAFKD--ASLNDYEAKNNEL---IKYFNDLKANLGKNKENMLYHQF---DEKEKATNDIEQK 1034
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1897 IVQLKKS-SEAEMERQKAIVDDTLKQRRVVEEEIRILKLN-FEKASSGKLDLELELNKLK--NIADETQQSKIRAEEEae 1972
Cdd:TIGR01612 1035 IEDANKNiPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEiLEEAEINITNFNEIKEKLKhyNFDDFGKEENIKYADE-- 1112
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1973 klrklaleeekrrreaeekVKKIAAAEEEAARQRKAALEELERLRKKAE----EARKQKDEADKEAEKQIvvaqqAAQKC 2048
Cdd:TIGR01612 1113 -------------------INKIKDDIKNLDQKIDHHIKALEEIKKKSEnyidEIKAQINDLEDVADKAI-----SNDDP 1168
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2049 SAAEQQVQSVLAQ-----QIEDSItQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAK 2123
Cdd:TIGR01612 1169 EEIEKKIENIVTKidkkkNIYDEI-KKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEA 1247
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2124 AQEDAERLRKEAEfeaaKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQ--ELTKVKLKLDETDKQKSVLDEE 2201
Cdd:TIGR01612 1248 YIEDLDEIKEKSP----EIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENisDIREKSLKIIEDFSEESDINDI 1323
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2202 LQRLKDEVDDAVKQRGQVEE------------ELFKVKVQMEELLKLKNKIEEENQRlIKKDKDSTQKLLAEEAEN---- 2265
Cdd:TIGR01612 1324 KKELQKNLLDAQKHNSDINLylneianiynilKLNKIKKIIDEVKEYTKEIEENNKN-IKDELDKSEKLIKKIKDDinle 1402
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2266 ------------------MRKLAEDAAR-LSVEAQEAARLRQIAEDDLNQQRALAE-KMLKEKMQAIQEASR-------- 2317
Cdd:TIGR01612 1403 eckskiestlddkdidecIKKIKELKNHiLSEESNIDTYFKNADENNENVLLLFKNiEMADNKSQHILKIKKdnatndhd 1482
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2318 -----LKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLE--------IMAEAERLRLQVSQ 2384
Cdd:TIGR01612 1483 fnineLKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAktkkdseiIIKEIKDAHKKFIL 1562
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2385 LSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSkeadDLRKAIADLENEKARLKKEAEELQn 2464
Cdd:TIGR01612 1563 EAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKIS----DIKKKINDCLKETESIEKKISSFS- 1637
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2465 kskemADAQQKKIEHEKTVLQ--QTFMtekEMLLKKEKLIEDEKKRLESqfeeevkkakaLKDEQERQKQQMEQEKKTLQ 2542
Cdd:TIGR01612 1638 -----IDSQDTELKENGDNLNslQEFL---ESLKDQKKNIEDKKKELDE-----------LDSEIEKIEIDVDQHKKNYE 1698
|
1290 1300 1310
....*....|....*....|....*....|..
gi 1988774682 2543 ATMDAALSKQKEAEEEMLRKQKEMQELERQRL 2574
Cdd:TIGR01612 1699 IGIIEKIKEIAIANKEEIESIKELIEPTIENL 1730
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1348-1646 |
5.31e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.45 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1348 DEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQEL 1427
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1428 KNLSEQ----QIKDKSQQVDEALHSRTKIEEEIRLIRIQLETT---------------EKQKY-----TAESELKQLRDR 1483
Cdd:PRK04778 185 VELTESgdyvEAREILDQLEEELAALEQIMEEIPELLKELQTElpdqlqelkagyrelVEEGYhldhlDIEKEIQDLKEQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1484 AAEAEK-LRKLAQDEAEKLRKQVSEETQkkrQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQ----AEEAERqVKQA- 1557
Cdd:PRK04778 265 IDENLAlLEELDLDEAEEKNEEIQERID---QLYDILEREVKARKYVEKNSDTLPDFLEHAKEQnkelKEEIDR-VKQSy 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1558 -----EIEK----EKQIKvAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEhgAVLQLQQE--AERLkKQQEDAENsr 1626
Cdd:PRK04778 341 tlnesELESvrqlEKQLE-SLEKQYDEITERIAEQEIAYSELQEELEEILKQL--EEIEKEQEklSEML-QGLRKDEL-- 414
|
330 340
....*....|....*....|
gi 1988774682 1627 eEAEKELEKWRQKANEALRL 1646
Cdd:PRK04778 415 -EAREKLERYRNKLHEIKRY 433
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1343-1658 |
5.32e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 48.88 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1343 QRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKqLAEAHAKaiAKAEKEAQELKLKMQEEvskreiaavdaekqktniql 1422
Cdd:pfam15558 78 ERRRADRREKQVIEKESRWREQAEDQENQRQEK-LERARQE--AEQRKQCQEQRLKEKEE-------------------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1423 ELQELKNLSEQQIKDKSQQvdeALHSRTKIEEEIRLIRIQLETTEKQKYTAeseLKQLRDRAAEAEKLRKLAQDEAEKLR 1502
Cdd:pfam15558 135 ELQALREQNSLQLQERLEE---ACHKRQLKEREEQKKVQENNLSELLNHQA---RKVLVDCQAKAEELLRRLSLEQSLQR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1503 KQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQikVAHEAAQKSAAAELQS 1582
Cdd:pfam15558 209 SQENYEQLVEERH-RELREKAQKEEEQFQRAKWRAEEKEEERQEHKEALAELADRKIQQARQ--VAHKTVQDKAQRAREL 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774682 1583 KHMSfaEKTSKLEEsLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKT 1658
Cdd:pfam15558 286 NLER--EKNHHILK-LKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEARKTARASFHMREKVREETNNRT 358
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1201-1933 |
5.53e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1201 QRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQavpitdskTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDT 1280
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQ--------TRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEE 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1281 IKDYELQLVAYKAQVEplvsplkkTKLDSASDniiqeyvtLRTRYSELMTLtsqyIKFITDTQRRLDDEEKAAEKLKAEE 1360
Cdd:PRK04863 447 FQAKEQEATEELLSLE--------QKLSVAQA--------AHSQFEQAYQL----VRKIAGEVSRSEAWDVARELLRRLR 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1361 RKKMaemqaeLDKQKQLAEAHAKAIAKAEKEAQELKlKMQEEVSKREIAAVDAEKqktniqlELQELKNLSEQQIKDKSQ 1440
Cdd:PRK04863 507 EQRH------LAEQLQQLRMRLSELEQRLRQQQRAE-RLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1441 QVDEALHSRTKIEEEIRLIRIQ---LETTEKQKYTAESELKQLRDRAAEA----EKLRKLAQDEAEKLRK---QVSEETQ 1510
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARiqrLAARAPAWLAAQDALARLREQSGEEfedsQDVTEYMQQLLEREREltvERDELAA 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1511 KKRQAEEELKRKSEAEK-------------------------------------------------EAAKQKQKALEDL- 1540
Cdd:PRK04863 653 RKQALDEEIERLSQPGGsedprlnalaerfggvllseiyddvsledapyfsalygparhaivvpdlSDAAEQLAGLEDCp 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1541 EKLRM-------------QAEEAERQV------KQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESlkqe 1601
Cdd:PRK04863 733 EDLYLiegdpdsfddsvfSVEELEKAVvvkiadRQWRYSRFPEVPLFGRAAREKRIEQLRAEREELAERYATLSFD---- 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1602 hgavlqlQQEAERLKKQQEDAENS------REEAEKELEKWRQKANEALRlRLQAEDEAHKKTLAQEEAEKQKEEAEREA 1675
Cdd:PRK04863 809 -------VQKLQRLHQAFSRFIGShlavafEADPEAELRQLNRRRVELER-ALADHESQEQQQRSQLEQAKEGLSALNRL 880
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1676 KKRAK--AEESALKQKEMAEEELERQRKIAESTAQQKLTA---EQELIRLRADFDNAEQqrslledelyrLKNEVAAAQQ 1750
Cdd:PRK04863 881 LPRLNllADETLADRVEEIREQLDEAEEAKRFVQQHGNALaqlEPIVSVLQSDPEQFEQ-----------LKQDYQQAQQ 949
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1751 QRKQLedelakvrsemdiliQLKTKAEKETMSNTEkskQLLEAEAAKMkdLAEEA---SRLRAISEEAKHQRQIAEEEAA 1827
Cdd:PRK04863 950 TQRDA---------------KQQAFALTEVVQRRA---HFSYEDAAEM--LAKNSdlnEKLRQRLEQAEQERTRAREQLR 1009
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1828 RQRAEAERILKEKLAAISEATRLKTEaeiaLKEKEAENERLRRQAEDEAyqrkalEDQASQHKQEIEEKIV--QLKKSS- 1904
Cdd:PRK04863 1010 QAQAQLAQYNQVLASLKSSYDAKRQM----LQELKQELQDLGVPADSGA------EERARARRDELHARLSanRSRRNQl 1079
|
810 820
....*....|....*....|....*....
gi 1988774682 1905 EAEMERQKAIVDDTLKQRRVVEEEIRILK 1933
Cdd:PRK04863 1080 EKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3464-3499 |
5.80e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 5.80e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1988774682 3464 LLEAQIVSGGIIDPVKSHRVPTDVAYQKNILSRDIA 3499
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1835-2601 |
6.12e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1835 RILKEKLAAISEATRLKTEAEIALKEKEAENERL---RRQAEDEAYQRKALEDQ-------------ASQHKQEIEEKIV 1898
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDyqaasdhlnlvqtALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1899 QLKKSSEAeMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKiRAEEEAEKLRKLA 1978
Cdd:PRK04863 356 DLEELEER-LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAV-QALERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1979 LEEEkrrreaeekvkkiaaaeeeaarqrKAALEELERLRKKAEEArkqkDEADKEAEKQIVVAQQAAQKCSAAEQQVQSv 2058
Cdd:PRK04863 434 DLTA------------------------DNAEDWLEEFQAKEQEA----TEELLSLEQKLSVAQAAHSQFEQAYQLVRK- 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2059 LAQQIEDSITQKKLKEeyekakklAKEAEAAKEKAEREAALLRQQAEEAERQktaaeeeaanqAKAQEDAERLRKEAEFE 2138
Cdd:PRK04863 485 IAGEVSRSEAWDVARE--------LLRRLREQRHLAEQLQQLRMRLSELEQR-----------LRQQQRAERLLAEFCKR 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2139 AAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSV---LDEELQRLKDEVDDAVKQ 2215
Cdd:PRK04863 546 LGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFED 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2216 RGQVEEelfkvkvQMEELLKLKNKIEEENQRLikkdkdstqkllaeeAENMRKLAEDAARLS-VEAQEAARLRQIAE--- 2291
Cdd:PRK04863 626 SQDVTE-------YMQQLLERERELTVERDEL---------------AARKQALDEEIERLSqPGGSEDPRLNALAErfg 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2292 --------DDLNQQRA-LAEKMLKEKMQAIQeASRLKAEAEMLQKQKDlaqeqaqkLLEDKQLMQ---QRLEE---ETEE 2356
Cdd:PRK04863 684 gvllseiyDDVSLEDApYFSALYGPARHAIV-VPDLSDAAEQLAGLED--------CPEDLYLIEgdpDSFDDsvfSVEE 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2357 YHKSLEVErkrqleimaEAERlRLQVSQLSEA----QARAEEEAKKFKKQADKVATRLHETEIATQEkmtvVERL--EFE 2430
Cdd:PRK04863 755 LEKAVVVK---------IADR-QWRYSRFPEVplfgRAAREKRIEQLRAEREELAERYATLSFDVQK----LQRLhqAFS 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2431 R-----LNTSKEAD------DLRKAIADLENEKARLKKEAEELQN---KSKEMADAQQKKIEHEKTVLQQTFMTEKEMLl 2496
Cdd:PRK04863 821 RfigshLAVAFEADpeaelrQLNRRRVELERALADHESQEQQQRSqleQAKEGLSALNRLLPRLNLLADETLADRVEEI- 899
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2497 kKEKLIEDEK-----KRLESQFEEEVKKAKALKDEQE------RQKQQMEQEKKTLQATMDA---------ALSKQKEAe 2556
Cdd:PRK04863 900 -REQLDEAEEakrfvQQHGNALAQLEPIVSVLQSDPEqfeqlkQDYQQAQQTQRDAKQQAFAltevvqrraHFSYEDAA- 977
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1988774682 2557 eEMLRKQKEMQELERQRLEQ-ERILAEENQKLREKLQQLedAQKDQ 2601
Cdd:PRK04863 978 -EMLAKNSDLNEKLRQRLEQaEQERTRAREQLRQAQAQL--AQYNQ 1020
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1350-1597 |
6.22e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.10 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1350 EKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIqlelqelkn 1429
Cdd:pfam02029 137 EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV--------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1430 lseqqikdKSQQVDEALHSRTKIEEEIRLIRIQLETTE---KQKYTAESELKQLRDRAAEAEklrklaQDEAEKLRkqvs 1506
Cdd:pfam02029 208 --------KSQNGEEEVTKLKVTTKRRQGGLSQSQEREeeaEVFLEAEQKLEELRRRRQEKE------SEEFEKLR---- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1507 eetQKKRQAE---EELKRKSEaekeaakQKQKALEDlEKLRMQAEEAERQVKqaEIEKEKQIKvaheaaqksaaAELQSK 1583
Cdd:pfam02029 270 ---QKQQEAElelEELKKKRE-------ERRKLLEE-EEQRRKQEEAERKLR--EEEEKRRMK-----------EEIERR 325
|
250
....*....|....
gi 1988774682 1584 HMSFAEKTSKLEES 1597
Cdd:pfam02029 326 RAEAAEKRQKLPED 339
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3388-3421 |
6.59e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 6.59e-05
10 20 30
....*....|....*....|....*....|....
gi 1988774682 3388 LLEAQAASGFIVDPVRNQCLSVDEAVKSGVVGPE 3421
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1454-1601 |
6.78e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.85 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1454 EEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE--AAK 1531
Cdd:pfam05262 199 DMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKqvAEN 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1532 QKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSaAAELQSKHMSFAEKTSKLEESLKQE 1601
Cdd:pfam05262 279 QKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDK-ELEAQKKREPVAEDLQKTKPQVEAQ 347
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1673-1896 |
6.87e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.45 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1673 REAKKRAKAEESALKQKEMAEE-----ELERQRKIAE-STAQQKLTAEQELirlrADFDNAEQQRSLLEDELYRLKNEVA 1746
Cdd:NF012221 1548 SKHAKQDDAAQNALADKERAEAdrqrlEQEKQQQLAAiSGSQSQLESTDQN----ALETNGQAQRDAILEESRAVTKELT 1623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1747 AAQQQRKQLEDE-------------------LAKVRSEMDiliqlktKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASR 1807
Cdd:NF012221 1624 TLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLD-------DAKKISGKQLADAKQRHVDNQQKVKDAVAKSEA 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1808 LRAISEeakHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAledQAS 1887
Cdd:NF012221 1697 GVAQGE---QNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQA---DAK 1770
|
....*....
gi 1988774682 1888 QHKQEIEEK 1896
Cdd:NF012221 1771 GAKQDESDK 1779
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1791-1921 |
7.11e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 45.93 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1791 LEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAarqRAEAERILKEklaAISEATRLKTEaeiALKEKEAENERLRR 1870
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEA---RAEAAEIIAE---ARKEAEAIAEE---AKAEAEAEAERIIA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774682 1871 QAEDEAYQ-----RKALEDQASQHKQEIEEKIVQlkksSEAEMERQKAIVDDTLKQ 1921
Cdd:COG0711 100 QAEAEIEQerakaLAELRAEVADLAVAIAEKILG----KELDAAAQAALVDRFIAE 151
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
1365-1763 |
7.33e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 49.20 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1365 AEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDE 1444
Cdd:COG4995 76 LLLALALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1445 ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSE 1524
Cdd:COG4995 156 AAAAAAAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1525 AEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsfAEKTSKLEESLKQEHGA 1604
Cdd:COG4995 236 LLLALLALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALAL-----AAAALALALLLAAAAAA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1605 VLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 1684
Cdd:COG4995 311 ALAALALLLLAALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALL 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1685 ALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQ-QRSLLEDELYRLkneVAAAQQQRKQLEDELAKVR 1763
Cdd:COG4995 391 AALLLLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALiEYIILPDRLYAF---VQLYQLLIAPIEAELPGIK 467
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1604-1930 |
7.41e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.38 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1604 AVLQLQQEAERLKKQQEDAENSREEAEKELEkwRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEE 1683
Cdd:pfam13868 22 KERDAQIAEKKRIKAEEKEEERRLDEMMEEE--RERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1684 SALKQKEMAEEELERQRKIAESTAQQKLTAE--QELIRLRADFDNAEQQRSLLEDElyRLKNEVAAAQQQRKQLEDELAK 1761
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKELEKEEEREEDE--RILEYLKEKAEREEEREAEREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1762 VRSEMDILIQLKTKAEKETMsnteksKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKL 1841
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQ------DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1842 AAIsEATRLKTEAEIALKEKEAENERLRRQAEDeayQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQ 1921
Cdd:pfam13868 252 LAE-EAEREEEEFERMLRKQAEDEEIEQEEAEK---RRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAER 327
|
....*....
gi 1988774682 1922 RRVVEEEIR 1930
Cdd:pfam13868 328 RERIEEERQ 336
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
47-112 |
7.65e-05 |
|
first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409070 Cd Length: 106 Bit Score: 44.57 E-value: 7.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 47 KKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREK----GRMRFHKLQNVQIALDFL 112
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1742-1920 |
7.66e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 49.25 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1742 KNEVAAAQQQRKQLEDElAKVRSEmdiLIQLKTKAEKEtmsntEKSKQLLEAEAakmKDLAEEAS-RLRAISEeakhqrq 1820
Cdd:PTZ00491 662 KSQEAAARHQAELLEQE-ARGRLE---RQKMHDKAKAE-----EQRTKLLELQA---ESAAVESSgQSRAEAL------- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1821 iAEEEAARQRAEAErilkeklaaiSEATRLKTEAEIALKEKEAENERLRRQAEdeayqrkaLEDQASQHKQEIEEKivql 1900
Cdd:PTZ00491 723 -AEAEARLIEAEAE----------VEQAELRAKALRIEAEAELEKLRKRQELE--------LEYEQAQNELEIAKA---- 779
|
170 180
....*....|....*....|....
gi 1988774682 1901 KKSSEAEMERQKAIVD----DTLK 1920
Cdd:PTZ00491 780 KELADIEATKFERIVEalgrETLI 803
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1467-1635 |
7.77e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1467 EKQKYTAESELKQLRDRA-AEAEKLRKL----AQDEAEKLRKQVSEETQKKR-----------QAEEELKRKSeaekEAA 1530
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAkKEAEAIKKEalleAKEEIHKLRNEFEKELRERRnelqklekrllQKEENLDRKL----ELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1531 KQKQKALEDLEKlRMQAEEAERQVKQAEIEK--EKQIKVAHEAAQksaaaelqskhMSFAEKTSKLEESLKQEhgavlqL 1608
Cdd:PRK12704 106 EKREEELEKKEK-ELEQKQQELEKKEEELEEliEEQLQELERISG-----------LTAEEAKEILLEKVEEE------A 167
|
170 180
....*....|....*....|....*..
gi 1988774682 1609 QQEAERLKKQQEdaENSREEAEKELEK 1635
Cdd:PRK12704 168 RHEAAVLIKEIE--EEAKEEADKKAKE 192
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1408-1629 |
7.77e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1408 IAAVDAEKQKTNIQLELQELKNLSEQ---QIKDKSQQVDEAlhsrtkiEEEIRLIRIQLETTEKQKYTAESELKQLRDRA 1484
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAaqaELDALQAELEEL-------NEEYNELQAELEALQAEIDKLQAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1485 AEA-EKLRKLAQDEAEK------------------------LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQkalED 1539
Cdd:COG3883 82 EERrEELGERARALYRSggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKL---AE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1540 LEKLRMQAEEAERQVKQAEIEKEKQIkvaheaaqksaaAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQ 1619
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALL------------AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
250
....*....|
gi 1988774682 1620 EDAENSREEA 1629
Cdd:COG3883 227 AAAAAAAAAA 236
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
150-263 |
7.93e-05 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 45.18 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 150 DIQVNGQSEDMTAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVA 228
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQ---NKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKpVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774682 229 EKDLGVTRLLDPEDVDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1473-1632 |
8.01e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 46.98 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1473 AESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQA----EEELKRKSEAEKEAAKQKQKALE-DLEKLRMQA 1547
Cdd:pfam04012 34 MQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAAltkgNEELAREALAEKKSLEKQAEALEtQLAQQRSAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1548 EEAERQV-----KQAEIEKEKQIKVAHEAAQKSAAAELQSKH-MSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQED 1621
Cdd:pfam04012 114 EQLRKQLaaletKIQQLKAKKNLLKARLKAAKAQEAVQTSLGsLSTSSATDSFERIEEKIEEREARADAAAELASAVDLD 193
|
170
....*....|.
gi 1988774682 1622 AENSREEAEKE 1632
Cdd:pfam04012 194 AKLEQAGIQME 204
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1547-2021 |
9.16e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1547 AEEAERQVKQA-EIEKEKQIKVAHEAAQKSAAAELQSKhmsfAEKTSKLEESLKQEHGAV---LQLQQEAERLKKQQEDA 1622
Cdd:PRK04863 278 ANERRVHLEEAlELRRELYTSRRQLAAEQYRLVEMARE----LAELNEAESDLEQDYQAAsdhLNLVQTALRQQEKIERY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1623 ENSREEAEKELEkwrqkanEALRLRLQAEDEAhkktlaqeeaekqkeeAEREAKKRAkAEESALK-QKEMA--EEELERQ 1699
Cdd:PRK04863 354 QADLEELEERLE-------EQNEVVEEADEQQ----------------EENEARAEA-AEEEVDElKSQLAdyQQALDVQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1700 --RKIAESTAQQKLTAEQELIRLRA-DFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKA 1776
Cdd:PRK04863 410 qtRAIQYQQAVQALERAKQLCGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEV 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1777 EKETMSNTEKSkqlLEAEAAKMKDLAEEASRLRAISEEAKhQRQIAEEEAARQRAEAERILKEKLAAISEATRLkteaei 1856
Cdd:PRK04863 490 SRSEAWDVARE---LLRRLREQRHLAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL------ 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1857 aLKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEE--KIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKL 1934
Cdd:PRK04863 560 -QEELEARLESLSESVSEARERRMALRQQLEQLQARIQRlaARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLE 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1935 NfEKassgkldlELELNKlkniaDETQQSKIRAEEEAEKLRklaleeekrrreaeekvkkiaaaeeeaarQRKAAleELE 2014
Cdd:PRK04863 639 R-ER--------ELTVER-----DELAARKQALDEEIERLS-----------------------------QPGGS--EDP 673
|
....*..
gi 1988774682 2015 RLRKKAE 2021
Cdd:PRK04863 674 RLNALAE 680
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1479-1735 |
9.53e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1479 QLRDRAAEAEKLRKLAQDEAEKLRKQVSEetqkKRQAEEELKRKS-----EAEKEAAKQKQKALED-LEKLRMQAEEAER 1552
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQKNglvdlSEEAKLLLQQLSELESqLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1553 QVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKkqqedaensreeaeke 1632
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR---------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1633 lekwRQKANEALRLRLQAEDEAhkktlaqeeaekqkeeaereakKRAKAEESALKQkemaeeELERQRKIAESTAQQklt 1712
Cdd:COG3206 305 ----AQLQQEAQRILASLEAEL----------------------EALQAREASLQA------QLAQLEARLAELPEL--- 349
|
250 260
....*....|....*....|....
gi 1988774682 1713 aEQELIRLRADFDNAEQQ-RSLLE 1735
Cdd:COG3206 350 -EAELRRLEREVEVARELyESLLQ 372
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
46-153 |
1.08e-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: 45.39 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 46 QKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 112
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1988774682 113 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 153
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1739-2054 |
1.09e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1739 YRL-KNEVAAAQQQRKQleDELAKVRSEMDILIQLKTKAEKEtmsntEKSKQLLEAEAAKMKD-LAEEASRLRAISEEAK 1816
Cdd:PRK05035 431 YRQaKAEIRAIEQEKKK--AEEAKARFEARQARLEREKAARE-----ARHKKAAEARAAKDKDaVAAALARVKAKKAAAT 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1817 HQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAedeayqRKALEDQASQhkqEIEEK 1896
Cdd:PRK05035 504 QPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKA------KKAAQQAANA---EAEEE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1897 IVQLKKSSEAEMERQKAivddtlkqrrvveeeiRILKLNFEKASSGKLDLELELNKlkniadetqqSKIRAEEEAEKLRK 1976
Cdd:PRK05035 575 VDPKKAAVAAAIARAKA----------------KKAAQQAASAEPEEQVAEVDPKK----------AAVAAAIARAKAKK 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1977 LALEEEKRRREAEEKvkkiaaaeeeaarqRKAALE-ELERLR-KKAEEARKQKDEADKEAE-KQIVVAQQAAQKCSAAEQ 2053
Cdd:PRK05035 629 AEQQANAEPEEPVDP--------------RKAAVAaAIARAKaRKAAQQQANAEPEEAEDPkKAAVAAAIARAKAKKAAQ 694
|
.
gi 1988774682 2054 Q 2054
Cdd:PRK05035 695 Q 695
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1412-1825 |
1.11e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.92 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1412 DAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESEL--KQLRDRAAEAEK 1489
Cdd:COG5022 814 SYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELaeRQLQELKIDVKS 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1490 LRKLA----QDEAE--KLRKQVSEETQKKRQA-------EEELKRKSEAEKEAAKQKQKaLEDLEKLRMQ-------AEE 1549
Cdd:COG5022 894 ISSLKlvnlELESEiiELKKSLSSDLIENLEFkteliarLKKLLNNIDLEEGPSIEYVK-LPELNKLHEVesklketSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1550 AERQVKQAEIEKEKQIKVAHEAAQ-KSAAAELQSKHMSFAEKTSkleeSLKQEHGAVLQLQQEAERLKkqQEDAENSREE 1628
Cdd:COG5022 973 YEDLLKKSTILVREGNKANSELKNfKKELAELSKQYGALQESTK----QLKELPVEVAELQSASKIIS--SESTELSILK 1046
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1629 AEKELEKWRQKANEALRLRLQAEDEAhKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQ 1708
Cdd:COG5022 1047 PLQKLKGLLLLENNQLQARYKALKLR-RENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKL 1125
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1709 QKLTAEQELIRLRADF-DNAEQQRSLLEDELYRLKNEvaaaqqqrKQLEDELAKVRsemdiLIQLKTKAEKETMSNTEKS 1787
Cdd:COG5022 1126 NLLQEISKFLSQLVNTlEPVFQKLSVLQLELDGLFWE--------ANLEALPSPPP-----FAALSEKRLYQSALYDEKS 1192
|
410 420 430
....*....|....*....|....*....|....*...
gi 1988774682 1788 KQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEE 1825
Cdd:COG5022 1193 KLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEG 1230
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1610-1831 |
1.11e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.92 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1610 QEAERLKKQQEDAENSREEAEKELEkwrQKAnEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQK 1689
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLE---QQA-EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1690 EMAEEELERQRK-IAESTAQQKLTAEQELIRLRADFDNAEQQRsllEDELYRLKNEVAAAQQQRKQLEDELAKVRSEmdi 1768
Cdd:TIGR02794 126 AKQAAEAKAKAEaEAERKAKEEAAKQAEEEAKAKAAAEAKKKA---EEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE--- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 1769 liQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRA 1831
Cdd:TIGR02794 200 --AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1349-1616 |
1.14e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 48.05 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1349 EEKAAEKLKAEErkKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNiqlELQELK 1428
Cdd:PRK07735 38 EEENREKEKALP--KNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAA---ALAKQK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1429 NLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEklrklAQDEAEKLRKqvsee 1508
Cdd:PRK07735 113 REGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAA-----AKAKAAALAK----- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1509 tQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSfa 1588
Cdd:PRK07735 183 -QKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTKGAE-- 259
|
250 260 270
....*....|....*....|....*....|
gi 1988774682 1589 ektSKLEESLKQEHGAVLQ--LQQEAERLK 1616
Cdd:PRK07735 260 ---GKKEEEPKQEEPSVNQpyLNKYVEVIK 286
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
46-143 |
1.15e-04 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 45.35 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 46 QKKTFTKWVN---------KHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 112
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1988774682 113 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 143
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1790-2036 |
1.16e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1790 LLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEeAARQRAEAERILKEKLAAISEATRL--KTEAEIALKEKEAE--N 1865
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAelE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1866 ERLRRQAEDEAYQRKALEDQ--ASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvveEEIRILKLNFEKASSGK 1943
Cdd:COG4942 90 KEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1944 LDLELELNKLKNIADETQQSKIRAEEEAEKLRKLAleeekrrREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEA 2023
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLL-------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|...
gi 1988774682 2024 RKQKDEADKEAEK 2036
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1520-1931 |
1.18e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.11 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1520 KRKSEAEKEAAKQKQKALEDLEKLRMQAEE----AERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLE 1595
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEaeqkAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1596 ESLKQEHGAVLQLQQEAERLKKQQEDAENSREEA----EKELEKWRQKANEALRLRLQAE-DEAHKKTLAQEEAEKQKEE 1670
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAaaaeKEKAEEAKRKAEEEAKRKAEEErKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1671 AEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1750
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1751 QRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQR 1830
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1831 AEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMER 1910
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGL 400
|
410 420
....*....|....*....|.
gi 1988774682 1911 QKAIVDDTLKQRRVVEEEIRI 1931
Cdd:COG3064 401 LGLRLDLGAALLEAASAVELR 421
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1501-1789 |
1.21e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 48.36 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1501 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAE-EAERQVKQAEIEKEKqIKVAHEAAQKSAAAE 1579
Cdd:pfam15964 319 VRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELErQKERLEKELASQQEK-RAQEKEALRKEMKKE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1580 ---LQSKHMSFAEKTSKLEESL----KQEHGAVLQLQQEAERLKKQQED--------------AENSREEAEKELEKWRQ 1638
Cdd:pfam15964 398 reeLGATMLALSQNVAQLEAQVekvtREKNSLVSQLEEAQKQLASQEMDvtkvcgemryqlnqTKMKKDEAEKEHREYRT 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1639 KANEALRLrlqAEDEAHKKTLAQEEAEKQKEEAEREAkkrAKAEESALKQKEMAEE--------ELER---QRKIAESTA 1707
Cdd:pfam15964 478 KTGRQLEI---KDQEIEKLGLELSESKQRLEQAQQDA---ARAREECLKLTELLGEsehqlhltRLEKesiQQSFSNEAK 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1708 QQKLTAEQELIRLRADFDNAEQQRSLLEDELYRL---KNEVAAAQQQR-----KQLEDELAKVRSEMDILIQ----LKTK 1775
Cdd:pfam15964 552 AQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLltsQNTFIAKLKEEcctlaKKLEEITQKSRSEVEQLSQekeyLQDR 631
|
330
....*....|....
gi 1988774682 1776 AEKETMSNTEKSKQ 1789
Cdd:pfam15964 632 LEKLQKRNEELEEQ 645
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
2176-2599 |
1.25e-04 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 48.32 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2176 QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDST 2255
Cdd:pfam09730 38 ELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2256 QKLLAEEA--ENMRKLAEDAARLSVEAQEAARLRQIaeddlnqqralAEKMLKEKMQAIQEASRLKAeaemlqkqkDLAQ 2333
Cdd:pfam09730 118 QNQVEFEGlkHEITRKEEETELLNSQLEEAIRLREI-----------AERQLDEALETLKTEREQKN---------SLRK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2334 EQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLhet 2413
Cdd:pfam09730 178 ELSHYMTLNDFDYVSHLSISLDGLKFSEDEGAGTEPNNDGEAMDGGENGGGGLKNSGLDNRTSTPRKSEVFPPAPSL--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2414 eiatqekmtvVERLeFERLNTSkEADDLRKAIADLENEKARLKKEAEELQnksKEMADAQQKKIEHEKTVLQqtfMTEKE 2493
Cdd:pfam09730 255 ----------VSDL-LSELNIS-EIQKLKQQLIQVEREKVSLLSTLQESQ---KQLEQAKGALSEQQEKVNR---LTENL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2494 MLLKKeklIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEqekkTLQATMDAALSKQKEAEEEMLRKQKEMQELERQR 2573
Cdd:pfam09730 317 EAMRG---LQASKERQDALDSEKDRDSHEDGDYYEVDINGPE----ILECKYRVAVEEAGELREELKALKARYNTLEERY 389
|
410 420
....*....|....*....|....*.
gi 1988774682 2574 LEQERILAEENQKLREKLQQLEDAQK 2599
Cdd:pfam09730 390 KEEKTRWEAEAQDLAEKIRQLEKASH 415
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2155-2356 |
1.26e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2155 QADTEMAKHKKLAEQTL---KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQR------GQVEEELFK 2225
Cdd:PRK11281 53 LLEAEDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2226 VKVQMEEllkLKNKIEEENQRLIkkdkdsTQKLLAEEA-----ENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRAL 2300
Cdd:PRK11281 133 TLDQLQN---AQNDLAEYNSQLV------SLQTQPERAqaalyANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQAL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 2301 AEKMLKEKMQAIQEASRLKaeaEMLQKQKDLAQEQAQKLLEDKQLMQ-----QRLeEETEE 2356
Cdd:PRK11281 204 LNAQNDLQRKSLEGNTQLQ---DLLQKQRDYLTARIQRLEHQLQLLQeainsKRL-TLSEK 260
|
|
| SH3_and_anchor |
TIGR04211 |
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
2176-2265 |
1.26e-04 |
|
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.
Pssm-ID: 275056 [Multi-domain] Cd Length: 198 Bit Score: 46.15 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2176 QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLknkiEEENQRLIKKDKDST 2255
Cdd:TIGR04211 70 ELQQELAELQEELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIKQISANAIEL----DEENRELREELAELK 145
|
90
....*....|
gi 1988774682 2256 QKLLAEEAEN 2265
Cdd:TIGR04211 146 QENEALEAEN 155
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2291-2565 |
1.28e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2291 EDDLNQQRALAEKMLKE----KMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEEteeyhksleveRK 2366
Cdd:COG1340 10 LEELEEKIEELREEIEElkekRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL-----------KE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2367 RQLEIMAEAERLRLQVSQLSEAQARAEEEA---KKFKKQADKVATRLHETEIATQEKMTVVERLE--FERLNTSKEADDL 2441
Cdd:COG1340 79 ERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKelEKELEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2442 RKAIADLENEKARLKKEAEELQNKSKEMADAQQKKieHEKtvlqqtfMTEkemLLKKEKLIEDEKKRLESQFEEEVKKAK 2521
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQEL--HEE-------MIE---LYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1988774682 2522 ALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKE 2565
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1694-2216 |
1.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1694 EELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQ--QQRKQLEDELAKVRSEmdiliq 1771
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPER------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1772 lktkaeketmsntekskqlLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLK 1851
Cdd:COG4717 148 -------------------LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1852 TEAEIALKEKEAENERLRRQAEDEayqrkaledQASQHKQEIEEKIVQLKKSSEAEmerqKAIVDDTLKQRRVVEEEIRI 1931
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQL---------ENELEAAALEERLKEARLLLLIA----AALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1932 LKLNFekASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALeeekrrreaeekvKKIAAAEEEAARQRKAALE 2011
Cdd:COG4717 276 AGVLF--LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEL-------------EELLAALGLPPDLSPEELL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2012 ELERLRKKAEEARKQKDEADKEAEKQivvaqqaaqkcsAAEQQVQSVLAQQIEDSItqkklkEEYEKAKKLAKEAEAAKE 2091
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLE------------ELEQEIAALLAEAGVEDE------EELRAALEQAEEYQELKE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2092 KAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAakraqaeaaalMQKQQADTEMAKHKKLAEQTL 2171
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE-----------LREELAELEAELEQLEEDGEL 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 2172 KQKfqvEQELTKVKLKLDETDKQ-------KSVLDEELQRLKDEVDDAVKQR 2216
Cdd:COG4717 472 AEL---LQELEELKAELRELAEEwaalklaLELLEEAREEYREERLPPVLER 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1274-1506 |
1.29e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1274 AKAYIDTIKDYELQLVAYKAQVEPLVSPLKKTKldSASDNIIQEYVTLRTRYSELMTL---TSQYIKFITDTQRRLDDEE 1350
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALK--KEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1351 KAAEKLKAEERKKMAEMQAELdkQKQLAEAHAKAIAKAEKEAQELK-LKMQEEVSKREIAAVDAEKQKTNiqlELQELKN 1429
Cdd:COG4942 93 AELRAELEAQKEELAELLRAL--YRLGRQPPLALLLSPEDFLDAVRrLQYLKYLAPARREQAEELRADLA---ELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774682 1430 LSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKL-RKLAQDEAEKLRKQVS 1506
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiARLEAEAAAAAERTPA 245
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1510-1642 |
1.31e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 44.55 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1510 QKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEaerqvkqaeiekekqikvaheaAQKSAAAELQsKHMSFAE 1589
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIARE----------------------AQQNYERELV-LHAEDIK 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 1590 KTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANE 1642
Cdd:pfam07926 58 ALQALREELNELKAEIAELKAEAESAKAELEESEESWEEQKKELEKELSELEK 110
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
925-1524 |
1.31e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 925 RLIMRNLELHYQDFMRDSQDSQLFGPDDRMQVEDDYTKSTQHFDNLLRSmeKGQQNETLCKNYISELKDLRLRIEDCEAG 1004
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ--KLEERSQKESKARSGLKVLLALIKDGVGG 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1005 TVARIRKPVEKEPLKEYIQKTTEQKKVQGELDGLKKDLDKVSVKTQEVLASPQPSASAPVLRSELDLTVQKMDHAHMLSS 1084
Cdd:pfam02463 523 RIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPI 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1085 VYLEKLKTVEMVIRNTQGAEGVLKQYEDCLREVHTVPSDVKEVETYRAK-------LKKMRTEAEDEQPVFDSLEEELKK 1157
Cdd:pfam02463 603 LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGvsleeglAEKSEVKASLSELTKELLEIQELQ 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1158 ASAVSDKMVRVHSERDVELDhFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLGYYREsydwLIRWIADAKQRQEKIQA 1237
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIK-KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL----LKQKIDEEEEEEEKSRL 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1238 VPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKayidtIKDYELQLVAYKAQVEPLVSPLKKTKLDSASDNIIQE 1317
Cdd:pfam02463 758 KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEK-----LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1318 YVTLRTRYSELMTLTSQYiKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQlaeahakaiaKAEKEAQELKL 1397
Cdd:pfam02463 833 EELEELALELKEEQKLEK-LAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES----------KEEKEKEEKKE 901
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1398 KMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKqkytaesEL 1477
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL-------GK 974
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1988774682 1478 KQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSE 1524
Cdd:pfam02463 975 VNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
52-142 |
1.40e-04 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 44.21 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 52 KWVNKHLIKAQR---HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM---RFHKLQNVQIALDFLRhrQVKLVN-IRN 124
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 1988774682 125 DDIADGNPKLTLGLIWTI 142
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1511-1844 |
1.56e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.22 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1511 KKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQaeiEKEKQIKVAHEAAQKSAAAELQSKHMsfaek 1590
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQ---ELEEQIEEREQKRQEEYEEKLQEREQ----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1591 tskLEESLKQEHgavLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlaqeeaekqkeE 1670
Cdd:pfam13868 103 ---MDEIVERIQ---EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKE------------K 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1671 AEREAKKRAKAEEsalkQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 1750
Cdd:pfam13868 165 AEREEEREAEREE----IEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1751 QRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQR 1830
Cdd:pfam13868 241 REEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
|
330
....*....|....
gi 1988774682 1831 AEAERILKEKLAAI 1844
Cdd:pfam13868 321 REEEAERRERIEEE 334
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1605-1929 |
1.56e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 47.34 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1605 VLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRL-------QAEDEAHKKTLAQEEAEKQKEEAEREAKK 1677
Cdd:pfam15558 13 MLARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLqqsqeqwQAEKEQRKARLGREERRRADRREKQVIEK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1678 RAKAEESALKQKEMAEEELERQRKIAESTAQ---QKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVaaAQQQRKQ 1754
Cdd:pfam15558 93 ESRWREQAEDQENQRQEKLERARQEAEQRKQcqeQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKER--EEQKKVQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1755 LEDELAKVRSE-MDILIQLKTKAEKETMSNT---------EKSKQLLEAEAAKMKDLA----EEASRLRAISEEAKHQRQ 1820
Cdd:pfam15558 171 ENNLSELLNHQaRKVLVDCQAKAEELLRRLSleqslqrsqENYEQLVEERHRELREKAqkeeEQFQRAKWRAEEKEEERQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1821 ------IAEEEAARQRAE--AERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKaledqasqhkqe 1892
Cdd:pfam15558 251 ehkealAELADRKIQQARqvAHKTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKK------------ 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 1988774682 1893 iEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEI 1929
Cdd:pfam15558 319 -EQRSEQISREKEATLEEARKTARASFHMREKVREET 354
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1502-1641 |
1.66e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 46.24 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1502 RKQvsEETQKKRQAEEELKRKSEAEKEAAKQ--KQKALEDLEKlrmqaeeaerqvKQAEIEKEKQIKVAHEAAQKSAAAE 1579
Cdd:pfam13904 63 AKQ--RQRQKELQAQKEEREKEEQEAELRKRlaKEKYQEWLQR------------KARQQTKKREESHKQKAAESASKSL 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774682 1580 LQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSR--EEAEKELEKWRQKAN 1641
Cdd:pfam13904 129 AKPERKVSQEEAKEVLQEWERKKLEQQQRKREEEQREQLKKEEEEQErkQLAEKAWQKWMKNVK 192
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2178-2615 |
1.66e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2178 EQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIeeeNQRLIKKDKDStqK 2257
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKF---LTEIKKKEKEL--E 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2258 LLAEEAENMRKLAEDaarlsVEAQEAARLRQIAE-----DDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKdla 2332
Cdd:TIGR04523 156 KLNNKYNDLKKQKEE-----LENELNLLEKEKLNiqkniDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQN--- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2333 qeqaQKLLEDKQLMQQRLEEETEEYHKSLEverkrqleimaeaerlrlQVSQLseaqaraeeeakkfKKQADKVATRLhe 2412
Cdd:TIGR04523 228 ----NQLKDNIEKKQQEINEKTTEISNTQT------------------QLNQL--------------KDEQNKIKKQL-- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2413 teiatQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKAR--LKKEAEELQNKSKEMADAQQKKIEHEKTVLQqtfMT 2490
Cdd:TIGR04523 270 -----SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQ---LN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2491 EKEMLLKKEKL-IEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQekktlqatmdaaLSKQKEAEEEMLRKQKEMQEL 2569
Cdd:TIGR04523 342 EQISQLKKELTnSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN------------LESQINDLESKIQNQEKLNQQ 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1988774682 2570 ERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDII 2615
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1376-1575 |
1.72e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 47.71 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1376 QLAEAHAKAIAKAEKEAQELKLKMQEEVSkreiaavdaekqktniqlELQELKNLSEQQIKDKSQQVDEALHSRTKIEEE 1455
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREEELE------------------ELQEQLEDLESSIQELEKEIKKLESSIKQVEEE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1456 IRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLrKQVSEETQKKRQAE-EELKRKSEAEKEAAKQKQ 1534
Cdd:pfam05667 372 LEELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLiEEYRALKEAKSNKEDESQ 450
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1988774682 1535 KALEDLEKLRMQAEEAERQVKQAEiEKEKQIKVAHEAAQKS 1575
Cdd:pfam05667 451 RKLEEIKELREKIKEVAEEAKQKE-ELYKQLVAEYERLPKD 490
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1499-1692 |
1.81e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.69 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1499 EKLRKQVSEETQKKRQAEEELKRKSEaekEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAA 1578
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERESQ---EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1579 ELQSKHMSFAEKtSKLEESLKQEhgavlqlqqeaerLKKQQEDAENSREEAEKELEkwrQKANEALRLRLQAEDEAHKKT 1658
Cdd:pfam05262 261 PKPADTSSPKED-KQVAENQKRE-------------IEKAQIEIKKNDEEALKAKD---HKAFDLKQESKASEKEAEDKE 323
|
170 180 190
....*....|....*....|....*....|....
gi 1988774682 1659 LAQEEAEKQKEEAEREAKKRAKAEESALKQKEMA 1692
Cdd:pfam05262 324 LEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAID 357
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2172-2353 |
1.87e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 46.80 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2172 KQKFQ--VEQELTKVKLKLDETDKQKSV--LDEELQRLKDEVDDAVKQ---------------RGQVEEELFKVK---VQ 2229
Cdd:cd16269 88 DQKFQkkLMEQLEEKKEEFCKQNEEASSkrCQALLQELSAPLEEKISQgsysvpggyqlyledREKLVEKYRQVPrkgVK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2230 MEELLK--LKNKIEEENQRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAaRLRQIAEDdlnQQRALAE--KML 2305
Cdd:cd16269 168 AEEVLQefLQSKEAEAEAIL-QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQR-ELEQKLED---QERSYEEhlRQL 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1988774682 2306 KEKMQaiQEASRLKAEAEMLQKQKDlaQEQAQKLLEDKQLMQQRLEEE 2353
Cdd:cd16269 243 KEKME--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEE 286
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1801-1974 |
1.93e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1801 LAEEASRLRAiSEEAKHQRQIAEEEAARQRAEAERI---LKEKLAAISEATRLKTEAEIALKEKEAENERLRrqaEDEAY 1877
Cdd:pfam07888 40 LQERAELLQA-QEAANRQREKEKERYKRDREQWERQrreLESRVAELKEELRQSREKHEELEEKYKELSASS---EELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1878 QRKALEDQASQHKQEIEE------KIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELN 1951
Cdd:pfam07888 116 EKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170 180
....*....|....*....|...
gi 1988774682 1952 KLKNIADETQQSKIRAEEEAEKL 1974
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDTITTL 218
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2804-2840 |
1.94e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 1.94e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1988774682 2804 IRVLEAQLATGGIIDPINSHRVPTETAYKQGHYDAEM 2840
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1787-1930 |
2.02e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1787 SKQLLEAEAAKMKDLAEEASRLRAISEEAKHQrqiAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENE 1866
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLE---AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774682 1867 RLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKsseaEMERQKAIVDDTLKQR--RVVEEEIR 1930
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEAR 168
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2409-2573 |
2.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2409 RLHETEIATQEKMTVVERLE--FERLNTSKEADDLRKAIADLENEKARLKKEAEELQnksKEMADAQQKKIEHEKTVLQQ 2486
Cdd:COG4913 259 ELAERYAAARERLAELEYLRaaLRLWFAQRRLELLEAELEELRAELARLEAELERLE---ARLDALREELDELEAQIRGN 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2487 TFmTEKEMLLKKEKLIEDEKKRLE---SQFEEEVKKA-----------KALKDEQERQKQQMEQEKKTLQATMDAALSKQ 2552
Cdd:COG4913 336 GG-DRLEQLEREIERLERELEERErrrARLEALLAALglplpasaeefAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
170 180
....*....|....*....|.
gi 1988774682 2553 KEAEEEMLRKQKEMQELERQR 2573
Cdd:COG4913 415 RDLRRELRELEAEIASLERRK 435
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1683-1977 |
2.17e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1683 ESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKV 1762
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1763 RSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLA 1842
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1843 AISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQR 1922
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 1923 RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKL 1977
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADL 342
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3055-3090 |
2.23e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.23e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1988774682 3055 LNLLEAQAGTGYLVDPVHNQKYTVDEAVKAGVVGPE 3090
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2310-2478 |
2.31e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.17 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2310 QAIQEASRLKAEAEmlqKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQlEIMAEAERLRLQVSQlseAQ 2389
Cdd:COG2268 196 EIIRDARIAEAEAE---RETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKA-EERREAETARAEAEA---AY 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2390 ARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEferlntskeADDLRKAIADLENEKARLKKEAEELQNKSKEM 2469
Cdd:COG2268 269 EIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELE---------ADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAE 339
|
....*....
gi 1988774682 2470 ADAQQKKIE 2478
Cdd:COG2268 340 AEGKRALAE 348
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4383-4420 |
2.32e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.32e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1988774682 4383 QRFLEVQYLTGGLIEPDVEGRVSIDESIRKGTIDARTA 4420
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1549-1799 |
2.47e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1549 EAERQvkqaEIEKEKQIKVAHEAAqksaaaELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREE 1628
Cdd:pfam17045 5 EAELQ----ELMKQIDIMVAHKKS------EWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1629 AEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKR--AKAEESALKQKEMAEEELERQRKIAEST 1706
Cdd:pfam17045 75 LVAKYEQQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRlnGKLEEFRQKSLEWEQQRLQYQQQVASLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1707 AQQKLTAEQ-ELIRLRADFDNAEQQRSLLED---ELYRLKNEVAAAQQQRKQLEDELAKVRSEMDIL------IQLKTKA 1776
Cdd:pfam17045 155 AQRKALAEQsSLIQSAAYQVQLEGRKQCLEAsqsEIQRLRSKLERAQDSLCAQELELERLRMRVSELgdsnrkLLEEQQR 234
|
250 260
....*....|....*....|...
gi 1988774682 1777 EKETMSNTEKSKQLLEAEAAKMK 1799
Cdd:pfam17045 235 LLEELRMSQRQLQVLQNELMELK 257
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1464-1885 |
2.60e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.96 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1464 ETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKL 1543
Cdd:COG3064 30 EAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1544 RMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAE 1623
Cdd:COG3064 110 AEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1624 NSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIA 1703
Cdd:COG3064 190 VEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1704 ESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSN 1783
Cdd:COG3064 270 GAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1784 TEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEA 1863
Cdd:COG3064 350 AAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGA 429
|
410 420
....*....|....*....|..
gi 1988774682 1864 ENERLRRQAEDEAYQRKALEDQ 1885
Cdd:COG3064 430 AGAVVALLVKLVADLAGGLVGI 451
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1763-2558 |
2.64e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1763 RSEMDILIQLKTKAEKETMSNT---EKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEeAARQR--------- 1830
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRrqlAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQT-ALRQQekieryqad 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1831 -AEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDeaYQRkALEDQ---ASQHKQEIE--EKIVQLKKSS 1904
Cdd:PRK04863 357 lEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD--YQQ-ALDVQqtrAIQYQQAVQalERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1905 EAEMERQKAIVDDTLKQRRVVEEEIRIL--KLNFEKASSGKLDLELELnkLKNIADET-----QQSKIRAEEEAEKLRKL 1977
Cdd:PRK04863 434 DLTADNAEDWLEEFQAKEQEATEELLSLeqKLSVAQAAHSQFEQAYQL--VRKIAGEVsrseaWDVARELLRRLREQRHL 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1978 AleeekrrreaeekvkkiaaaeeEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQS 2057
Cdd:PRK04863 512 A----------------------EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLES 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2058 vLAQQIEDSITQKklkeeyekakklakeaeaakekaereaALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRkeAEF 2137
Cdd:PRK04863 570 -LSESVSEARERR---------------------------MALRQQLEQLQARIQRLAARAPAWLAAQDALARLR--EQS 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2138 EAAKRAQAEAAALMQKQQadtemakhKKLAEQTLkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKD---------- 2207
Cdd:PRK04863 620 GEEFEDSQDVTEYMQQLL--------ERERELTV-ERDELAARKQALDEEIERLSQPGGSEDPRLNALAErfggvllsei 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2208 ----EVDDA---------------VKQRGQVEEEL-------------------FKVKVQMEELLKlKNKIEEENQRLIK 2249
Cdd:PRK04863 691 yddvSLEDApyfsalygparhaivVPDLSDAAEQLagledcpedlyliegdpdsFDDSVFSVEELE-KAVVVKIADRQWR 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2250 KDKDSTQKLLAEEAENMR---------KLAEDAARLSVEAQEAARLRQIAEDDLNQQRALA-----EKMLKEKMQAIQEA 2315
Cdd:PRK04863 770 YSRFPEVPLFGRAAREKRieqlraereELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVEL 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2316 SRLKAEAE----MLQKQKDLAQEQAQ---------KLLEDKQLmQQRLEEETEEYHKSLEVERK--------RQLEIMAE 2374
Cdd:PRK04863 850 ERALADHEsqeqQQRSQLEQAKEGLSalnrllprlNLLADETL-ADRVEEIREQLDEAEEAKRFvqqhgnalAQLEPIVS 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2375 A--------ERLRLQVSQLseaqaraEEEAKKFKKQADKVAtrlheteiatqekmTVVERLefERLNTSKEADDLRKAIA 2446
Cdd:PRK04863 929 VlqsdpeqfEQLKQDYQQA-------QQTQRDAKQQAFALT--------------EVVQRR--AHFSYEDAAEMLAKNSD 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2447 DLENEKARLkKEAEELQNKSKEMADAQQKKIEHEKTV---LQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEevkKAKAL 2523
Cdd:PRK04863 986 LNEKLRQRL-EQAEQERTRAREQLRQAQAQLAQYNQVlasLKSSYDAKRQMLQELKQELQDLGVPADSGAEE---RARAR 1061
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1988774682 2524 KDE-QER------QKQQMEQEKKTLQATMDAALSKQKEAEEE 2558
Cdd:PRK04863 1062 RDElHARlsanrsRRNQLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2337-2613 |
2.65e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 46.99 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2337 QKLLEDKQLMQQRLEEEteEYHKSLEVERKRQLeiMAEAERLRLQVSQLSEAQARAEEEAKKFKkQADKVATRLHEteia 2416
Cdd:pfam05622 3 SEAQEEKDELAQRCHEL--DQQVSLLQEEKNSL--QQENKKLQERLDQLESGDDSGTPGGKKYL-LLQKQLEQLQE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2417 tqekmtvverlEFERLNTSKeaDDLRKAIADLENEKARLKKEAEELQNKSKEmadAQQKKIEHEktVLQQTfmteKEMLL 2496
Cdd:pfam05622 74 -----------ENFRLETAR--DDYRIKCEELEKEVLELQHRNEELTSLAEE---AQALKDEMD--ILRES----SDKVK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2497 KKEKLIEDEKKRLES-----------------------QFEEEVKKAKALKDEQERQKQQMEQekktLQATMDAALSKQK 2553
Cdd:pfam05622 132 KLEATVETYKKKLEDlgdlrrqvklleernaeymqrtlQLEEELKKANALRGQLETYKRQVQE----LHGKLSEESKKAD 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2554 EAEEEMLRKQKEMQELERqrlEQERILAEENQkLREKLQQLEDAQKDQHTRETDKVLHKD 2613
Cdd:pfam05622 208 KLEFEYKKLEEKLEALQK---EKERLIIERDT-LRETNEELRCAQLQQAELSQADALLSP 263
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2457-2599 |
2.68e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2457 KEAEELQNKSKEMADAQQKKiehEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfEEEVKKAKALKDEQERQKQQMEQ 2536
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQR---KKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQAEEAAKQAALKQKQAEEA 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774682 2537 EKKTLQATMDAALSKQKEAEEemLRKQKEMQELERQRLEQERILAEENQKLRE---KLQQLEDAQK 2599
Cdd:PRK09510 138 AAKAAAAAKAKAEAEAKRAAA--AAKKAAAEAKKKAEAEAAKKAAAEAKKKAEaeaAAKAAAEAKK 201
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1341-2202 |
2.69e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1341 DTQRRLDDEEKAAEKLkAEERKKMAEMQAELDKQKQLAEAH----AKAIAKAEK--------EAQELKLKMQEEVSK-RE 1407
Cdd:COG3096 296 GARRQLAEEQYRLVEM-ARELEELSARESDLEQDYQAASDHlnlvQTALRQQEKieryqedlEELTERLEEQEEVVEeAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1408 IAAVDAEKQKTNIQLELQELKNlseqQIKDKSQQVDEaLHSRTkieeeirlirIQLETTEKQKYTAEsELKQLRDRAAEA 1487
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKS----QLADYQQALDV-QQTRA----------IQYQQAVQALEKAR-ALCGLPDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1488 eklrklAQDEAEKLRKQVSEETQKKRQAEEELkrkSEAEkEAAKQKQKALEDLEKL-----RMQAEEAERQVkqaeieke 1562
Cdd:COG3096 439 ------AEDYLAAFRAKEQQATEEVLELEQKL---SVAD-AARRQFEKAYELVCKIageveRSQAWQTAREL-------- 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1563 kqikVAHEAAQKSAAAELQSKHMSFAEktskLEESLKQEHGAVLQLQQEAERLKKQQEDA---ENSREEAEKELEKWRQK 1639
Cdd:COG3096 501 ----LRRYRSQQALAQRLQQLRAQLAE----LEQRLRQQQNAERLLEEFCQRIGQQLDAAeelEELLAELEAQLEELEEQ 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1640 ANEAL--RLRLQAEDEAHKktlaqeeaekqkeEAEREAKKRA----KAEESALKQKEMAEEELERQRKIAEsTAQQKLTA 1713
Cdd:COG3096 573 AAEAVeqRSELRQQLEQLR-------------ARIKELAARApawlAAQDALERLREQSGEALADSQEVTA-AMQQLLER 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1714 EQELIRLRadfDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVR-SEM--DILIqlktkaeketmsntekskql 1790
Cdd:COG3096 639 EREATVER---DELAARKQALESQIERLSQPGGAEDPRLLALAERLGGVLlSEIydDVTL-------------------- 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1791 leaeaakmkdlaEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAIS-------EATRLKTEAEIALKEKEA 1863
Cdd:COG3096 696 ------------EDAPYFSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLYLIEgdpdsfdDSVFDAEELEDAVVVKLS 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1864 ENE-RLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSS--EAEMERQKAIVDDTLKQRRVV------EEEIRILKl 1934
Cdd:COG3096 764 DRQwRYSRFPEVPLFGRAAREKRLEELRAERDELAEQYAKASfdVQKLQRLHQAFSQFVGGHLAVafapdpEAELAALR- 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1935 nfekASSGKLDLELElnklkNIADETQQSKIRAEEEAEKLRKLAleeekrrreaeekvKKIAAAEEEAARQRKAALEELE 2014
Cdd:COG3096 843 ----QRRSELERELA-----QHRAQEQQLRQQLDQLKEQLQLLN--------------KLLPQANLLADETLADRLEELR 899
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2015 RLRKKAEEAR---KQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQieDSITQKKLKEEYEKAKKLAKEAEAAKE 2091
Cdd:COG3096 900 EELDAAQEAQafiQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQ--RRLKQQIFALSEVVQRRPHFSYEDAVG 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2092 KAEREAAL---LRQQAEEAERQKTAAEEEAANQAKAQEDA-------------------ERLRKEAEFEAAKRAQAEAAA 2149
Cdd:COG3096 978 LLGENSDLnekLRARLEQAEEARREAREQLRQAQAQYSQYnqvlaslkssrdakqqtlqELEQELEELGVQADAEAEERA 1057
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 2150 LMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEEL 2202
Cdd:COG3096 1058 RIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1529-1719 |
2.83e-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: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1529 AAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKekqikvaheAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQL 1608
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAEL---------AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1609 QQEAERLKKQQEDAENSRE--EAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESAL 1686
Cdd:COG1579 72 EARIKKYEEQLGNVRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180 190
....*....|....*....|....*....|...
gi 1988774682 1687 KQKEMAEEELERQRKIAESTAQQKLTAEQELIR 1719
Cdd:COG1579 152 AELEAELEELEAEREELAAKIPPELLALYERIR 184
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3425-3456 |
2.93e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.93e-04
10 20 30
....*....|....*....|....*....|..
gi 1988774682 3425 KLLSAEKAVTGYKDPFTGNKISLFEAMQKDLI 3456
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1698-1924 |
3.33e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.86 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1698 RQRKiAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELyRLKnevAAAQQQRKQLEDE----LAKVRSEMDILIQLK 1773
Cdd:PRK05035 432 RQAK-AEIRAIEQEKKKAEEAKARFEARQARLEREKAAREA-RHK---KAAEARAAKDKDAvaaaLARVKAKKAAATQPI 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1774 TKAEKETMSNTEkskqllEAEAAKMKDLAEEASRLRAISEEAKHQRQiAEEEAARQRAEAERILKEKLAAISEATRLKTE 1853
Cdd:PRK05035 507 VIKAGARPDNSA------VIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKKAAQQAANAEAEEEVDPKK 579
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 1854 AEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDtlKQRRV 1924
Cdd:PRK05035 580 AAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDP--RKAAV 648
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1673-1957 |
3.50e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1673 REAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 1752
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1753 KQLEDELAKVRSEMDIL------IQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQ--RQIAEE 1824
Cdd:COG4372 83 EELNEQLQAAQAELAQAqeelesLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEleEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1825 EAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSS 1904
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 1905 EAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIA 1957
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALEL 295
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1484-1635 |
3.56e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1484 AAEAEKLRKLAQ---------DEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQV 1554
Cdd:COG1579 3 PEDLRALLDLQEldseldrleHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1555 K-----------QAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAE 1623
Cdd:COG1579 83 GnvrnnkeyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|..
gi 1988774682 1624 NSREEAEKELEK 1635
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1374-1565 |
3.70e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1374 QKQLAEAHAKaIAKAEKEAQELKLK-----MQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQ---QIKDKSQQVDEA 1445
Cdd:COG3206 181 EEQLPELRKE-LEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAlraQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1446 LHSRTKIEEEIRLIRIQLE-TTEKQKYTAES-ELKQLRDRAAEAEK-LRKLAQDEAEKLRKQVSEETQKK---RQAEEEL 1519
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAElAELSARYTPNHpDVIALRAQIAALRAqLQQEAQRILASLEAELEALQAREaslQAQLAQL 339
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1988774682 1520 KRKSEAEKEAAkQKQKALE-DLEKLRMQAEEAERQVKQAEIEKEKQI 1565
Cdd:COG3206 340 EARLAELPELE-AELRRLErEVEVARELYESLLQRLEEARLAEALTV 385
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2241-2381 |
3.70e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.48 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2241 EEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDdlnQQRALAEKMLKEKMQAIQEASRLKa 2320
Cdd:pfam15709 356 EQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEE---RKQRLQLQAAQERARQQQEEFRRK- 431
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 2321 eaeMLQKQKDLAQEQAQKLLEDKQlMQQRLEEETEEyhkslevERKRQLEiMAEAERLRLQ 2381
Cdd:pfam15709 432 ---LQELQRKKQQEEAERAEAEKQ-RQKELEMQLAE-------EQKRLME-MAEEERLEYQ 480
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1225-1503 |
3.81e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1225 IADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKK 1304
Cdd:COG1340 24 IEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1305 TKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKaEERKKMAEMQAELDKQKQLAEAHAKA 1384
Cdd:COG1340 104 LNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKAL-EKNEKLKELRAELKELRKEAEEIHKK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1385 IAKAEKEAQELKLKMQEEVSKREiaavdaekqktniqlELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLE 1464
Cdd:COG1340 183 IKELAEEAQELHEEMIELYKEAD---------------ELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
250 260 270
....*....|....*....|....*....|....*....
gi 1988774682 1465 TTEKQKYTAEselkqlrdRAAEAEKLRKLAQDEAEKLRK 1503
Cdd:COG1340 248 KLRKKQRALK--------REKEKEELEEKAEEIFEKLKK 278
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1225-1451 |
3.82e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1225 IADAKQRQEKIQAvpitdskTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKK 1304
Cdd:COG3883 25 LSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1305 TKLDSASDNII---QEYVTLRTRYSelmtltsqYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAH 1381
Cdd:COG3883 98 SGGSVSYLDVLlgsESFSDFLDRLS--------ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 1382 AKAI--AKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTK 1451
Cdd:COG3883 170 KAELeaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1451-1568 |
3.83e-04 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 45.75 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1451 KIEEEIRLIRIQLETtEKQKYTAESELKQLRDRAAEAEklRKLAQDEAEKLRkQVSEETQKKRQAEEE-LKRKSEAEKEA 1529
Cdd:cd03406 159 KIPEAIRRNYEAMEA-EKTKLLIAEQHQKVVEKEAETE--RKRAVIEAEKDA-EVAKIQMQQKIMEKEaEKKISEIEDEM 234
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1988774682 1530 AKQKQKALEDLE--KLRMQAEEAERQVKQAEIEKEKQIKVA 1568
Cdd:cd03406 235 HLAREKARADAEyyRALREAEANKLKLTPEYLELKKYQAIA 275
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2442-2574 |
3.87e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2442 RKAIADLENEKARLKKEAE-ELQNKSKEM-----ADAQQKKIEHEKTV---------LQQTFMTEKEMLLKKEKLIEDEK 2506
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKkEAEAIKKEAlleakEEIHKLRNEFEKELrerrnelqkLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774682 2507 KRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATmdAALSKQkEAEEEMLRKQKEMQELERQRL 2574
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI--SGLTAE-EAKEILLEKVEEEARHEAAVL 174
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1590-1723 |
4.08e-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: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1590 KTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlAQEEAEKQKE 1669
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKE--DKQVAENQKR 281
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 1670 EAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK-LTAEQELIRLRAD 1723
Cdd:pfam05262 282 EIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKeLEAQKKREPVAED 336
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1689-1911 |
4.29e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1689 KEMAEEELERQRKIAESTAQQKLTAEQELIRLRADfdnAEQQRSLLEDELyRLKNEV-AAAQQQRKQLEDE-LAKVRSEM 1766
Cdd:pfam00038 49 YSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLA---AEDFRQKYEDEL-NLRTSAeNDLVGLRKDLDEAtLARVDLEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1767 DI------LIQLKTKAE---KETMSNTEKSKQLLEAEAAKMKDLAeeasrlRAISEeakhQRQIAEEEAARQRAEAERIL 1837
Cdd:pfam00038 125 KIeslkeeLAFLKKNHEeevRELQAQVSDTQVNVEMDAARKLDLT------SALAE----IRAQYEEIAAKNREEAEEWY 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1838 KEKLAAISEATRLKTEAEIALKEKEAENERL--RRQAEDEAY--QRKALEDQ--------ASQHKQ------EIEEKIVQ 1899
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTiqSLEIELQSLkkQKASLERQlaeteeryELQLADyqelisELEAELQE 274
|
250
....*....|..
gi 1988774682 1900 LKksseAEMERQ 1911
Cdd:pfam00038 275 TR----QEMARQ 282
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1132-1544 |
4.34e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1132 AKLKKMRTEAEDeqpvfdsLEEELKKASAVSDKMVRVHSerdveldHFRQQLSSLQDRW-----KAVFTQIDLRQRELEq 1206
Cdd:COG3096 785 KRLEELRAERDE-------LAEQYAKASFDVQKLQRLHQ-------AFSQFVGGHLAVAfapdpEAELAALRQRRSELE- 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1207 lgRQLGYYResydwlirwiADAKQRQEKIQAvpitdsktLKEQLAQEKKLL------------EEIEQNKDKVDECQkYA 1274
Cdd:COG3096 850 --RELAQHR----------AQEQQLRQQLDQ--------LKEQLQLLNKLLpqanlladetlaDRLEELREELDAAQ-EA 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1275 KAYIDtikdyelQLVAYKAQVEPLVSPLKKTKLDSasDNIIQEYVTLrtrySELMTLTSQYIKFIT------------DT 1342
Cdd:COG3096 909 QAFIQ-------QHGKALAQLEPLVAVLQSDPEQF--EQLQADYLQA----KEQQRRLKQQIFALSevvqrrphfsyeDA 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1343 QRRLDDEEKAAEKLKAeerkKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqeevskreiAAVDAEKQktniql 1422
Cdd:COG3096 976 VGLLGENSDLNEKLRA----RLEQAEEARREAREQLRQAQAQYSQYNQVLASLK------------SSRDAKQQ------ 1033
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1423 ELQELKN-LSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAE-- 1499
Cdd:COG3096 1034 TLQELEQeLEELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqa 1113
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 1500 KLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQK----------QKALEDLEKLR 1544
Cdd:COG3096 1114 KAGWCAVLRLARDNDVERRLHRRELAYLSADELRsmsdkalgalRLAVADNEHLR 1168
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1891-2378 |
4.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1891 QEIEEKIVQLKksseaEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAdETQQSKIRAEEE 1970
Cdd:COG4717 71 KELKELEEELK-----EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ-ELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1971 AEKLRKLaleeEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSA 2050
Cdd:COG4717 145 PERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2051 AEQQVQSVLAqQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAER 2130
Cdd:COG4717 221 ELEELEEELE-QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2131 LRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQeltkVKLKLDETDKQKSVLdeELQRLKDEVD 2210
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE----LQELLREAEELEEEL--QLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2211 DAVKQRGQVEEELFKVKV-QMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENmrkLAEDAARLSVEAQEAARLRqi 2289
Cdd:COG4717 374 ALLAEAGVEDEEELRAALeQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE---LEEELEELEEELEELEEEL-- 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2290 aeDDLNQQRALAEKMLKEkMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLledkQLMQQRLEEETEEYHksleveRKRQL 2369
Cdd:COG4717 449 --EELREELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEYR------EERLP 515
|
....*....
gi 1988774682 2370 EIMAEAERL 2378
Cdd:COG4717 516 PVLERASEY 524
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
1532-1932 |
4.92e-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: 46.21 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1532 QKQKALEDLEkLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGavlQLQQE 1611
Cdd:pfam04747 50 QRKEAFASLE-LTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEARRAEAEAKKRAAQEEEHK---QWKAE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1612 AERLKKQQEdaenSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEM 1691
Cdd:pfam04747 126 QERIQKEQE----KKEADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTPTNTP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1692 AEEELERQRKIAESTAQQKLTAEQELIRLRADFDN-AEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILI 1770
Cdd:pfam04747 202 AEPAEQVQEITGKKNKKNKKKSESEATAAPASVEQvVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETPVEP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1771 -----------QLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASR--LRAISEEAKHQRQIAEEEAARQRAEAERIL 1837
Cdd:pfam04747 282 vvettppasenQKKNKKDKKKSESEKVVEEPVQAEAPKSKKPTADDNMdfLDFVTAKEEPKDEPAETPAAPVEEVVENVV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1838 KEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALED--QASQHKQEIEEKIVQLKKSSEAEMERQKAIV 1915
Cdd:pfam04747 362 ENVVEKSTTPPATENKKKNKKDKKKSESEKVTEQPVESAPAPPQVEQvvETTPPASENKKKNKKDKKKSESEKAVEEPVQ 441
|
410
....*....|....*..
gi 1988774682 1916 DDTLKQRRVVEEEIRIL 1932
Cdd:pfam04747 442 AAPSSKKPTADDNMDFL 458
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2274-2608 |
4.95e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2274 ARLSVEAQEAARLRQIAE--DDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQR-L 2350
Cdd:pfam07888 67 DREQWERQRRELESRVAElkEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRvL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2351 EEETEEYHKSLEVERKRQLEIMAEAERLRLQvSQLSEAQARAEEEAKKFKK------QADKVATRLHETEIATQEKMTVV 2424
Cdd:pfam07888 147 ERETELERMKERAKKAGAQRKEEEAERKQLQ-AKLQQTEEELRSLSKEFQElrnslaQRDTQVLQLQDTITTLTQKLTTA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2425 ERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEEL-QNKSKEMADAQQKKIEHEKTVLQqtfMTEKEMLLKKEKlie 2503
Cdd:pfam07888 226 HRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMaAQRDRTQAELHQARLQAAQLTLQ---LADASLALREGR--- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2504 dekkrleSQFEeevkkakalkdeQERQ--KQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILA 2581
Cdd:pfam07888 300 -------ARWA------------QEREtlQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLS 360
|
330 340
....*....|....*....|....*..
gi 1988774682 2582 EENQKLREKLQQLEDAQKDQHTRETDK 2608
Cdd:pfam07888 361 ESRRELQELKASLRVAQKEKEQLQAEK 387
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1627-1979 |
5.03e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1627 EEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQkemAEEELERQRKIAEST 1706
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ---ARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1707 AQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEM--------DILIQLKTKAEK 1778
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIaereeelkELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1779 ETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIAL 1858
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1859 KEKEAENER-LRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFE 1937
Cdd:COG4372 246 EDKEELLEEvILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1988774682 1938 KASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLAL 1979
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1823-1922 |
5.06e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 43.07 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1823 EEEAARQRAEAERILKEKLAAISEAtrlkteaEIALKEKEAENERLRRQAEDEAYQ-RKALEDQASQHkqeieekIVQLK 1901
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAALAEA-------EQQLKEARAEAQEIIENAKKRAEKlKEEIVAAAEAE-------AERII 97
|
90 100
....*....|....*....|.
gi 1988774682 1902 KSSEAEMERQKAIVDDTLKQR 1922
Cdd:pfam00430 98 EQAAAEIEQEKDRALAELRQQ 118
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1344-1508 |
5.16e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1344 RRLDDEEKAAEKLKAEERKKMAEMQAELDKQKqlaeahaKAIAKAEKEAQELKLKMQEevSKREIAAVDAEKQKTNIQLE 1423
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLE-------KEIKRLELEIEEVEARIKK--YEEQLGNVRNNKEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1424 LQELKnlseQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQkytAESELKQLRDRAAEAEKLRKLAQDEAEKLRK 1503
Cdd:COG1579 98 IESLK----RRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEELAELEAELEELEAEREELAA 170
|
....*
gi 1988774682 1504 QVSEE 1508
Cdd:COG1579 171 KIPPE 175
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1488-1710 |
5.82e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 46.14 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1488 EKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQikv 1567
Cdd:TIGR00927 628 GDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEA--- 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1568 ahEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLR 1647
Cdd:TIGR00927 705 --DHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGE 782
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774682 1648 LQA-EDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 1710
Cdd:TIGR00927 783 IQAgEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAK 846
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3349-3385 |
6.01e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 6.01e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1988774682 3349 KYLQGSSSIAGLYLEPTKEKLSIYQAMKKKLLRHNTG 3385
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1477-1615 |
6.12e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.86 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1477 LKQLRDRAAEAEKLRKLAQDEAEKLRKQV------------SEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLR 1544
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAAlleakelllrerNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 1545 MQAEEAERQVKQAEIE-KEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQ-LQQEAERL 1615
Cdd:PRK12705 105 NQLEEREKALSARELElEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEeADLEAERK 177
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2154-2286 |
6.13e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2154 QQADTEMAKHKKLAEQTLKQKF-----QVEQELTKVKLKLDETDKQ----KSVLDEELQRLKDEVDDAVKQRGQVEEELF 2224
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIhklrnEFEKELRERRNELQKLEKRllqkEENLDRKLELLEKREEELEKKEKELEQKQQ 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 2225 KVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENmrKLAEDAARLSVEAQEAARL 2286
Cdd:PRK12704 125 ELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVEE--EARHEAAVLIKEIEEEAKE 184
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1826-2071 |
6.29e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1826 AARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSsE 1905
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL-R 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1906 AEMERQKAIVDDTLkqrRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQqskiraeEEAEKLRKLALEEEKRR 1985
Cdd:COG4942 97 AELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR-------EQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1986 REAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIED 2065
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
....*.
gi 1988774682 2066 SITQKK 2071
Cdd:COG4942 247 GFAALK 252
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1343-1545 |
6.41e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.63 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1343 QRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREiaavdaekqktnIQL 1422
Cdd:COG2268 225 EAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAERE------------REI 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1423 ELQELKnlseqqikdksqqvdealhsrtKIEEEIRLIRIQLETTEKQKYTAESElkqlrdRAAEAEKLRKLAQDEAEKLR 1502
Cdd:COG2268 293 ELQEKE----------------------AEREEAELEADVRKPAEAEKQAAEAE------AEAEAEAIRAKGLAEAEGKR 344
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1988774682 1503 KQVseETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRM 1545
Cdd:COG2268 345 ALA--EAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITI 385
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1607-1761 |
6.53e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1607 QLQQEAERLKKQQEDAENSREEAEKELEKWRQ--KANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 1684
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTelEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774682 1685 ALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQrslLEDELYRLKNEVAAAQQQRKQLEDELAK 1761
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1230-1534 |
6.64e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.77 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1230 QRQEKIQAVPITDSKTLKEQLAQ-EKKLLE-EIEQNKDKVDECQKYakayiDTIKDYELQLVAYKAQVeplvSPLKKTKL 1307
Cdd:NF033838 158 QKEEDRRNYPTNTYKTLELEIAEsDVEVKKaELELVKEEAKEPRDE-----EKIKQAKAKVESKKAEA----TRLEKIKT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1308 D--SASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAE------LDKQKQLAE 1379
Cdd:NF033838 229 DreKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGEEtlpspsLKPEKKVAE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1380 AHaKAIAKAEKeaqelKLKMQEEVSKR------------EIAAVDAEKQKTNIQLELQELKnlsEQQIKDKSQQVDEALH 1447
Cdd:NF033838 309 AE-KKVEEAKK-----KAKDQKEEDRRnyptntyktlelEIAESDVKVKEAELELVKEEAK---EPRNEEKIKQAKAKVE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1448 SRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEA-----EKLRKQVSEETQKKRQAEEELKRK 1522
Cdd:NF033838 380 SKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKpapkpEKPAEQPKAEKPADQQAEEDYARR 459
|
330
....*....|..
gi 1988774682 1523 SEAEKEAAKQKQ 1534
Cdd:NF033838 460 SEEEYNRLTQQQ 471
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1714-1973 |
7.07e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1714 EQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQlktkaeketmsNTEKSKQLLEA 1793
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNE-----------KVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1794 EAAKMKDLAEEASRLRAISEE--------AKHQRQIAEEEAARQRA----EAERILKEKLAAIS---EATRLKTEAEIAL 1858
Cdd:COG1340 83 LNEKLNELREELDELRKELAElnkaggsiDKLRKEIERLEWRQQTEvlspEEEKELVEKIKELEkelEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1859 KEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDdtlKQRRVVEEEIRILKLNFEK 1938
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVE---AQEKADELHEEIIELQKEL 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1988774682 1939 AssgklDLELELNKLKNIADETQQSKIRAEEEAEK 1973
Cdd:COG1340 240 R-----ELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
181-262 |
7.49e-04 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 42.29 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 181 RCDNFTTSWRDGKLFNAVIHKHYPRLIN---MGKVYQQTNLE-NLEQAFSVAEKdLGVTRLLDPEDVDVPHPDEksIITY 256
Cdd:cd21218 32 RVTNFSSDLKDGEVYALLLHSLAPELCDkelVLEVLSEEDLEkRAEKVLQAAEK-LGCKYFLTPEDIVSGNPRL--NLAF 108
|
....*.
gi 1988774682 257 VSSLYD 262
Cdd:cd21218 109 VATLFN 114
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
811-855 |
8.03e-04 |
|
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212702 [Multi-domain] Cd Length: 54 Bit Score: 40.33 E-value: 8.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1988774682 811 IQAVCDFK---QQEITVHKGDECALLNNSQPFKWKVLNRSGHEAMVPS 855
Cdd:cd11768 2 VVALYDFQpiePGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2234-2373 |
8.14e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2234 LKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQ 2313
Cdd:PRK00409 497 LGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ 576
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 2314 EA-SRLKAEAEMLQKQKDLAQEQAQKLLEDKQL--MQQRLEEETEEYHKSLEVERKRQLEIMA 2373
Cdd:PRK00409 577 QAiKEAKKEADEIIKELRQLQKGGYASVKAHELieARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2326-2558 |
8.46e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2326 QKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLE--IMAEAERLRLQVSQLSeaqaraeeeakkfKKQA 2403
Cdd:PRK05035 441 IEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAKDKdaVAAALARVKAKKAAAT-------------QPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2404 DKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKE-------------MA 2470
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEeevdpkkaavaaaIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2471 DAQQKKIEHEKTVLQQTFMTEKEMLLK--------KEKLIEDEKKRLESQFEEE----------VKKAKALKDEQERQKQ 2532
Cdd:PRK05035 588 RAKAKKAAQQAASAEPEEQVAEVDPKKaavaaaiaRAKAKKAEQQANAEPEEPVdprkaavaaaIARAKARKAAQQQANA 667
|
250 260
....*....|....*....|....*...
gi 1988774682 2533 QMEQEKKTLQATMDAALS--KQKEAEEE 2558
Cdd:PRK05035 668 EPEEAEDPKKAAVAAAIAraKAKKAAQQ 695
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1459-1558 |
8.56e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1459 IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLA-QDEAEKLRKqvsEETQKKRQAEEeLKRKSEAEKEAAKQKQKAL 1537
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAsFERLAELRD---ELAELEEELEA-LKARWEAEKELIEEIQELK 477
|
90 100
....*....|....*....|.
gi 1988774682 1538 EDLEKLRMQAEEAERQVKQAE 1558
Cdd:COG0542 478 EELEQRYGKIPELEKELAELE 498
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1311-1683 |
8.61e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1311 SDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEK 1390
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1391 EAQELKLKMQEEVSKREiaavDAEKQKTNIQLELQELknlsEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQK 1470
Cdd:COG4372 81 ELEELNEQLQAAQAELA----QAQEELESLQEEAEEL----QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1471 YTAESELKQLRDRAAEAEK-----LRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRM 1545
Cdd:COG4372 153 KELEEQLESLQEELAALEQelqalSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1546 QAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENS 1625
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774682 1626 REEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEE 1683
Cdd:COG4372 313 LEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2219-2568 |
8.73e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2219 VEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAE------- 2291
Cdd:COG5185 188 LLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEqntdlrl 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2292 DDLNQQRALAEKMLKEKMQAIQEASRLKAE-AEMLQKQKDLA-----QEQAQKLLEDKQLMQQRLEEETEEYHKSLEVEr 2365
Cdd:COG5185 268 EKLGENAESSKRLNENANNLIKQFENTKEKiAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETETGIQNLTAEIE- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2366 KRQLEIMAEAERLRLQVSQLSEAQARAEEEAK--KFKKQADKVATRLHETEIATQEKMTVVER-LEFERLNTSKEADDLR 2442
Cdd:COG5185 347 QGQESLTENLEAIKEEIENIVGEVELSKSSEEldSFKDTIESTKESLDEIPQNQRGYAQEILAtLEDTLKAADRQIEELQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2443 KAIADLENEKARLKKEAEELQNkskEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKA 2522
Cdd:COG5185 427 RQIEQATSSNEEVSKLLNELIS---ELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEK 503
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1988774682 2523 LKDEQERQKQQMEQEKKTLQATMDAALSKQKEA---EEEMLRKQKEMQE 2568
Cdd:COG5185 504 LRAKLERQLEGVRSKLDQVAESLKDFMRARGYAhilALENLIPASELIQ 552
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2404-2604 |
9.02e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2404 DKVATRLHETEIATQEKMTVVERLEFERlNTSKEADDLRKAIADLE-NEKARLKKEAEelqnKSKEMADAQQKKIEHEKT 2482
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRRER-EKAERYQALLKEKREYEgYELLKEKEALE----RQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2483 vlqqtfmtekemllKKEKLIEDEKKRLESqfeeevkKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRK 2562
Cdd:TIGR02169 255 --------------KLTEEISELEKRLEE-------IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEK 313
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1988774682 2563 QKEMQELErqrlEQERILAEENQKLREKLQQLEDAQKDQHTR 2604
Cdd:TIGR02169 314 ERELEDAE----ERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2769-2799 |
9.17e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 9.17e-04
10 20 30
....*....|....*....|....*....|.
gi 1988774682 2769 LLAERAVVGYKDPYTGGKISVFEAMKKGLIE 2799
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2450-2601 |
9.87e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2450 NEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKL--IEDEKKRLESQFEEEVKKAKALKDEQ 2527
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIraLEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2528 ERQKQQMEQEKKTLQ-----------------------ATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQER-ILAEE 2583
Cdd:COG4942 100 EAQKEELAELLRALYrlgrqpplalllspedfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERaELEAL 179
|
170
....*....|....*...
gi 1988774682 2584 NQKLREKLQQLEDAQKDQ 2601
Cdd:COG4942 180 LAELEEERAALEALKAER 197
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1149-1496 |
9.96e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1149 DSLEEELKKASAVSDKMVRVHserdvelDHFRQQLSSLQDRWKAVFTQIDLR--QRELEQLGRQLGYYREsydwlirwia 1226
Cdd:PRK04863 796 EELAERYATLSFDVQKLQRLH-------QAFSRFIGSHLAVAFEADPEAELRqlNRRRVELERALADHES---------- 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1227 daKQRQEKIQAvpitdsKTLKEQLAQEKKLL------------EEIEQNKDKVDECQKyAKAYIDtikdyelQLVAYKAQ 1294
Cdd:PRK04863 859 --QEQQQRSQL------EQAKEGLSALNRLLprlnlladetlaDRVEEIREQLDEAEE-AKRFVQ-------QHGNALAQ 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1295 VEPLVSPLKktkldsaSDNiiQEYVTLRTRYSELMTLTSQYIKFI---------------TDTQRRLDDEEKAAEKLKAe 1359
Cdd:PRK04863 923 LEPIVSVLQ-------SDP--EQFEQLKQDYQQAQQTQRDAKQQAfaltevvqrrahfsyEDAAEMLAKNSDLNEKLRQ- 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1360 erkKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqeevskreiAAVDAEKQktNIQLELQELKNL-------SE 1432
Cdd:PRK04863 993 ---RLEQAEQERTRAREQLRQAQAQLAQYNQVLASLK------------SSYDAKRQ--MLQELKQELQDLgvpadsgAE 1055
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 1433 QQIKDKSQQVDEALHS----RTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEK----LRKLAQD 1496
Cdd:PRK04863 1056 ERARARRDELHARLSAnrsrRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAgwcaVLRLVKD 1127
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1521-1715 |
1.01e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1521 RKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKtsklEESLKQ 1600
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK----EENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1601 EHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAL-RL-RLQAEdEAHKKTLaqeeaekqkeeaeREAKKR 1678
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELeRIsGLTAE-EAKEILL-------------EKVEEE 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 1988774682 1679 AKAEESAL-KQKEM-AEEELERQRKIAESTAQQKLTAEQ 1715
Cdd:PRK12704 167 ARHEAAVLiKEIEEeAKEEADKKAKEILAQAIQRCAADH 205
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2286-2477 |
1.04e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2286 LRQIAEDDLNQQRALAEKMLKEKmqaiqeasrlKAEAEMLQKQKDL-AQEQAQKLledkqlmQQRLEEETEEYHKSLEve 2364
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEA----------KKEAEAIKKEALLeAKEEIHKL-------RNEFEKELRERRNELQ-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2365 rkrQLEimaeaERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETE--IATQEKMTVVERLEFERLN--TSKEADD 2440
Cdd:PRK12704 86 ---KLE-----KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEkkEEELEELIEEQLQELERISglTAEEAKE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1988774682 2441 --LRKAIADLENEKARLKKEAEElqnKSKEMADAQQKKI 2477
Cdd:PRK12704 158 ilLEKVEEEARHEAAVLIKEIEE---EAKEEADKKAKEI 193
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1495-1574 |
1.11e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.33 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1495 QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAK------QKQKALE-DLEKLRMQAEEAERQvkqaeiEKEKQIKV 1567
Cdd:PRK11448 148 QQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGlaaeleEKQQELEaQLEQLQEKAAETSQE------RKQKRKEI 221
|
....*..
gi 1988774682 1568 AHEAAQK 1574
Cdd:PRK11448 222 TDQAAKR 228
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2154-2307 |
1.14e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2154 QQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVK------ 2227
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2228 -VQME-ELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKML 2305
Cdd:COG1579 93 aLQKEiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
..
gi 1988774682 2306 KE 2307
Cdd:COG1579 173 PP 174
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1673-2071 |
1.14e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1673 REAKKRAKAEESALKqkemAEEELERQRKiaestaqqKLTAEQE-LIRLRADFDNAEQQRSLLEDELYRLK---NEVAAA 1748
Cdd:PRK04863 276 RHANERRVHLEEALE----LRRELYTSRR--------QLAAEQYrLVEMARELAELNEAESDLEQDYQAASdhlNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1749 QQQRKQLEdelakvRSEMDILiQLKTKAEKETMSNTEKSKQLLEAEAAKmkDLAEEaSRLRAISEEAKHQRQIaeeEAAR 1828
Cdd:PRK04863 344 LRQQEKIE------RYQADLE-ELEERLEEQNEVVEEADEQQEENEARA--EAAEE-EVDELKSQLADYQQAL---DVQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1829 QRAEAERilkEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHK--QEIEEKIVQLKKSSEA 1906
Cdd:PRK04863 411 TRAIQYQ---QAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQaaHSQFEQAYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1907 EMERQKAivDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNK---LKNIADETQQSKIRAEEEAEKLRKLALEEEK 1983
Cdd:PRK04863 488 EVSRSEA--WDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1984 RRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEkQIVVAQQAAQKCSAAEQQVQSVL--AQ 2061
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLRE-QSGEEFEDSQDVTEYMQQLLEREreLT 644
|
410
....*....|
gi 1988774682 2062 QIEDSITQKK 2071
Cdd:PRK04863 645 VERDELAARK 654
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2437-2538 |
1.14e-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: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2437 EADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKkeklIEDEKKRLESQFEEE 2516
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEE----IQELKEELEQRYGKI 487
|
90 100
....*....|....*....|..
gi 1988774682 2517 VKKAKALKDEQERQKQQMEQEK 2538
Cdd:COG0542 488 PELEKELAELEEELAELAPLLR 509
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1610-1833 |
1.18e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1610 QEAERLKKQQEDAENSREEAEKELEkwrQKANEalrlrLQAEDEAHkktlaqeeaekqkeeaeRE-----AKKRAKAEES 1684
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQ---QQAEE-----LQQKQAAE-----------------QErlkqlEKERLAAQEQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1685 ALKQKEMAEEELERQRKIAESTAQQ----KLTAEQELIRLRADFDNAEQQrslledelyrlKNEVAAAQQQRKQLEDELA 1760
Cdd:PRK09510 117 KKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAAKKAAAE-----------AKKKAEAEAAKKAAAEAKK 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 1761 KVRSEMdiliqlKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEA 1833
Cdd:PRK09510 186 KAEAEA------AAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1819-1995 |
1.21e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1819 RQIAEEEAARQRAEAERILKEklaAISEATRLKTEAEIALKEkeaENERLRRQAEDEAYQRKA----LEDQASQHKQEIE 1894
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEE---AKKEAEAIKKEALLEAKE---EIHKLRNEFEKELRERRNelqkLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1895 EKIVQLKKSsEAEMERQKAIVDDTLKQRRVVEEEIRILKLnfekassgKLDLELE--------------LNKLKNIADET 1960
Cdd:PRK12704 100 RKLELLEKR-EEELEKKEKELEQKQQELEKKEEELEELIE--------EQLQELErisgltaeeakeilLEKVEEEARHE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1988774682 1961 QQSKIR-----AEEEAEKlrklaleeekrrreaeeKVKKI 1995
Cdd:PRK12704 171 AAVLIKeieeeAKEEADK-----------------KAKEI 193
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1478-1578 |
1.21e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.47 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1478 KQLRDRAAEAEKLRKlaqdEAEKLRKQVSEETQK-KRQAEEELKrksEAEKEAAKQKQKALEDLEklrmqaEEAERQVKQ 1556
Cdd:COG0711 34 EKIADGLAEAERAKE----EAEAALAEYEEKLAEaRAEAAEIIA---EARKEAEAIAEEAKAEAE------AEAERIIAQ 100
|
90 100
....*....|....*....|..
gi 1988774682 1557 AEIEKEKQIKVAHEAAQKSAAA 1578
Cdd:COG0711 101 AEAEIEQERAKALAELRAEVAD 122
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2397-2577 |
1.24e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2397 KKFKKQADKVATRLHETEIATQEKmtvVERLEFERLntskEADDLRKAIADLENEKARLKKEAEELQNKSKEM----ADA 2472
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQER---LKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAakakAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2473 QQK-------KIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfeeevKKAKALKDEQERQKQQMEQEKKTLQATM 2545
Cdd:PRK09510 152 EAKraaaaakKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAE-----AKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
170 180 190
....*....|....*....|....*....|..
gi 1988774682 2546 DAALSKQKEAEEEMLRKQKEMQELERQRLEQE 2577
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1930-2356 |
1.28e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1930 RILKLNFEKASSGKLDLELELNKLKNIADETQQ-SKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKA 2008
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2009 ALEELERLRKKAEEaRKQKDEADKEAEKQIvvaQQAAQKCSAAEQQVQSVLAQQIEDsitqkkLKEEYEKAKKLAKEAEA 2088
Cdd:COG4717 144 LPERLEELEERLEE-LRELEEELEELEAEL---AELQEELEELLEQLSLATEEELQD------LAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2089 AKEKAEREAALLRQQAEEAERQKTaaeeeaanqakAQEDAERLrKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLA- 2167
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELE-----------AAALEERL-KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2168 ---------EQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKN 2238
Cdd:COG4717 282 vlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2239 KI-----EEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLsveAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQ 2313
Cdd:COG4717 362 ELqleelEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELE 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1988774682 2314 EA-SRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEE 2356
Cdd:COG4717 439 EElEELEEELEELREELAELEAELEQLEEDGELAELLQELEELK 482
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1627-1872 |
1.30e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1627 EEAE-KELEKWRQKANEAlRLRLQA-----EDEAhkktlaqeeaekqkeeAEREAKKRAKAEESALKQKEMAEEELER-Q 1699
Cdd:PRK05035 434 AKAEiRAIEQEKKKAEEA-KARFEArqarlEREK----------------AAREARHKKAAEARAAKDKDAVAAALARvK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1700 RKIAESTAQQKLTAEQE--------LIRLRADFDNAEQQRSLLEDELYRLKNEVAAA----QQQRKQLEDELAKVRSEMD 1767
Cdd:PRK05035 497 AKKAAATQPIVIKAGARpdnsaviaAREARKAQARARQAEKQAAAAADPKKAAVAAAiaraKAKKAAQQAANAEAEEEVD 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1768 iliQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEE-AKHQRQIAEEEAARQRAEAERILKEKLAAISE 1846
Cdd:PRK05035 577 ---PKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKAAVAAAIA 653
|
250 260
....*....|....*....|....*.
gi 1988774682 1847 ATRLKTEAEIALKEKEAENERLRRQA 1872
Cdd:PRK05035 654 RAKARKAAQQQANAEPEEAEDPKKAA 679
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2414-2535 |
1.35e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2414 EIATQ----EKMTVVERLEFErlntSKEADDLRKAIADLENEKAR---LKKEAE----ELQNKSKEMADAQQK--KIEHE 2480
Cdd:PTZ00491 658 EITTKsqeaAARHQAELLEQE----ARGRLERQKMHDKAKAEEQRtklLELQAEsaavESSGQSRAEALAEAEarLIEAE 733
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 2481 KTVlQQTFMTEKEMLLKKEKLIEDEKKRLE-------SQFEEEVKKAKALKD-EQERQKQQME 2535
Cdd:PTZ00491 734 AEV-EQAELRAKALRIEAEAELEKLRKRQEleleyeqAQNELEIAKAKELADiEATKFERIVE 795
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1728-1864 |
1.41e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1728 EQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSemdiliqLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASR 1807
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEA-------LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774682 1808 LR--AISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAE 1864
Cdd:PRK00409 578 AIkeAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1854-2595 |
1.45e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.74 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1854 AEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILK 1933
Cdd:pfam07111 7 SDIPLVQSPGHQDVLERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQQAELISRQLQELRRLEEEVRLLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1934 lnfekassgkldlelelnklkniaDETQQSKIRAEEEAEKLRKLAleeekrrreaeekvkkiaaaeeeaaRQRKAALEEL 2013
Cdd:pfam07111 87 ------------------------ETSLQQKMRLEAQAMELDALA-------------------------VAEKAGQAEA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2014 ERLRKK---AEEARKQKDEAD-KEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDsiTQKKLKEeyekakklakeaeaa 2089
Cdd:pfam07111 118 EGLRAAlagAEMVRKNLEEGSqRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEG--LEKSLNS--------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2090 kekaereaaLLRQQAEEAERqktaaeeeaanQAKAQEDAERLRKEaefeaakraqaeaaalMQKQQADTEmakhkklAEQ 2169
Cdd:pfam07111 181 ---------LETKRAGEAKQ-----------LAEAQKEAELLRKQ----------------LSKTQEELE-------AQV 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2170 TLKQ---KFQVEQELTKVKLKLDETDKQKsvLDEELQRLKDEVDDAvkqrgQVEEELFKVKVQmeellklknkieeenqr 2246
Cdd:pfam07111 218 TLVEslrKYVGEQVPPEVHSQTWELERQE--LLDTMQHLQEDRADL-----QATVELLQVRVQ----------------- 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2247 likkdkDSTQKLLAEEAENMRKLAEDAarlSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQ 2326
Cdd:pfam07111 274 ------SLTHMLALQEEELTRKIQPSD---SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQ 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2327 KQ-KDLAQEQA--QKLLEDK--QLMQQRLEEET--EEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKF 2399
Cdd:pfam07111 345 EQvTSQSQEQAilQRALQDKaaEVEVERMSAKGlqMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRV 424
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2400 KKQADKVATRLHETEIATQEKMTV---------VERLEFERLNTSKEA----DDLRKAIADLENEKARLKKE----AEEL 2462
Cdd:pfam07111 425 EQAVARIPSLSNRLSYAVRKVHTIkglmarkvaLAQLRQESCPPPPPAppvdADLSLELEQLREERNRLDAElqlsAHLI 504
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2463 QN---KSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 2539
Cdd:pfam07111 505 QQevgRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVA 584
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774682 2540 TLQATMDAALSKQKEAEEEMLRKQ------------KEMQELERQ---RLEQERILAEENQKLREKLQQLE 2595
Cdd:pfam07111 585 EVETRLREQLSDTKRRLNEARREQakavvslrqiqhRATQEKERNqelRRLQDEARKEEGQRLARRVQELE 655
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1371-1527 |
1.46e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 42.61 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1371 LDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQEL---KNLSEQQIKDKSQQVDEAlh 1447
Cdd:pfam08614 13 LDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELyrsRGELAQRLVDLNEELQEL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1448 srtkiEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEE--------L 1519
Cdd:pfam08614 91 -----EKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKEnrelverwM 165
|
....*....
gi 1988774682 1520 KRKS-EAEK 1527
Cdd:pfam08614 166 KRKGqEAEA 174
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2422-2601 |
1.47e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.48 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2422 TVVERLEFERLNTSKE----------ADDLRK--------AIADLENEK-----------ARLKKEAEELQN---KSKEM 2469
Cdd:COG2268 135 AVAAQMTVEELNEDREkfaekvqevaGTDLAKnglelesvAITDLEDENnyldalgrrkiAEIIRDARIAEAeaeRETEI 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2470 ADAQQKKIEHEKTVLQQTfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAK---ALKDEQERQKQQMEQEKKTLQATMD 2546
Cdd:COG2268 215 AIAQANREAEEAELEQER---EIETARIAEAEAELAKKKAEERREAETARAEaeaAYEIAEANAEREVQRQLEIAERERE 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2547 AALsKQKEAEEEMLRKQKEMQ---ELERQRLEQE------------RILAEENQKLREKLQQLEDAQKDQ 2601
Cdd:COG2268 292 IEL-QEKEAEREEAELEADVRkpaEAEKQAAEAEaeaeaeairakgLAEAEGKRALAEAWNKLGDAAILL 360
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2205-2604 |
1.48e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2205 LKDEVDDAVKQRGQVEEELFKVKVQMEELLK---LKNKIEEENQRLIKKDKDSTQKLLAE-EAENMRKLAEDAARLSVEA 2280
Cdd:pfam12128 198 VKSMIVAILEDDGVVPPKSRLNRQQVEHWIRdiqAIAGIMKIRPEFTKLQQEFNTLESAElRLSHLHFGYKSDETLIASR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2281 QEAarlRQIAEDDLNQQRALAEKMLKEKMQAI-QEASRLKAEAEMLQKQKDLAQEQAQklledkqlmqQRLEEETEEYHk 2359
Cdd:pfam12128 278 QEE---RQETSAELNQLLRTLDDQWKEKRDELnGELSAADAAVAKDRSELEALEDQHG----------AFLDADIETAA- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2360 sleverkrqleimAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRlheTEIATQEKMTVVERLEfERLNTSKEAD 2439
Cdd:pfam12128 344 -------------ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRR---RSKIKEQNNRDIAGIK-DKLAKIREAR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2440 DLRKAIA--DLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLK--KEKLIEDEKKRLESQFEE 2515
Cdd:pfam12128 407 DRQLAVAedDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLenFDERIERAREEQEAANAE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2516 ------EVKKAKALKDEQERQKQQMEQEKKTLQATMDAA--------------LSKQKEAEEEMLRKQKEMQELERQ--- 2572
Cdd:pfam12128 487 verlqsELRQARKRRDQASEALRQASRRLEERQSALDELelqlfpqagtllhfLRKEAPDWEQSIGKVISPELLHRTdld 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 2573 -----------------RLEQERILAEE----NQKLREKLQQLEDAQKDQHTR 2604
Cdd:pfam12128 567 pevwdgsvggelnlygvKLDLKRIDVPEwaasEEELRERLDKAEEALQSAREK 619
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1704-1807 |
1.48e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.94 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1704 ESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEmdiLIQLKTKAEKETMSN 1783
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQ---LEQLQEKAAETSQER 214
|
90 100
....*....|....*....|....
gi 1988774682 1784 TEKSKQLLEaEAAKMKDLAEEASR 1807
Cdd:PRK11448 215 KQKRKEITD-QAAKRLELSEEETR 237
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1497-1626 |
1.48e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 43.82 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1497 EAEKLRKQVSEETQK--KRQAEEELKR-KSEAEKEAakqkqkaleDLEKLRMQA--EEAERQVKQAEIEKEkqikvAHEA 1571
Cdd:cd03406 172 EAEKTKLLIAEQHQKvvEKEAETERKRaVIEAEKDA---------EVAKIQMQQkiMEKEAEKKISEIEDE-----MHLA 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774682 1572 AQKSAAAelqskhmsfAEKTSKleesLKQEHGAVLQLQQEAERLKKQQEDAENSR 1626
Cdd:cd03406 238 REKARAD---------AEYYRA----LREAEANKLKLTPEYLELKKYQAIANNTK 279
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3798-3831 |
1.51e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.51e-03
10 20 30
....*....|....*....|....*....|....
gi 1988774682 3798 LEAQTATGGIIDPEFQFHLPTDVAMQRGYINKET 3831
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2232-2385 |
1.55e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2232 ELLKLKNKIEEENQRlikkdkdstQKLLAEEAENmrklaedaarLSVEAQEAARlrqiaeddlnqqrALAEkmlkekmqA 2311
Cdd:PTZ00491 684 ERQKMHDKAKAEEQR---------TKLLELQAES----------AAVESSGQSR-------------AEAL--------A 723
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774682 2312 IQEASRLKAEAEMLQKQkdlAQEQAQKLLEDKQLMQQRLEEETE-EYHKS---LEVERKRQLEiMAEAERLRLQVSQL 2385
Cdd:PTZ00491 724 EAEARLIEAEAEVEQAE---LRAKALRIEAEAELEKLRKRQELElEYEQAqneLEIAKAKELA-DIEATKFERIVEAL 797
|
|
| Mcm10 |
pfam09332 |
Mcm10 replication factor; Mcm10 is a eukaryotic DNA replication factor that regulates the ... |
1485-1599 |
1.61e-03 |
|
Mcm10 replication factor; Mcm10 is a eukaryotic DNA replication factor that regulates the stability and chromatin association of DNA polymerase alpha.
Pssm-ID: 462760 Cd Length: 349 Bit Score: 43.98 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1485 AEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQ 1564
Cdd:pfam09332 133 AEAAKLAAIAKLKAKGGVLEKEDPNAVKRKRSDSGEIKERVEKNLESSSSSSPDEEEPALKKRREQLAYLKSEEFQKILN 212
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774682 1565 IKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLK 1599
Cdd:pfam09332 213 AKSKHTGELKEAEAEMQERYFEPLVKKEQMEEKMR 247
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1681-2025 |
1.61e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.47 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1681 AEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQ---QQRKQLED 1757
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREerrQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1758 ELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEAS---RLRAISEEAKHQ--RQIAE--EEAARQR 1830
Cdd:pfam02029 84 ERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEEteiREKEYQENKWSTevRQAEEegEEEEDKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1831 AEAERILKE-------KLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKS 1903
Cdd:pfam02029 164 EEAEEVPTEnfakeevKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1904 SEAEMERQKaivddtLKQRRVVEEEirilkLNFEKASSGKLDLELELNKLKNIADEtqQSKIRAEEEaeklrklaleeek 1983
Cdd:pfam02029 244 LEAEQKLEE------LRRRRQEKES-----EEFEKLRQKQQEAELELEELKKKREE--RRKLLEEEE------------- 297
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1988774682 1984 RRREAEEKVKKIaaAEEEAARQRKaalEELERLRKKAEEARK 2025
Cdd:pfam02029 298 QRRKQEEAERKL--REEEEKRRMK---EEIERRRAEAAEKRQ 334
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1346-1644 |
1.62e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.85 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1346 LDDEEKAAEKLKAEERKKMAEMQAELDK-QKQLAEAHAKAIAKAEKEAQELKLKMQEEvskreiaaVDAEKQKTNIQLEL 1424
Cdd:PLN03229 413 VDPERKVNMKKREAVKTPVRELEGEVEKlKEQILKAKESSSKPSELALNEMIEKLKKE--------IDLEYTEAVIAMGL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1425 QE-LKNLSEQQIKDKSQqvDEALHSRTKIEEEIRLIRIQLETTEKQKYTAeseLKQLRDRAAEAEKLRKLAQ--DEAEKL 1501
Cdd:PLN03229 485 QErLENLREEFSKANSQ--DQLMHPVLMEKIEKLKDEFNKRLSRAPNYLS---LKYKLDMLNEFSRAKALSEkkSKAEKL 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1502 RKQVSEETqKKRQAEEELKRKSEAEK-EAAKQKQKALEDLEKlrMQAEEAERQVKQAEIEKEKQIKVAH----EAAQKSA 1576
Cdd:PLN03229 560 KAEINKKF-KEVMDRPEIKEKMEALKaEVASSGASSGDELDD--DLKEKVEKMKKEIELELAGVLKSMGleviGVTKKNK 636
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 1577 AAELQSKHMSFAEKTSKLEESLKQEHGAVLQ---LQQEAERLKKQQEDAENSREEAEKE-LEKWRQKANEAL 1644
Cdd:PLN03229 637 DTAEQTPPPNLQEKIESLNEEINKKIERVIRssdLKSKIELLKLEVAKASKTPDVTEKEkIEALEQQIKQKI 708
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2150-2314 |
1.68e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2150 LMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQ 2229
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2230 MEELLKLKNKIEEENQRLIKKDKDSTQKLlaEEAENMRK---LAEDAARLSVEAQE--AARLRQIAEDDLNQQRALAEKM 2304
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNEL--YRVAGLTPeqaRKLLLKLLDAELEEekAQRVKKIEEEADLEAERKAQNI 181
|
170
....*....|
gi 1988774682 2305 LKEKMQAIQE 2314
Cdd:PRK12705 182 LAQAMQRIAS 191
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
2105-2273 |
1.74e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 44.75 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2105 EEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQ-KQQADTEMAKHKKLAEQT---LKQKFQVEQE 2180
Cdd:COG1193 521 EELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKaREEAEEILREARKEAEELireLREAQAEEEE 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2181 LTKVKLKLDETDKQksvLDEELQRLKD-----------EVDDAVK-----QRGQVEEE-----------LFKVKVQMEEL 2233
Cdd:COG1193 601 LKEARKKLEELKQE---LEEKLEKPKKkakpakppeelKVGDRVRvlslgQKGEVLEIpkggeaevqvgILKMTVKLSDL 677
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1988774682 2234 LKLKNKIEEENQRLIKKDKDSTQKLLAEEAE-NMR-KLAEDA 2273
Cdd:COG1193 678 EKVEKKKPKKPKKRPAGVSVSVSKASTVSPElDLRgMRVEEA 719
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1401-1558 |
1.76e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1401 EEVSKREIAAVDAEKQKTNIQLELQELKNLS--EQQIKDKSQQVDEalhsrtkIEEEIRLIRIQLETTEKQKYTAESELK 1478
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHEERELTeeEEEIRRLEEQVER-------LEAEVEELEAELEEKDERIERLERELS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1479 QLRDRA-AEAEKLRKLA--QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQA-EEAERQV 1554
Cdd:COG2433 452 EARSEErREIRKDREISrlDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEAiRRLEEEY 531
|
....
gi 1988774682 1555 KQAE 1558
Cdd:COG2433 532 GLKE 535
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3350-3388 |
1.76e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.85 E-value: 1.76e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1988774682 3350 YLQGSSSIAGLYLEPTKEKLSIYQAMKKKLLRHNTGLSL 3388
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1399-1652 |
1.81e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1399 MQEEVSKREIAAVDAEKQKTniqleLQELKNLSEQQIKDKSQQVD-----EALHSRTKIEEEIRLIRiQLETTEKqkyTA 1473
Cdd:PRK05771 2 APVRMKKVLIVTLKSYKDEV-----LEALHELGVVHIEDLKEELSnerlrKLRSLLTKLSEALDKLR-SYLPKLN---PL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1474 ESELKQLRDRaaEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKsEAEKEAAKqKQKALE-DLEKLRM------- 1545
Cdd:PRK05771 73 REEKKKVSVK--SLEELIKDVEEELEKIEKEIKELEEEISELENEIKEL-EQEIERLE-PWGNFDlDLSLLLGfkyvsvf 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1546 -------QAEEAERQVKQAEIEKEKQIK-------VAHEAAQKSAAAELQSkhMSFAEKTSKLEESLKQehgAVLQLQQE 1611
Cdd:PRK05771 149 vgtvpedKLEELKLESDVENVEYISTDKgyvyvvvVVLKELSDEVEEELKK--LGFERLELEEEGTPSE---LIREIKEE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1988774682 1612 AERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAED 1652
Cdd:PRK05771 224 LEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAE 264
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
1482-1566 |
1.88e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 43.71 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1482 DRAAEAEKLRKLAQDEAEKLRKQVSEETQKkrQAEEElkrKSEAEKEAAKQKQKALEDLEKLRMQAEEaerQVKQAEIEK 1561
Cdd:pfam07946 246 DKLAKRAKLRPEALKKAKKTREEEIEKIKK--AAEEE---RAEEAQEKKEEAKKKEREEKLAKLSPEE---QRKYEEKER 317
|
....*
gi 1988774682 1562 EKQIK 1566
Cdd:pfam07946 318 KKEQR 322
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2502-2583 |
1.91e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 41.06 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2502 IEDEKKRLES---QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEM--LRKQKEMQELERQRLEQ 2576
Cdd:pfam20492 4 AEREKQELEErlkQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKerLEESAEMEAEEKEQLEA 83
|
....*..
gi 1988774682 2577 ERILAEE 2583
Cdd:pfam20492 84 ELAEAQE 90
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
1481-1558 |
1.99e-03 |
|
Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.
Pssm-ID: 459956 [Multi-domain] Cd Length: 136 Bit Score: 41.56 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1481 RDRAAEAEKLRKLA---QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALedLEKLRMQAEEAERQVKQA 1557
Cdd:pfam00836 57 RRKSLEAQKLKQLAekrEKEEEALQKADEENNNFSKMAEEKLKQKMEAYKENREAQIAAL--KEKLKEKEKHVEEVRKNK 134
|
.
gi 1988774682 1558 E 1558
Cdd:pfam00836 135 E 135
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
524-618 |
2.03e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.39 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 524 LRYVQDLLAWVEENQRRIDNAEWGSDLPSMESQLGSHRGLHQTVEDFKSKIERAKADETQL---SPVSKGTYREYLGKLD 600
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1988774682 601 LQYGKLLNSSKSRLRNLE 618
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1693-1913 |
2.04e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1693 EEELERQRKIAESTAQQKLTAEQELI-RLRADfdNAEQQRslLEDELYRLKNEVAAAQQQRKQLEDElaKVRSEMDILIQ 1771
Cdd:pfam15709 310 ESEEERSEEDPSKALLEKREQEKASRdRLRAE--RAEMRR--LEVERKRREQEEQRRLQQEQLERAE--KMREELELEQQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1772 LKTKAEKETMSNTEKSKQLLEAEAAKmKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKlaaiseatRLK 1851
Cdd:pfam15709 384 RRFEEIRLRKQRLEEERQRQEEEERK-QRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEK--------QRQ 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774682 1852 TEAEIALKEkeaENERLRRQAEDE--AYQRKaledqasqhKQEIEEKIVQlkkssEAEMERQKA 1913
Cdd:pfam15709 455 KELEMQLAE---EQKRLMEMAEEErlEYQRQ---------KQEAEEKARL-----EAEERRQKE 501
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1595-1829 |
2.05e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1595 EESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQaedeahkktlaqeeaekqkeeaere 1674
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQ------------------------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1675 akkraKAEESALKQkemaeEELERQRKIAESTAQQKLTAEQELIRLRAdfdnAEQQRSLLEDELYRlkneVAAAQQQRKQ 1754
Cdd:pfam15709 395 -----RLEEERQRQ-----EEEERKQRLQLQAAQERARQQQEEFRRKL----QELQRKKQQEEAER----AEAEKQRQKE 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774682 1755 LEDELA---KVRSEMDILIQLKTKAEKEtmsnTEKSKQLLEAEAAKMKdlAEEASRLraISEEAKHQRQiaeeEAARQ 1829
Cdd:pfam15709 457 LEMQLAeeqKRLMEMAEEERLEYQRQKQ----EAEEKARLEAEERRQK--EEEAARL--ALEEAMKQAQ----EQARQ 522
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1600-1863 |
2.09e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1600 QEHGAVLQLQQEAER--LKKQQEDAENSREEAEKELEKWRQKANEAlrlRLQAEDEAHKKtlaqeeaekqkeeaerEAKK 1677
Cdd:PRK05035 433 QAKAEIRAIEQEKKKaeEAKARFEARQARLEREKAAREARHKKAAE---ARAAKDKDAVA----------------AALA 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1678 RAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQ----RK 1753
Cdd:PRK05035 494 RVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAAnaeaEE 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1754 QLEDELAKVRSEMdiliqLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEA-SRLRAISEEAKHQRQIAEEEAARQRAE 1832
Cdd:PRK05035 574 EVDPKKAAVAAAI-----ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKAAV 648
|
250 260 270
....*....|....*....|....*....|.
gi 1988774682 1833 AERILKEKlAAISEATRLKTEAEIALKEKEA 1863
Cdd:PRK05035 649 AAAIARAK-ARKAAQQQANAEPEEAEDPKKA 678
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
45-147 |
2.11e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 41.13 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 45 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21337 20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
|
90 100
....*....|....*....|....*..
gi 1988774682 121 NIRNDDIADGNPKLTLGLIWTIILHFQ 147
Cdd:cd21337 100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2430-2607 |
2.15e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2430 ERLNTSKEADDLRKAIADLEN-----EKARLKKEA-EELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIE 2503
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealEDAREQIELlEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2504 DEkkrlesqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEA-EEEMLRKQKEMQELERQRLEQER---- 2578
Cdd:COG4913 299 EL--------RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEAllaa 370
|
170 180 190
....*....|....*....|....*....|....*....
gi 1988774682 2579 ----------ILAEENQKLREKLQQLEDAQKDQHTRETD 2607
Cdd:COG4913 371 lglplpasaeEFAALRAEAAALLEALEEELEALEEALAE 409
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
32-140 |
2.26e-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: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 32 LKAMDGRKDERDRVqkktFTKWVNKHLIKAQrhVTDLYEDLRDGHNLISLLEVLSGE---TLPREKGR-------MRFHK 101
Cdd:COG5069 370 IEEFDAEGEFEARV----FTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKA 443
|
90 100 110
....*....|....*....|....*....|....*....
gi 1988774682 102 LQNVQIALDFLRHRQVKLVNIRNDDIADGNpKLTLGLIW 140
Cdd:COG5069 444 FENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVW 481
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
1801-1899 |
2.29e-03 |
|
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex
Pssm-ID: 339878 [Multi-domain] Cd Length: 104 Bit Score: 40.50 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1801 LAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKE---KLAAISEATRLKTEAEIALKEKEAenerlRRQAEDEAy 1877
Cdd:pfam16999 7 LSELAEREAALDQQIEAARKEAEREVEAAEAEAARILREaeaKAKALQAEYRQELAAETARIREEA-----RARAEAEA- 80
|
90 100
....*....|....*....|..
gi 1988774682 1878 qrKALEDQASQHKQEIEEKIVQ 1899
Cdd:pfam16999 81 --QAVRTRAEGRLQQAVELILR 100
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2134-2453 |
2.30e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.90 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2134 EAEFEAAKRAQAEAAALMQKQQADTE-----MAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDE 2208
Cdd:pfam19220 82 EGELEELVARLAKLEAALREAEAAKEelrieLRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2209 VDDAVKQRGQVEEELFKVKVQMEE----LLKLKNKIEEENQRLikkdkdstqkllaeeAENMRKLAEDAARLSVEAQEAA 2284
Cdd:pfam19220 162 LATARERLALLEQENRRLQALSEEqaaeLAELTRRLAELETQL---------------DATRARLRALEGQLAAEQAERE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2285 RLRQIAEDDLNQQRAlAEKMLKEKMQAIQE----ASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEyhks 2360
Cdd:pfam19220 227 RAEAQLEEAVEAHRA-ERASLRMKLEALTAraaaTEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAG---- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2361 LEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLhETEIATQEKMTVVERLEFERLNtskeadd 2440
Cdd:pfam19220 302 LEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASL-SDRIAELTKRFEVERAALEQAN------- 373
|
330
....*....|...
gi 1988774682 2441 lRKAIADLENEKA 2453
Cdd:pfam19220 374 -RRLKEELQRERA 385
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2320-2558 |
2.37e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2320 AEAEMLQKQKDL--AQEQAQKLLEDKQLMQQRLEEETEEYhKSLEVERKrqlEIMAEAERLRLQVSQLSeaqaraeeeaK 2397
Cdd:COG3883 14 ADPQIQAKQKELseLQAELEAAQAELDALQAELEELNEEY-NELQAELE---ALQAEIDKLQAEIAEAE----------A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2398 KFKKQADKVATRLHeteiATQEKMTVVERLEFerLNTSKEADDLRKAIADLENEKARLKKEAEELQnkskemadAQQKKI 2477
Cdd:COG3883 80 EIEERREELGERAR----ALYRSGGSVSYLDV--LLGSESFSDFLDRLSALSKIADADADLLEELK--------ADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2478 EHEKTVLQQtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEE 2557
Cdd:COG3883 146 EAKKAELEA----KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
.
gi 1988774682 2558 E 2558
Cdd:COG3883 222 A 222
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1392-1685 |
2.37e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1392 AQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKY 1471
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1472 TAESELKQLRDRAAEAEKLRKLAqdEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAE 1551
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAKEA--EAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1552 RQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEK 1631
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1988774682 1632 ELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESA 1685
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAA 293
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1589-1701 |
2.46e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1589 EKTSKLEESLKQEHGAVLQLQQEAERLKKQQED-AENSREEAEKELEKWRQKANEALRlrlQAEDEAHK--KTLAQEEAE 1665
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEkKEKLQEEEDKLLEEAEKEAQQAIK---EAKKEADEiiKELRQLQKG 599
|
90 100 110
....*....|....*....|....*....|....*.
gi 1988774682 1666 KQKEEAEREAKKRAKAEESALKQKEMAEEELERQRK 1701
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4273-4306 |
2.48e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.48e-03
10 20 30
....*....|....*....|....*....|....
gi 1988774682 4273 EETGPVAGILDIDTLEKVSVTEAIHRNLVDNITG 4306
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
183-260 |
2.55e-03 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 39.98 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 183 DNFTTSWRDGKLFNAVIHK------HYPRLInmgkvyQQTNLENLEQAFSvAEKDLGVTRLLDPEDVDVPHPDEKSIITY 256
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNAlggsvpGWPNLD------PEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAY 92
|
....
gi 1988774682 257 VSSL 260
Cdd:cd21185 93 AAQL 96
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
41-149 |
2.64e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 40.74 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 41 ERDRVQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 111
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1988774682 112 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1511-1601 |
2.68e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.88 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1511 KKRQA--EEELKRKSEAEKEAAKQKQKALEDLEKLRmqaEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFA 1588
Cdd:cd06503 29 DEREEkiAESLEEAEKAKEEAEELLAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIE 105
|
90
....*....|...
gi 1988774682 1589 EKTSKLEESLKQE 1601
Cdd:cd06503 106 QEKEKALAELRKE 118
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
2199-2354 |
2.70e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 44.21 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2199 DEELQRLKDEVDDAVkQRGQVEEELFKvkvQMEELlklknkieeenqrlikkdKDSTQKLLAEEAENMRKLAEDAARLSV 2278
Cdd:pfam13779 488 ERRLRAAQERLSEAL-ERGASDEEIAK---LMQEL------------------REALDDYMQALAEQAQQNPQDLQQPDD 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2279 EAQEAAR-------LRQIAEDDLNQQRALAEKMLKEkMQAIQEasRLKAeAEMlQKQKDLAQEQAQKLLEDKQLM---QQ 2348
Cdd:pfam13779 546 PNAQEMTqqdlqrmLDRIEELARSGRRAEAQQMLSQ-LQQMLE--NLQA-GQP-QQQQQQGQSEMQQAMDELGDLlreQQ 620
|
....*.
gi 1988774682 2349 RLEEET 2354
Cdd:pfam13779 621 QLLDET 626
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1371-1543 |
2.75e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1371 LDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNiqLELQELKNLSEQQIKDKSQQVDEAlhsrt 1450
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEAR--REREELQREEERLVQKEEQLDARA----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1451 kieEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEaeKLRKLAQDEAEKLRKQVSEETQKKrqAEEELKrkseaeKEAA 1530
Cdd:PRK12705 98 ---EKLDNLENQLEEREKALSARELELEELEKQLDN--ELYRVAGLTPEQARKLLLKLLDAE--LEEEKA------QRVK 164
|
170
....*....|...
gi 1988774682 1531 KQKQKALEDLEKL 1543
Cdd:PRK12705 165 KIEEEADLEAERK 177
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2171-2630 |
2.76e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2171 LKQKFQVEQ-ELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFkvkvQMEELLKLKNKIEEEnqrliK 2249
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN----ELSSLEDMKNRYESE-----I 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2250 KDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQK 2329
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2330 DlAQEQAQKLLEDkqLMQQRLEEETEE-----YHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKK--- 2401
Cdd:PRK01156 339 N-DYIKKKSRYDD--LNNQILELEGYEmdynsYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNein 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2402 -------------QADKVATRLHETEIatQEKMTVVE-RLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSK 2467
Cdd:PRK01156 416 vklqdisskvsslNQRIRALRENLDEL--SRNMEMLNgQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2468 EMAD--AQQKKIEH-------EKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQK------- 2531
Cdd:PRK01156 494 DIDEkiVDLKKRKEyleseeiNKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKrtswlna 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2532 --QQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHT-RETDK 2608
Cdd:PRK01156 574 laVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKlRGKID 653
|
490 500
....*....|....*....|..
gi 1988774682 2609 VLHKDIIHLTTIETTKTVYNGQ 2630
Cdd:PRK01156 654 NYKKQIAEIDSIIPDLKEITSR 675
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1559-1876 |
2.78e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.07 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1559 IEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEhgAVLQLQQEAERLKKQ--------------QEDAEN 1624
Cdd:PLN03229 413 VDPERKVNMKKREAVKTPVRELEGEVEKLKEQILKAKESSSKP--SELALNEMIEKLKKEidleyteaviamglQERLEN 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1625 SREEAEKELEKwRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEeSALKQKEMAEE-ELERQRKIA 1703
Cdd:PLN03229 491 LREEFSKANSQ-DQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAK-ALSEKKSKAEKlKAEINKKFK 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1704 ESTAQQKLTAEQELIRlradfDNAEQQRSLLEDELYR-LKNEVAAAqqqRKQLEDELAKVRSEMDILIQLKTKAEKETMS 1782
Cdd:PLN03229 569 EVMDRPEIKEKMEALK-----AEVASSGASSGDELDDdLKEKVEKM---KKEIELELAGVLKSMGLEVIGVTKKNKDTAE 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1783 NT------EKSKQLLEAEAAKMKDLAeEASRLRAISEEAKhqRQIAEEEAARQRAEAERI------LKEKLAAISEATRL 1850
Cdd:PLN03229 641 QTpppnlqEKIESLNEEINKKIERVI-RSSDLKSKIELLK--LEVAKASKTPDVTEKEKIealeqqIKQKIAEALNSSEL 717
|
330 340 350
....*....|....*....|....*....|...
gi 1988774682 1851 KT-----EAEIALKEK--EAENERLRRQAEDEA 1876
Cdd:PLN03229 718 KEkfeelEAELAAAREtaAESNGSLKNDDDKEE 750
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2192-2377 |
2.91e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2192 DKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKL--KNKIEEENQRLIKKdkdstQKLLAEEAenmRKL 2269
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAqeQKKQAEEAAKQAAL-----KQKQAEEA---AAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2270 AEDAARLSVEAQE---AARLRQIAEDDLNQQRALAEKMLKEKMQAIQEA-SRLKAEAEMLQKQKDLAQEQAQKLLEDKQL 2345
Cdd:PRK09510 141 AAAAAKAKAEAEAkraAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAeAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|..
gi 1988774682 2346 MQQRLEEETEEYHKSLEVERKRQLEIMAEAER 2377
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| SH3_Eps8 |
cd11764 |
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ... |
820-855 |
2.91e-03 |
|
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar proteins; This group is composed of Eps8 and Eps8-like proteins including Eps8-like 1-3, among others. These proteins contain N-terminal Phosphotyrosine-binding (PTB), central SH3, and C-terminal effector domains. Eps8 binds either Abi1 (also called E3b1) or Rab5 GTPase activating protein RN-tre through its SH3 domain. With Abi1 and Sos1, it becomes part of a trimeric complex that is required to activate Rac. Together with RN-tre, it inhibits the internalization of EGFR. The SH3 domains of Eps8 and similar proteins recognize peptides containing a PxxDY motif, instead of the classical PxxP motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212698 [Multi-domain] Cd Length: 54 Bit Score: 38.78 E-value: 2.91e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1988774682 820 QEITVHKGDECALLNNSQPFkWKVLNRSGHEAMVPS 855
Cdd:cd11764 14 KELSVLKGEYLEVLDDSRQW-WKVRNSRGQVGYVPH 48
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2126-2338 |
2.96e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2126 EDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRL 2205
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2206 KdevdDAVKQRGQVEEELFKVK----VQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAEnmrkLAEDAARLSVEAQ 2281
Cdd:COG4942 110 L----RALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE----LEAERAELEALLA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774682 2282 EAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQK 2338
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2428-2610 |
3.08e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2428 EFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKskeMADAQQKKI-----EHEKTVLQQTFMTEKEMLLKKEKLI 2502
Cdd:COG3206 160 AYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAA---LEEFRQKNGlvdlsEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2503 EDEKKR--LESQFEEEVKKAKALKdeQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERIL 2580
Cdd:COG3206 237 EAEARLaaLRAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
|
170 180 190
....*....|....*....|....*....|
gi 1988774682 2581 AEENQKLREKLQQLEDAQKDQHTRETDKVL 2610
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLA 344
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
1433-1544 |
3.08e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.
Pssm-ID: 214019 [Multi-domain] Cd Length: 161 Bit Score: 41.61 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1433 QQIKDKSQQVDEALHSRTKIEEEIRL-----------IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQdeAEKL 1501
Cdd:cd12926 15 QQYQDKSREYDQLYEEYTRTSQELQMkrtaieafnetIKIFEEQGQTQEKCSKEYLERFRREGNEKEMQRILLN--SERL 92
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1988774682 1502 RKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLR 1544
Cdd:cd12926 93 KSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKPDLMQLR 135
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2160-2543 |
3.10e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2160 MAKHKKLAEQtlkqkfqvEQELTKVKLKLDETDKQKSVLDEELQRLKDE---VDDAVKQRGQVEEelfkvkvQMEELLKL 2236
Cdd:COG3096 295 FGARRQLAEE--------QYRLVEMARELEELSARESDLEQDYQAASDHlnlVQTALRQQEKIER-------YQEDLEEL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2237 KNKIEEenqrlikkdkdstQKLLAEEAENMRKLAEDAARLSVEaqEAARLR-QIAED----DLNQQRALAekmLKEKMQA 2311
Cdd:COG3096 360 TERLEE-------------QEEVVEEAAEQLAEAEARLEAAEE--EVDSLKsQLADYqqalDVQQTRAIQ---YQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2312 IQEASRLKAEAEMLQKQKDLAQEQAQKllEDKQLMQQRLEEET---------EEYHKSL--------EVER----KRQLE 2370
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRA--KEQQATEEVLELEQklsvadaarRQFEKAYelvckiagEVERsqawQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2371 IMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADkvATRLHEtEIATQEKMTVVERLEFERLNTSKEA--DDLRKAIADL 2448
Cdd:COG3096 500 LLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQN--AERLLE-EFCQRIGQQLDAAEELEELLAELEAqlEELEEQAAEA 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2449 ENEKARLKKEAEELQNKSKEMAD------AQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKrlesqfeeevkkAKA 2522
Cdd:COG3096 577 VEQRSELRQQLEQLRARIKELAArapawlAAQDALERLREQSGEALADSQEVTAAMQQLLERERE------------ATV 644
|
410 420
....*....|....*....|.
gi 1988774682 2523 LKDEQERQKQQMEQEKKTLQA 2543
Cdd:COG3096 645 ERDELAARKQALESQIERLSQ 665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2011-2601 |
3.22e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2011 EELERLRKKAEEARKQKDeadkeaekQIVVAQQAAQKCSAAEQQVQsvLAQQIEDSITQKKLKEEYEkakklakeaeaak 2090
Cdd:COG4913 235 DDLERAHEALEDAREQIE--------LLEPIRELAERYAAARERLA--ELEYLRAALRLWFAQRRLE------------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2091 ekaereaaLLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALmQKQQADTEmakhKKLAEQT 2170
Cdd:COG4913 292 --------LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL-EREIERLE----RELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2171 LKQKfQVEQELTKVKLKLDETDKQksvLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLikk 2250
Cdd:COG4913 359 RRRA-RLEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL--- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2251 dkDSTQKLLAEEAENMRKLAEDAARLS-VEAQEAARLRQIAEDDLNQQRAlAEKML--------------KEKMQAIqEA 2315
Cdd:COG4913 432 --ERRKSNIPARLLALRDALAEALGLDeAELPFVGELIEVRPEEERWRGA-IERVLggfaltllvppehyAAALRWV-NR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2316 SRLKAEAEMLQKQKDLAQEQAQKLLED-----------------KQLMQQRL-------EEETEEYHKSLEVER------ 2365
Cdd:COG4913 508 LHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawlEAELGRRFdyvcvdsPEELRRHPRAITRAGqvkgng 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2366 ---------------------KRQLEIM-AEAERLRLQVSQLSEAQARAEEEAKKFKKQAD--KVATRLHETEIATQEKM 2421
Cdd:COG4913 588 trhekddrrrirsryvlgfdnRAKLAALeAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2422 TVVERLEFERLNTSKEADDLRKA---IADLENEKARLKKEAEELQNK----SKEMADAQQkKIEHEKTVLQQtfMTEKEM 2494
Cdd:COG4913 668 REIAELEAELERLDASSDDLAALeeqLEELEAELEELEEELDELKGEigrlEKELEQAEE-ELDELQDRLEA--AEDLAR 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2495 LLKKEKLieDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELER--Q 2572
Cdd:COG4913 745 LELRALL--EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLAllD 822
|
650 660
....*....|....*....|....*....
gi 1988774682 2573 RLEQERiLAEENQKLREKLQQLEDAQKDQ 2601
Cdd:COG4913 823 RLEEDG-LPEYEERFKELLNENSIEFVAD 850
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1609-1837 |
3.31e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1609 QQEAERLKKQQEDAENSREEAE----KELEKWRQKANEAlrlRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 1684
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEqerlKQLEKERLAAQEQ---KKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1685 ALkqKEMAEEELERQRKIAESTAQQKLTAEQelirlradfdnaeqqrslledelyRLKNEVAAAQQQrkqleDELAKVRS 1764
Cdd:PRK09510 155 RA--AAAAKKAAAEAKKKAEAEAAKKAAAEA------------------------KKKAEAEAAAKA-----AAEAKKKA 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 1765 EMDIliqlKTKAEKEtmsntEKSKQLLEAEAAKMKDLAEEAsrlrAISEEAKHQRQIAEEEAARQRAEAERIL 1837
Cdd:PRK09510 204 EAEA----KKKAAAE-----AKKKAAAEAKAAAAKAAAEAK----AAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
1363-1596 |
3.38e-03 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 43.41 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1363 KMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIA---AVDAEKQKTNIQLELQELK----NLSEQQI 1435
Cdd:PRK15374 107 RLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKTDTAksvYDAAEKKLTQAQNKLQSLDpadpGYAQAEA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1436 KdKSQQVDEALHSRTKIEeeirliriqlettekQKYTAESelKQLRDRAAEAEKlrklAQDEAEKLRKQVSEETQkkrqa 1515
Cdd:PRK15374 187 A-VEQAGKEATEAKEALD---------------KATDATV--KAGTDAKAKAEK----ADNILTKFQGTANAASQ----- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1516 eeelkrkseaeKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLE 1595
Cdd:PRK15374 240 -----------NQVSQGEQDNLSNVARLTMLMAMFIEIVGKNTEESLQNDLALFNALQEGRQAEMEKKSAEFQEETRKAE 308
|
.
gi 1988774682 1596 E 1596
Cdd:PRK15374 309 E 309
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1966-2462 |
3.51e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1966 RAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEK--QIVVAQQ 2043
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2044 AAQKCSAAEQQVQSvLAQQIEdsitqkKLKEEYEKAKKLAKEAEAAKEKAEReaalLRQQAEEAERQKTaaEEEAANQAK 2123
Cdd:COG4717 130 LYQELEALEAELAE-LPERLE------ELEERLEELRELEEELEELEAELAE----LQEELEELLEQLS--LATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2124 AQEDAERLRKE-AEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEEL 2202
Cdd:COG4717 197 LAEELEELQQRlAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2203 QRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKL--KNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEA 2280
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALpaLEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2281 QEAARLRQIAEDDLNQQRALA------EKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLmqQRLEEET 2354
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2355 EEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEaqaraeeeakkfkkqadkvATRLHETEIATQEKMTVVERLEFERLNT 2434
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEE-------------------DGELAELLQELEELKAELRELAEEWAAL 495
|
490 500
....*....|....*....|....*....
gi 1988774682 2435 SKEADDLRKAIADLENEKA-RLKKEAEEL 2462
Cdd:COG4717 496 KLALELLEEAREEYREERLpPVLERASEY 524
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
2411-2531 |
3.55e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2411 HETEIATQEKMTVVERLEferlntsKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVlqQTFMT 2490
Cdd:COG2433 402 EHEERELTEEEEEIRRLE-------EQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREI--SRLDR 472
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1988774682 2491 EKEMLlkkEKLIEDEKKRLEsQFEEEVKKAKALKDEQERQK 2531
Cdd:COG2433 473 EIERL---ERELEEERERIE-ELKRKLERLKELWKLEHSGE 509
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1773-1875 |
3.56e-03 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 43.76 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1773 KTKaeKETMSNT-EKSKqLLEAEAAKMKDLAEE------------ASRLRAISEEAKHQRQIAEEEAARQRAEAE--RIL 1837
Cdd:pfam04147 162 KSK--KEVMEEViAKSK-LHKYERQKAKEEDEElreeldkelkdlRSLLSGSKRPKPEQAKKPEEKPDRKKPDDDydKLV 238
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1988774682 1838 KE----KLAAISEatRLKTEAEIALKEKE----AENERLRR-QAEDE 1875
Cdd:pfam04147 239 RElafdKRAKPSD--RTKTEEELAEEEKErlekLEEERLRRmRGEED 283
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1680-1847 |
3.58e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 42.66 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1680 KAEESALKQKEMAEEELerQRKIAESTAQQkltAEQELIRLRADfdnAEQQRSLLEDElyrlknevAAAQQQRKQLEDEL 1759
Cdd:pfam12037 46 KALELMKKQEQTRQAEL--QAKIKEYEAAQ---EQLKIERQRVE---YEERRKTLQEE--------TKQKQQRAQYQDEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1760 AKVRSEMDILIQLKTKAE-----------KETMSNTEKSKQLLEAEAakmkDLAEEASRLRAISE-EAK-HQRQIAEE-- 1824
Cdd:pfam12037 110 ARKRYQDQLEAQRRRNEEllrkqeesvakQEAMRIQAQRRQTEEHEA----ELRRETERAKAEAEaEARaKEERENEDln 185
|
170 180
....*....|....*....|....
gi 1988774682 1825 -EAARQRAEAERilKEKLAAISEA 1847
Cdd:pfam12037 186 lEQLREKANEER--ETVLESINTA 207
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1611-1887 |
3.68e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1611 EAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEahkktlaqeeaekqkeeaEREAKKRAKAEESALKQke 1690
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE------------------LEALQAEIDKLQAEIAE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1691 mAEEELERQRKIAESTAQQKLTAEQELIRLRA-----DFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSE 1765
Cdd:COG3883 77 -AEAEIEERREELGERARALYRSGGSVSYLDVllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1766 MDILIQLKTKAEKETmsnTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAIS 1845
Cdd:COG3883 156 LAELEALKAELEAAK---AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1988774682 1846 EATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQAS 1887
Cdd:COG3883 233 AAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1327-1633 |
3.69e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1327 ELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELdkqKQLAEAHAKAIAKaEKEAQELKLKMQEEvsKR 1406
Cdd:pfam07888 45 ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEEL---RQSREKHEELEEK-YKELSASSEELSEE--KD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1407 EIAAVDAEKQktniqlelQELKNLsEQQIKDKSQQVDEalhsrtkIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAE 1486
Cdd:pfam07888 119 ALLAQRAAHE--------ARIREL-EEDIKTLTQRVLE-------RETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1487 AEK-LRKLAQD-------------EAEKLRKQVSEETQKKRQAEeelkrKSEAEKEAAKQKQKALEDLEKLRMQAEEA-E 1551
Cdd:pfam07888 183 TEEeLRSLSKEfqelrnslaqrdtQVLQLQDTITTLTQKLTTAH-----RKEAENEALLEELRSLQERLNASERKVEGlG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1552 RQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSK---------LEESLKQEHGAVLQLQQEAERLKKQQEDA 1622
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRarwaqeretLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330
....*....|.
gi 1988774682 1623 ENSREEAEKEL 1633
Cdd:pfam07888 338 RMEREKLEVEL 348
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
2499-2599 |
3.92e-03 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 43.50 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2499 EKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLqATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQER 2578
Cdd:pfam14817 65 DKGKAESRQSAAARRLELQKEIERLRAEISRLDKQLEARELEL-SREEAERERALDEISDSRHRQLLLEAYDQQCEEARK 143
|
90 100
....*....|....*....|.
gi 1988774682 2579 ILAEENQKLREKLQQLEDAQK 2599
Cdd:pfam14817 144 ILAEDHQRLQGQLQQLRDAAR 164
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1323-1560 |
4.09e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.56 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1323 TRYSELMtltSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEahakaiaKAEKEAQELkLKMQEE 1402
Cdd:cd16269 44 AHYEEQM---EQRVQLPTETLQELLDLHAACEKEALEVFMKRSFKDEDQKFQKKLME-------QLEEKKEEF-CKQNEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1403 VSK-------REIAAVDAEKQKTNI-------QLELQELKNLSE--QQIKDKSQQVDEALH----SRTKIEEEIRLIRIQ 1462
Cdd:cd16269 113 ASSkrcqallQELSAPLEEKISQGSysvpggyQLYLEDREKLVEkyRQVPRKGVKAEEVLQeflqSKEAEAEAILQADQA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1463 LETTEKQKytaeselKQLRDRAAEAEKLRKLAQDEAEKLRKQVseETQKKRQAE--EELKRKSEAEKE-AAKQKQKALED 1539
Cdd:cd16269 193 LTEKEKEI-------EAERAKAEAAEQERKLLEEQQRELEQKL--EDQERSYEEhlRQLKEKMEEEREnLLKEQERALES 263
|
250 260
....*....|....*....|...
gi 1988774682 1540 L--EKLRMQAEEAERQVKQAEIE 1560
Cdd:cd16269 264 KlkEQEALLEEGFKEQAELLQEE 286
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1452-1542 |
4.33e-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: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1452 IEEEIRLIRIQLETTEKQKYTAESELKQLRDR----AAEAEKLRKLAQDEAEKLRKqvseetQKKRQAEEELKR-KSEAE 1526
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKlaeaRAEAAEIIAEARKEAEAIAE------EAKAEAEAEAERiIAQAE 102
|
90
....*....|....*.
gi 1988774682 1527 KEAAKQKQKALEDLEK 1542
Cdd:COG0711 103 AEIEQERAKALAELRA 118
|
|
| PRK01558 |
PRK01558 |
V-type ATP synthase subunit E; Provisional |
1488-1579 |
4.65e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 179302 Cd Length: 198 Bit Score: 41.67 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1488 EKLRKLAQDEAEKLRKQVSEETQKKRqaeEELKRKseAEKEAAKQKQKALEDLEKLRMQAEEAERQ-VKQAEIEKEKQIK 1566
Cdd:PRK01558 10 NKIKKDGLEEAERLANEIILEAKEEA---EEIIAK--AEEEAKELKAKAEKEANDYKRHALEASRQaGRDLLISFEKSIK 84
|
90
....*....|...
gi 1988774682 1567 VAHEAAQKSAAAE 1579
Cdd:PRK01558 85 SLFKAALKDEVAE 97
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
40-143 |
4.79e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 40.12 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 40 DERDRVQkktFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETL-------PREKGRM--RFHK 101
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIdervlnkPPRKNKPlnNFQM 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1988774682 102 LQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 143
Cdd:cd21294 81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1492-1910 |
4.82e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1492 KLAQDEAEKLRKQVS------EETQKkrQAEEELKRKSEAEKEAAKQKQKALEDLEKL------------RMQAEEAERQ 1553
Cdd:PRK10246 194 KSARTELEKLQAQASgvalltPEQVQ--SLTASLQVLTDEEKQLLTAQQQQQQSLNWLtrldelqqeasrRQQALQQALA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1554 VKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEK-- 1631
Cdd:PRK10246 272 AEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNtw 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1632 --ELEKWRQKANEALRLRL----QAEDEAHKKTLAQEEAEKQkeeaereaKKRAKAEESALkqkEMAEEELERQRkiAES 1705
Cdd:PRK10246 352 laEHDRFRQWNNELAGWRAqfsqQTSDREQLRQWQQQLTHAE--------QKLNALPAITL---TLTADEVAAAL--AQH 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1706 TAQQKLtaEQELIRLRAdfdnaeqQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEM----DILIQLKTKAEKE-T 1780
Cdd:PRK10246 419 AEQRPL--RQRLVALHG-------QIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYkektQQLADVKTICEQEaR 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1781 MSNTEKSKQLLEA---------------EAAKMKDLAEEASRLRAISEEAKhqrQIAEEEAA-------------RQRAE 1832
Cdd:PRK10246 490 IKDLEAQRAQLQAgqpcplcgstshpavEAYQALEPGVNQSRLDALEKEVK---KLGEEGAAlrgqldaltkqlqRDESE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1833 AERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAY-----QRKALEDQASQHKQEI---EEKIVQLKKSS 1904
Cdd:PRK10246 567 AQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQlrllsQRHELQGQIAAHNQQIiqyQQQIEQRQQQL 646
|
....*.
gi 1988774682 1905 EAEMER 1910
Cdd:PRK10246 647 LTALAG 652
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2153-2381 |
4.87e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2153 KQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFK-VKVQME 2231
Cdd:pfam13868 58 EEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREeIDEFNE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2232 ELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARlsvEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQA 2311
Cdd:pfam13868 138 EQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEE---KEREIARLRAQQEKAQDEKAERDELRAKLYQEE 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 2312 IQEASRLKAEAEMLQKQK---DLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQ 2381
Cdd:pfam13868 215 QERKERQKEREEAEKKARqrqELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMK 287
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
2425-2593 |
4.88e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.38 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2425 ERLEFERLN-TSKE------ADDLRkaiADLENEKARLKKEAEELQNKSK---EMADAQQKKIE-HEKTVLQQTFMTEKE 2493
Cdd:PLN03188 1047 KKLEQERLRwTEAEskwislAEELR---TELDASRALAEKQKHELDTEKRcaeELKEAMQMAMEgHARMLEQYADLEEKH 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2494 MLL-----KKEKLIEDEKKRL--------ESQFEEEVK-KAKALKDEQERQKQQMEQEKKTLQATM-DAA---------L 2549
Cdd:PLN03188 1124 IQLlarhrRIQEGIDDVKKAAaragvrgaESKFINALAaEISALKVEREKERRYLRDENKSLQAQLrDTAeavqaagelL 1203
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1988774682 2550 SKQKEAEEEMLRKQKEMQELERQrleqerilAEENQKLREKLQQ 2593
Cdd:PLN03188 1204 VRLKEAEEALTVAQKRAMDAEQE--------AAEAYKQIDKLKR 1239
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1799-1928 |
4.94e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1799 KDLAEEASRLRAISE-EAKHQRQIAEEEAARQRAEAErilKEKLAAISEATRLKTEAEIALK--EKEAENERLRRQAEDE 1875
Cdd:COG2268 191 RRKIAEIIRDARIAEaEAERETEIAIAQANREAEEAE---LEQEREIETARIAEAEAELAKKkaEERREAETARAEAEAA 267
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774682 1876 AYQRKALEDQASQHKQEIEEKIVQLK---KSSEAEMERQKAIVDDTLK-QRRVVEEE 1928
Cdd:COG2268 268 YEIAEANAEREVQRQLEIAEREREIElqeKEAEREEAELEADVRKPAEaEKQAAEAE 324
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
46-143 |
5.24e-03 |
|
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 39.82 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 46 QKKTFTKWVNKHL---------IKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 111
Cdd:cd21293 2 EKGSYVDHINRYLgddpflkqfLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1988774682 112 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 143
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2277-2556 |
5.59e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 43.28 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2277 SVEAQEAARLRQIAEDDLNQQRALAEKmlkekmqAIQEASRLKAEAEMLQKQKDLAQEQAQklLEDKQlmQQRLEEETEE 2356
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK-------ERAEADRQRLEQEKQQQLAAISGSQSQ--LESTD--QNALETNGQA 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2357 YHKSLEVERKrqlEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQ-----ADKVATRLHETEIATQEKMTVVERLEFER 2431
Cdd:NF012221 1607 QRDAILEESR---AVTKELTTLAQGLDALDSQATYAGESGDQWRNPfagglLDRVQEQLDDAKKISGKQLADAKQRHVDN 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2432 LNTSKEAddLRKAIADLENEKaRLKKEAEelQNKSKEMADAQQKKiehektvlqqtfmteKEMLLKKEkliedEKKRLES 2511
Cdd:NF012221 1684 QQKVKDA--VAKSEAGVAQGE-QNQANAE--QDIDDAKADAEKRK---------------DDALAKQN-----EAQQAES 1738
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1988774682 2512 QFEEEVKKAKalkdeQERQKQQMEQEKKTLQATMDAALSKQKEAE 2556
Cdd:NF012221 1739 DANAAANDAQ-----SRGEQDASAAENKANQAQADAKGAKQDESD 1778
|
|
| MRP-S27 |
pfam10037 |
Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins ... |
1686-1839 |
5.72e-03 |
|
Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins possess one of three conserved blocks of sequence found in proteins that stimulate the dissociation of guanine nucleotides from G-proteins, leaving open the possibility that MRP-S27 might be a functional partner of GTP-binding ribosomal proteins.
Pssm-ID: 462947 [Multi-domain] Cd Length: 395 Bit Score: 42.43 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1686 LKQKEMAEEELERQRKIAESTAQQKLTAE--QELIRLRADFDNAEqqrsllEDELYRLKNEVAAAQQQRKQLEdELAKVR 1763
Cdd:pfam10037 259 LGKVGYLDRALSVMEKVASSPGDLKLHKEvlDVLQDILETLDELE------ESEQSKLPEYVKSFQELLSKLQ-SLGKVE 331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774682 1764 SEmdILIQLKTKAEKETMSNTEKskQLLEAEAAKMKDLAEEasRLRAISEEAKHQrqiaeeEAARQRAEAERILKE 1839
Cdd:pfam10037 332 SE--SLLTLLENLVKESLPACEE--KDLANYEQLYQEWEEE--RRQLIQREKEMR------EKAEREDEARKALKE 395
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2235-2382 |
5.72e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.68 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2235 KLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQ---IAEDDLNQQRALAEKMLKEKMQA 2311
Cdd:pfam05262 181 KVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQkadFAQDNADKQRDEVRQKQQEAKNL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2312 ------------IQEASRLKAEAEMLQKQKDLAQEQAQKLLEDK--QLMQQRLEEETEEYHKSLEVERKRqLEIMAEAER 2377
Cdd:pfam05262 261 pkpadtsspkedKQVAENQKREIEKAQIEIKKNDEEALKAKDHKafDLKQESKASEKEAEDKELEAQKKR-EPVAEDLQK 339
|
....*
gi 1988774682 2378 LRLQV 2382
Cdd:pfam05262 340 TKPQV 344
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
1361-1529 |
5.73e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.41 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1361 RKKMAEmqaeldkqKQLAEAHAKA---IAKAEKEAQELK----LKMQEEVSKREiaaVDAEKQKTNIQLELQELKNL--- 1430
Cdd:pfam12072 21 RKSIAE--------AKIGSAEELAkriIEEAKKEAETKKkealLEAKEEIHKLR---AEAERELKERRNELQRQERRllq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1431 SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLEttEKQKYTAESELKQLrdraAEAEKLRKLAQDEAEK-LRKQVSEET 1509
Cdd:pfam12072 90 KEETLDRKDESLEKKEESLEKKEKELEAQQQQLE--EKEEELEELIEEQR----QELERISGLTSEEAKEiLLDEVEEEL 163
|
170 180
....*....|....*....|....*
gi 1988774682 1510 QKK-----RQAEEELKRksEAEKEA 1529
Cdd:pfam12072 164 RHEaavmiKEIEEEAKE--EADKKA 186
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1489-1716 |
5.74e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1489 KLRKLAQDEAEKlRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVA 1568
Cdd:PRK11637 48 QLKSIQQDIAAK-EKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1569 heaAQKSAAAELQSKHmsfaektSKLEESLKQEHGavlqlqQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLrL 1648
Cdd:PRK11637 127 ---AAQLDAAFRQGEH-------TGLQLILSGEES------QRGERILAYFGYLNQARQETIAELKQTREELAAQKAE-L 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774682 1649 QAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAE-ESALKQK-----EMAEEELERQRKIAESTAQQKLTAEQE 1716
Cdd:PRK11637 190 EEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGlESSLQKDqqqlsELRANESRLRDSIARAEREAKARAERE 263
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3682-3718 |
5.83e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.08 E-value: 5.83e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1988774682 3682 KQYLYGTGCVAGIT-TDSSSKLSIYQAMKRGFIKPEIG 3718
Cdd:smart00250 1 QRLLEAQSAIGGIIdPETGQKLSVEEALRRGLIDPETG 38
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1485-1564 |
5.95e-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: 40.11 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1485 AEAEKLRKlaqdEAEKLRKQVSEETQK-KRQAEEELKrksEAEKEAAKQKQKALEDLEklrmqaEEAERQVKQA--EIEK 1561
Cdd:cd06503 40 EEAEKAKE----EAEELLAEYEEKLAEaRAEAQEIIE---EARKEAEKIKEEILAEAK------EEAERILEQAkaEIEQ 106
|
...
gi 1988774682 1562 EKQ 1564
Cdd:cd06503 107 EKE 109
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1453-1560 |
6.04e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.41 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1453 EEEIRLIRIQLETTEKQKYTAESE----LKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE 1528
Cdd:pfam05672 17 AEKRRQAREQREREEQERLEKEEEerlrKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1988774682 1529 AAKQKQK------ALEDLEKLR------MQAEEAERQVKQAEIE 1560
Cdd:pfam05672 97 ERLQKQKeeaeakAREEAERQRqerekiMQQEEQERLERKKRIE 140
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1343-1611 |
6.05e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1343 QRRLDDEEKAAEKLKAEERKKMAEMQAELDK-----QKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQK 1417
Cdd:pfam15905 75 QKELEKEIRALVQERGEQDKRLQALEEELEKveaklNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQKKM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1418 TNIQLELQELKNLSEQQIKdksqqvdEALHSRTKIEeeirlirIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDE 1497
Cdd:pfam15905 155 SSLSMELMKLRNKLEAKMK-------EVMAKQEGME-------GKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1498 AEKLRKQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKALEDL--------EKLRMQAEEAERQVKQAEIEKEKQIKVAH 1569
Cdd:pfam15905 221 TEKLLEYITELSCVSEQV-EKYKLDIAQLEELLKEKNDEIESLkqsleekeQELSKQIKDLNEKCKLLESEKEELLREYE 299
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1988774682 1570 EAAQkSAAAELQSkhmsfaektskLEESLKQEHGAVLQLQQE 1611
Cdd:pfam15905 300 EKEQ-TLNAELEE-----------LKEKLTLEEQEHQKLQQK 329
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1677-1910 |
6.07e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 42.74 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1677 KRAKAEESALKQkemaeeELErqrkiaeSTAQQKLTAEQELIRLRADFDNAEQQ-RSLLEDELYRLKNEVAAAQQQ---- 1751
Cdd:pfam05911 20 EKAEAEALALKQ------QLE-------SVTLQKLTAEERAAHLDGALKECMQQlRNVKEEQEQKIHDVVLKKTKEweki 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1752 RKQLEDELAkvrsemdiliqlktkaeketmsntEKSKQLLEAEAakmkdlaeEASRL-RAISEEAKHQRQIAEEEAarqR 1830
Cdd:pfam05911 87 KAELEAKLV------------------------ETEQELLRAAA--------ENDALsRSLQERENLLMKLSEEKS---Q 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1831 AEAE-RILKEKLAAIS-EATRLKTEAEIALKEKEAENERL---RRQAEdeayqrkaledqaSQHKQEIE--EKIVQLkks 1903
Cdd:pfam05911 132 AEAEiEALKSRLESCEkEINSLKYELHVLSKELEIRNEEKnmsRRSAD-------------AAHKQHLEsvKKIAKL--- 195
|
....*..
gi 1988774682 1904 sEAEMER 1910
Cdd:pfam05911 196 -EAECQR 201
|
|
| iSH2_PIK3R1 |
cd12924 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
1433-1563 |
6.15e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 1, PIK3R1, also called p85alpha; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In addition, p85alpha, also called PIK3R1, contains N-terminal SH3 and GAP domains. p85alpha carry functions independent of its PI3K regulatory role. It can independently stimulate signaling pathways involved in cytoskeletal rearrangements. Insulin-sensitive tissues express splice variants of the PIK3R1 gene, p50alpha and p55alpha, which may play important roles in insulin signaling during lipid and glucose metabolism. Mice deficient with PIK3R1 die perinatally, indicating its importance in development.
Pssm-ID: 214017 [Multi-domain] Cd Length: 161 Bit Score: 40.45 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1433 QQIKDKSQQVDEALHSRTKIEEEIRLIRIQLET-TEKQKYTAESELKQLRDRAAEAEKLRKLAQDEA--------EKLRK 1503
Cdd:cd12924 15 TQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAfNETIKIFEEQCQTQERYSKEYIEKFKREGNEKEiqrimhnyEKLKS 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1504 QVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEK 1563
Cdd:cd12924 95 RISEIVDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKK 154
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2329-2593 |
6.26e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2329 KDLAQEQAQKLLEDKQLMQQRleeeteeyhKSLEVERKRQLEIMAEAER-LRLQVSQLSeaqaraeeeakKFKKQADKVA 2407
Cdd:PRK11637 50 KSIQQDIAAKEKSVRQQQQQR---------ASLLAQLKKQEEAISQASRkLRETQNTLN-----------QLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2408 TRLH--ETEIATQEKMTvverleferlntskeADDLRKAIADLENEKARLKKEAEELQNKSKEMA------DAQQKKIEH 2479
Cdd:PRK11637 110 ASIAklEQQQAAQERLL---------------AAQLDAAFRQGEHTGLQLILSGEESQRGERILAyfgylnQARQETIAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2480 ektvLQQTfmtekemllkKEKLIEdEKKRLESQFEEEvkkaKALKDEQERQKQQMEQ----EKKTLqATMDAALSKQKE- 2554
Cdd:PRK11637 175 ----LKQT----------REELAA-QKAELEEKQSQQ----KTLLYEQQAQQQKLEQarneRKKTL-TGLESSLQKDQQq 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1988774682 2555 -----AEEEMLRKQKEMQELE-RQRLEQErilAEENQKLREKLQQ 2593
Cdd:PRK11637 235 lselrANESRLRDSIARAEREaKARAERE---AREAARVRDKQKQ 276
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2489-2604 |
6.26e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.21 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2489 MTEKEMLLKKEKlieDEKKRLESQFEEEVKKAKALKDEQERQ-KQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQ 2567
Cdd:pfam13868 28 IAEKKRIKAEEK---EEERRLDEMMEEERERALEEEEEKEEErKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMD 104
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774682 2568 ELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTR 2604
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAE 141
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2229-2376 |
6.44e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2229 QMEELLKLKNKIEEENQRLIKKdKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEK 2308
Cdd:COG2268 193 KIAEIIRDARIAEAEAERETEI-AIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIA 271
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774682 2309 MQAIQEASRLKAEAEMLQKQKDLAQEQAQKlledkqlmqqRLEEETEEYHKSLEVERKRQlEIMAEAE 2376
Cdd:COG2268 272 EANAEREVQRQLEIAEREREIELQEKEAER----------EEAELEADVRKPAEAEKQAA-EAEAEAE 328
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
1728-1893 |
6.76e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 40.42 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1728 EQQRSLLEDELYRLKNEVAaaqqqRKQLEDELAKVRSEMDILIQLKTKAEKETMsntekskqlleaeaakMKDLAEEASR 1807
Cdd:pfam15346 2 EAESKLLEEETARRVEEAV-----AKRVEEELEKRKDEIEAEVERRVEEARKIM----------------EKQVLEELER 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1808 LRAISEEAKHQRqiaEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEaenerlrRQAEDEAYQRKALEDQAS 1887
Cdd:pfam15346 61 EREAELEEERRK---EEEERKKREELERILEENNRKIEEAQRKEAEERLAMLEEQ-------RRMKEERQRREKEEEERE 130
|
....*.
gi 1988774682 1888 QHKQEI 1893
Cdd:pfam15346 131 KREQQK 136
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2448-2605 |
6.81e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.79 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2448 LENEKARLKKEAEELQNKSKEMADAQQKKIE-----HEKTVLQQTFMTEKEMLLKKEKLIEDE--KKRLESQ--FEEEVK 2518
Cdd:cd16269 108 KQNEEASSKRCQALLQELSAPLEEKISQGSYsvpggYQLYLEDREKLVEKYRQVPRKGVKAEEvlQEFLQSKeaEAEAIL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2519 KAKALKDEQERQKQqmEQEKKTLQATMDAALSKQKEAEEEMLRKQ-----KEMQELERQRLEQER--ILAEENQKLREKL 2591
Cdd:cd16269 188 QADQALTEKEKEIE--AERAKAEAAEQERKLLEEQQRELEQKLEDqersyEEHLRQLKEKMEEERenLLKEQERALESKL 265
|
170
....*....|....
gi 1988774682 2592 QQLEDAQKDQHTRE 2605
Cdd:cd16269 266 KEQEALLEEGFKEQ 279
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1348-1471 |
6.96e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1348 DEEKAAEKLKAEE-RKKMAEMQAeldkQKQLAEAHAKAIAKAEKEAQELKLKMQEEVskrEIAAVDAEKQKTNIQLELQE 1426
Cdd:PTZ00491 684 ERQKMHDKAKAEEqRTKLLELQA----ESAAVESSGQSRAEALAEAEARLIEAEAEV---EQAELRAKALRIEAEAELEK 756
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1988774682 1427 LKNLSEQQIKdksqqvdealHSRTKIEEEIRLIRiQLETTEKQKY 1471
Cdd:PTZ00491 757 LRKRQELELE----------YEQAQNELEIAKAK-ELADIEATKF 790
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
2183-2515 |
7.05e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.53 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2183 KVKLKLDETDKQKSV-LDEELQRLKDEVDDAVKQRGQVEEELFKvkvqmEELLKLKNKIEEENQRLIKKdKDSTQKLLAE 2261
Cdd:PLN03229 418 KVNMKKREAVKTPVReLEGEVEKLKEQILKAKESSSKPSELALN-----EMIEKLKKEIDLEYTEAVIA-MGLQERLENL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2262 EAENMRKLAEDAARLSVEAQEAARLRQiaEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE 2341
Cdd:PLN03229 492 REEFSKANSQDQLMHPVLMEKIEKLKD--EFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKE 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2342 --DKQLMQQRLEEETEEYHKSleverkrqlEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQE 2419
Cdd:PLN03229 570 vmDRPEIKEKMEALKAEVASS---------GASSGDELDDDLKEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAE 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2420 KMTVVE-RLEFERLN--TSKEADDLRKAiADLENEKARLKKeaeELQNKSKEMADAQQKKIEHEKTVLQQTF---MTEKE 2493
Cdd:PLN03229 641 QTPPPNlQEKIESLNeeINKKIERVIRS-SDLKSKIELLKL---EVAKASKTPDVTEKEKIEALEQQIKQKIaeaLNSSE 716
|
330 340
....*....|....*....|..
gi 1988774682 2494 MLLKKEKLIEDEKKRLESQFEE 2515
Cdd:PLN03229 717 LKEKFEELEAELAAARETAAES 738
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2423-2528 |
7.09e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2423 VVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQN-KSKEMADAQQK--------KIEHEKTVLQQTFMTEKE 2493
Cdd:PRK00409 521 LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeEDKLLEEAEKEaqqaikeaKKEADEIIKELRQLQKGG 600
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774682 2494 MLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQE 2528
Cdd:PRK00409 601 YASVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1467-1554 |
7.16e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 39.99 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1467 EKQKYTAESElKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEElkrksEAEKEAAKQKQKALEDLEKlrmQ 1546
Cdd:PRK07353 54 EAEKLEAQYE-QQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQASKE-----KARREIEQQKQAALAQLEQ---Q 124
|
....*...
gi 1988774682 1547 AEEAERQV 1554
Cdd:PRK07353 125 VDALSRQI 132
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4279-4309 |
7.32e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.92 E-value: 7.32e-03
10 20 30
....*....|....*....|....*....|.
gi 1988774682 4279 AGILDIDTLEKVSVTEAIHRNLVDNITGQRL 4309
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1428-1710 |
7.33e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1428 KNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSE 1507
Cdd:pfam15905 54 RKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1508 ETQkkrqAEEELKRKSEAEKEAAKQKQKALEdLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAA--AELQSKHM 1585
Cdd:pfam15905 134 LTR----VNELLKAKFSEDGTQKKMSSLSME-LMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGkvAQLEEKLV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1586 SFA-EKTSKLEESLKQEHgAVLQLQQEAERLKKQQEDAENSREEAEKelekwRQKANEALRLRLQAEDEAHKKTLAQEEA 1664
Cdd:pfam15905 209 STEkEKIEEKSETEKLLE-YITELSCVSEQVEKYKLDIAQLEELLKE-----KNDEIESLKQSLEEKEQELSKQIKDLNE 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1988774682 1665 EKQKEEAEREAKKRAKAEESALKQKEMAE-EELERQRKIAESTAQQK 1710
Cdd:pfam15905 283 KCKLLESEKEELLREYEEKEQTLNAELEElKEKLTLEEQEHQKLQQK 329
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1595-1944 |
7.35e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.40 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1595 EESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELekwrQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAERE 1674
Cdd:pfam03528 3 DEDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKEL----YLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1675 AKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIR--LRADFDNAE--QQRSLLEDELYRLKNEVAAAQQ 1750
Cdd:pfam03528 79 NIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVREYEVQfhRRLEQERAQwnQYRESAEREIADLRRRLSEGQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1751 QrKQLEDELAKVRSEMDILIQLKTKAEKETMS----NTEKSKQLLEAEAAKMKDL-----AEEASR--LRAISEEAKHQR 1819
Cdd:pfam03528 159 E-ENLEDEMKKAQEDAEKLRSVVMPMEKEIAAlkakLTEAEDKIKELEASKMKELnhyleAEKSCRtdLEMYVAVLNTQK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1820 QIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIAlKEKEAENERLRRQaedeAYQRKALEDQASQHKQEIEEKivq 1899
Cdd:pfam03528 238 SVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKA-NDQFLESQRLLMR----DMQRMESVLTSEQLRQVEEIK--- 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1988774682 1900 lKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKL 1944
Cdd:pfam03528 310 -KKDQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPL 353
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
2468-2586 |
7.47e-03 |
|
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.
Pssm-ID: 434558 [Multi-domain] Cd Length: 154 Bit Score: 40.16 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2468 EMADAQQKKIEHEKTVLQQtfMTEKEmllkKEKLIEDEKKRLESQFEEEvkkakALKDEQERQKQQMEQEKKtlqatmda 2547
Cdd:pfam15236 46 ERERKRQKALEHQNAIKKQ--LEEKE----RQKKLEEERRRQEEQEEEE-----RLRREREEEQKQFEEERR-------- 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1988774682 2548 alsKQKEAEEEMLRKQKEM-QELER-----QRLEQERILAEENQK 2586
Cdd:pfam15236 107 ---KQKEKEEAMTRKTQALlQAMQKaqelaQRLKQEQRIRELAEK 148
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1495-1754 |
7.55e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1495 QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAeRQVKQAEIEKEKQIKvaheaAQK 1574
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQEL-REKRDELNEKVKELK-----EER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1575 SAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEA 1654
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1655 HKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAE--EELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRS 1732
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIElyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260
....*....|....*....|..
gi 1988774682 1733 LLEDELYRLKNEVAAAQQQRKQ 1754
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEK 262
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1693-1869 |
7.70e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1693 EEELER-QRKIAEST------AQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAkvrSE 1765
Cdd:PRK09039 52 DSALDRlNSQIAELAdllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELD---SE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1766 mdiliqlktkaeketmsnteksKQLLEAEAAKMKDLAEEASRLRaiseeakhqRQIAEEEAARQRAEAERilKEKLAAIS 1845
Cdd:PRK09039 129 ----------------------KQVSARALAQVELLNQQIAALR---------RQLAALEAALDASEKRD--RESQAKIA 175
|
170 180
....*....|....*....|....
gi 1988774682 1846 EatrLKTEAEIALKEKEAENERLR 1869
Cdd:PRK09039 176 D---LGRRLNVALAQRVQELNRYR 196
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1905-2472 |
7.95e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1905 EAEMERQKAI---VDDTLKQRRVVEEEIRILKLNfeKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEE 1981
Cdd:pfam05557 1 RAELIESKARlsqLQNEKKQMELEHKRARIELEK--KASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1982 EKRRREAEEKVKKIAAAEEEAA-----------------RQRKAALEELERLRKKAEEARKQKDEADK---EAEKQIVVA 2041
Cdd:pfam05557 79 RLKKKYLEALNKKLNEKESQLAdarevisclknelselrRQIQRAELELQSTNSELEELQERLDLLKAkasEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2042 QQAAQKCSAAEQQVQSV---LAQQIEDSITQKKLKEEyekakklakeaeaaKEKAEREAALLRQQAEEAERQKTAAEEEA 2118
Cdd:pfam05557 159 EKQQSSLAEAEQRIKELefeIQSQEQDSEIVKNSKSE--------------LARIPELEKELERLREHNKHLNENIENKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2119 ANQAKAQEDAERLRKEAEfeaakraqaeaaalMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVK-----LKLDETDK 2193
Cdd:pfam05557 225 LLKEEVEDLKRKLEREEK--------------YREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpedlsRRIEQLQQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2194 QKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQ-----KLLAEEAENMRK 2268
Cdd:pfam05557 291 REIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKerdgyRAILESYDKELT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2269 LAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQ--------EQAQKLL 2340
Cdd:pfam05557 371 MSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADpsyskeevDSLRRKL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2341 EDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEiATQEK 2420
Cdd:pfam05557 451 ETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLE-DDLEQ 529
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 2421 MTVVERLEFERLNtsKEADDLRKaiaDLENEKARLKKEAEELQNKSKEMADA 2472
Cdd:pfam05557 530 VLRLPETTSTMNF--KEVLDLRK---ELESAELKNQRLKEVFQAKIQEFRDV 576
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2340-2572 |
8.10e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2340 LEDKQLMQQRLEEETEEyHKSLEVERKRQleimAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRlheteiatqe 2419
Cdd:pfam15709 328 REQEKASRDRLRAERAE-MRRLEVERKRR----EQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLR---------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2420 kmtvVERLEFERLNTSKEAddlRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKiEHEKTVLQQTFMTEKEMLLKke 2499
Cdd:pfam15709 393 ----KQRLEEERQRQEEEE---RKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQE-EAERAEAEKQRQKELEMQLA-- 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 2500 klieDEKKRLESQFEEEvkkakalKDEQERQKQqmEQEKKTLQatmDAALSKQKEAEEEMLRKQKEMQELERQ 2572
Cdd:pfam15709 463 ----EEQKRLMEMAEEE-------RLEYQRQKQ--EAEEKARL---EAEERRQKEEEAARLALEEAMKQAQEQ 519
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1673-1764 |
8.13e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.54 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1673 REAKKRAKAEESALKQKE-MAEEELERQRKIAEsTAQQKLTAE--------QELIRLRADFDNAEQQRSLLEDELYRLKN 1743
Cdd:pfam07926 7 QSEIKRLKEEAADAEAQLqKLQEDLEKQAEIAR-EAQQNYERElvlhaediKALQALREELNELKAEIAELKAEAESAKA 85
|
90 100
....*....|....*....|....*
gi 1988774682 1744 EVAAAQ----QQRKQLEDELAKVRS 1764
Cdd:pfam07926 86 ELEESEesweEQKKELEKELSELEK 110
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2430-2607 |
8.26e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.30 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2430 ERLNTSKEAD-DLRKAIADLeneKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQtfmteKEMLLKKEKLIEDEKKR 2508
Cdd:pfam05262 184 EALREDNEKGvNFRRDMTDL---KERESQEDAKRAQQLKEELDKKQIDADKAQQKADF-----AQDNADKQRDEVRQKQQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2509 LESQFEE--EVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERilaEENQK 2586
Cdd:pfam05262 256 EAKNLPKpaDTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQ---KKREP 332
|
170 180
....*....|....*....|.
gi 1988774682 2587 LREKLQQLEDAQKDQHTRETD 2607
Cdd:pfam05262 333 VAEDLQKTKPQVEAQPTSLNE 353
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
1463-1601 |
8.32e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 41.54 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1463 LETTEKQKYTAESELKQlrdraaeaEKLRKLAQDEAEKLRKQVSEETQKKRQAEEElkrksEAEKEAAKQKQKALEDLEK 1542
Cdd:PRK06669 30 LSIKEKERLREEEEEQV--------EQLREEANDEAKEIIEEAEEDAFEIVEAAEE-----EAKEELLKKTDEASSIIEK 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 1543 LRMQaeeAERQVKQAEIEKEKQIKVA----HEAAQKSAAAELQSKHMSFAEKTSKLEESLKQE 1601
Cdd:PRK06669 97 LQMQ---IEREQEEWEEELERLIEEAkaegYEEGYEKGREEGLEEVRELIEQLNKIIEKLIKK 156
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2486-2606 |
8.53e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2486 QTFMTEKEMLLKKEKLIEDEKKRLESQFEEE--------VKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEE 2557
Cdd:pfam15709 301 QTFVVTGNMESEEERSEEDPSKALLEKREQEkasrdrlrAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELEL 380
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1988774682 2558 EMLRKQKEMQeLERQRLEQERILAEE---NQKLREKLQQLEDAQKDQHTRET 2606
Cdd:pfam15709 381 EQQRRFEEIR-LRKQRLEEERQRQEEeerKQRLQLQAAQERARQQQEEFRRK 431
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
2343-2537 |
8.76e-03 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 41.86 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2343 KQLMQQRLEEETEEYHKSLEVERKRQLEI-MAEAERLRLQVSQLSeaqaraeeeakkfKKQADKVATRLHETEIATQEKM 2421
Cdd:COG4487 21 ADIVKQRRAEFEKELAERLADAAKREAALeLAEAKAKAQLQEQVA-------------EKDAEIAELRARLEAEERKKAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2422 TVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQ-QTFMTEKEMLLKKEK 2500
Cdd:COG4487 88 AVAEEKEKELAALQEALAEKDAKLAELQAKELELLKKERELEDAKREAELTVEKERDEELDELKeKLKKEEEEKQLAEKS 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1988774682 2501 LIEDEKkrlESQFEEEVKKAKALKDEQERQKQQMEQE 2537
Cdd:COG4487 168 LKVAEY---EKQLKDMQEQIEELKRKKEQGSTQLQGE 201
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3959-3993 |
8.81e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 36.69 E-value: 8.81e-03
10 20 30
....*....|....*....|....*....|....*
gi 1988774682 3959 LLESQAATGYVIDPIKNLKLTVNEAVKMGIVGPEF 3993
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| SPFH_like_u4 |
cd03407 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1736-1884 |
8.96e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259805 [Multi-domain] Cd Length: 269 Bit Score: 41.42 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1736 DELYRLKNEVAaaqqqrKQLEDELAKVRSEMDILIqlktkaeketmsntekskqlleaEAAKMKDLAEEASRLRAISEEA 1815
Cdd:cd03407 106 DEVFESKDEIA------KAVKEELAKVMSEYGYEI-----------------------VKTLVTDIEPDASVKAAMNEIN 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774682 1816 KHQRqiaEEEAARQRAEAERILKEKLAaiseatrlkteaeialkekEAENERLRRQAEDEAYQRKALED 1884
Cdd:cd03407 157 AAQR---LREAAEEKAEAEKILQVKAA-------------------EAEAEAKRLQGVGIAEQRKAIVD 203
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1698-1888 |
9.45e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.16 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1698 RQRKIAESTAQQKLTAEQELIRLRADFD-NAEQQRSLLEDELYRLKNE--VAAAQQQRKQLEDELAKVRSEMDILIQLKT 1774
Cdd:PRK00106 25 KMKSAKEAAELTLLNAEQEAVNLRGKAErDAEHIKKTAKRESKALKKEllLEAKEEARKYREEIEQEFKSERQELKQIES 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1775 KAEKETMSNTEKSKQLLEAEaaKMKDLAEEAsrlraISEEAKH----QRQIAEEEAaRQRAEAERI----LKEKLAAISE 1846
Cdd:PRK00106 105 RLTERATSLDRKDENLSSKE--KTLESKEQS-----LTDKSKHiderEEQVEKLEE-QKKAELERVaalsQAEAREIILA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1988774682 1847 ATRLKTEAEIALKEKEAENE---RLRRQAED---EAYQRKALEDQASQ 1888
Cdd:PRK00106 177 ETENKLTHEIATRIREAEREvkdRSDKMAKDllaQAMQRLAGEYVTEQ 224
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1612-1710 |
9.45e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 39.76 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1612 AERLKKQQEDAEnsrEEAEKELEKWRQKANEalrLRLQAEDEAHKktlaqeeaekqkeeAEREAKKRAKAEesALKQKEM 1691
Cdd:PRK05759 47 AERAKKELELAQ---AKYEAQLAEARAEAAE---IIEQAKKRAAQ--------------IIEEAKAEAEAE--AARIKAQ 104
|
90
....*....|....*....
gi 1988774682 1692 AEEELERQRKIAESTAQQK 1710
Cdd:PRK05759 105 AQAEIEQERKRAREELRKQ 123
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2399-2613 |
9.48e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2399 FKKQADKVATRLHETE--IATQEKMTVVERLEFERL--NTSKEADDLRKAiadLENEKARLKKEAEELQNKSKEMADAQQ 2474
Cdd:PTZ00121 1081 FDAKEDNRADEATEEAfgKAEEAKKTETGKAEEARKaeEAKKKAEDARKA---EEARKAEDARKAEEARKAEDAKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 2475 KKIEHEKTVlqqtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKE 2554
Cdd:PTZ00121 1158 RKAEDARKA-------EEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK 1230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774682 2555 AEEEMLRKQKEMQELERQRLEQERILAEENQ----KLREKLQQLEDAQKDQHTRETDKVLHKD 2613
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEIRKFEEARmahfARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1870-2072 |
9.55e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1870 RQAEDEAYQRKALEDQASQHKQEIEEkivqLKKSSEAEMERQKAivddtLKQRRVVEEEIRIlklnfEKASSGKLDLELE 1949
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEE----LQQKQAAEQERLKQ-----LEKERLAAQEQKK-----QAEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1950 LNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAAR-----QRKAALEELERLRKKAEEAR 2024
Cdd:PRK09510 132 KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKaeaeaAAKAAAEAKKKAEAEAKKKA 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1988774682 2025 KQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKL 2072
Cdd:PRK09510 212 AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| PRK09173 |
PRK09173 |
F0F1 ATP synthase subunit B; Validated |
1791-1901 |
9.64e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 169691 [Multi-domain] Cd Length: 159 Bit Score: 40.11 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774682 1791 LEAEAAKMKDLAEEASRLRaisEEAKH-------QRQIAEEEAARQRAEAERilkEKLAAISEAtRLKTEAEIALKEKEA 1863
Cdd:PRK09173 31 LDARADRIKNELAEARRLR---EEAQQllaeyqrKRKEAEKEAADIVAAAER---EAEALTAEA-KRKTEEYVARRNKLA 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1988774682 1864 ENErlRRQAEDEAYQ--------------RKALEDQASQHKQE--IEEKIVQLK 1901
Cdd:PRK09173 104 EQK--IAQAETDAINavrssavdlaiaaaEKLLAEKVDAKAASelFKDALAQVK 155
|
|
| |
