|
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 |
1.04e-74 |
|
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: 244.23 E-value: 1.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 43 DRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNI 122
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1927222988 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 |
3.12e-71 |
|
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: 234.92 E-value: 3.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 40 DERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 119
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1927222988 120 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQINGQSE 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 |
1.72e-68 |
|
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: 227.56 E-value: 1.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 35 MDGRKDERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKH 114
Cdd:cd21236 7 LERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKR 86
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1927222988 115 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQINGQ 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 |
6.23e-67 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 222.20 E-value: 6.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 160 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLD 239
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1927222988 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 |
7.45e-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: 7.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDP 240
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1927222988 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 |
2.74e-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: 203.73 E-value: 2.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 40 DERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 119
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1927222988 120 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQINGQS 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 |
1.53e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 195.21 E-value: 1.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERdLGVTRLLDP 240
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1927222988 241 EDVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
159-265 |
1.10e-50 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 175.62 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 159 DMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERdLGVTRLL 238
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1927222988 239 DPEDVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
45-148 |
2.67e-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: 2.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 45 VQKKTFTKWVNKHLIKSQRQ-VTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 123
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKPpIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1927222988 124 NDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
40-144 |
2.00e-47 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 166.77 E-value: 2.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 40 DERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQVK 118
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRVH 90
|
90 100
....*....|....*....|....*.
gi 1927222988 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 |
2.39e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 162.97 E-value: 2.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDP 240
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1927222988 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 |
6.67e-45 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 159.46 E-value: 6.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 41 ERDRVQKKTFTKWVNKHLIKSQR--QVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 116
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1927222988 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 |
5.63e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 156.40 E-value: 5.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDP 240
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1927222988 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 |
4.56e-43 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 153.99 E-value: 4.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 39 KDERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLkHRQV 117
Cdd:cd21193 10 QEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL-KTKV 88
|
90 100
....*....|....*....|....*..
gi 1927222988 118 KLVNIRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21193 89 RLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1347-2589 |
4.22e-42 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 171.55 E-value: 4.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1347 TDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELdkqkqlaevHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEkqkhn 1426
Cdd:NF041483 90 ADAERELRDARAQTQRILQEHAEHQARLQAEL---------HTEAVQRRQQLDQELAERRQTVESHVNENVAWAE----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1427 iqlelhELKNLSEQQ---IMDKSKQVDDALQSRVKIEEEirliRLQLETTVKQKSTAES---ELKQLRDRA-AEAEKLRK 1499
Cdd:NF041483 156 ------QLRARTESQarrLLDESRAEAEQALAAARAEAE----RLAEEARQRLGSEAESaraEAEAILRRArKDAERLLN 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1500 AAQEEA-------EKLRKQVNEETQKKRMAEEELKRKAEAEKEaakqkqkalEDLENLKRQAEEAERQVKQAEIEKERQI 1572
Cdd:NF041483 226 AASTQAqeatdhaEQLRSSTAAESDQARRQAAELSRAAEQRMQ---------EAEEALREARAEAEKVVAEAKEAAAKQL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1573 QVAHVA-AQKSAAAELQSKHMsfVEKTSKLEESLKQEHGAVL---QLQHEAAALKKQQEDAERAREEAEKELEKWRQKAN 1648
Cdd:NF041483 297 ASAESAnEQRTRTAKEEIARL--VGEATKEAEALKAEAEQALadaRAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAE 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1649 EALRlrlQAEEEAHKKS-LAQEDAEKQKEEAEREAKK-RAKAEDSALKQKEMAENELERQRkvAESTAQQkltaeQELIR 1726
Cdd:NF041483 375 EVLT---KASEDAKATTrAAAEEAERIRREAEAEADRlRGEAADQAEQLKGAAKDDTKEYR--AKTVELQ-----EEARR 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1727 LRADfdnAEQQRSLLEDELYRLKNE-----VVAAQQQRKQLEDELAKVRSEMDvliQLKSKAEKEtmsnSERSKQLLEVE 1801
Cdd:NF041483 445 LRGE---AEQLRAEAVAEGERIRGEarreaVQQIEEAARTAEELLTKAKADAD---ELRSTATAE----SERVRTEAIER 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1802 ATKMRDLAE--------EASKLRAIAEE-AKHQRQVAEEEAARQRAEAERILKEKLA-AISDATRLKTEAE-------IA 1864
Cdd:NF041483 515 ATTLRRQAEetlertraEAERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEerltaaeEA 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1865 LKEKEAENERLRRQAEDEAYQRKAledqanqhkqQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRIlKLNFE 1944
Cdd:NF041483 595 LADARAEAERIRREAAEETERLRT----------EAAERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAV-RLRSE 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1945 KASsgkldlelELNKLKNIAEETQQsKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLK 2024
Cdd:NF041483 664 AAA--------EAERLKSEAQESAD-RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAR 734
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2025 KKAEE----ARKQKDDADKEAEKQILMA-QQAAQKCSAAEQQvqsvlAQQKEDTImqtklkeeyekakklakqaEAAKEK 2099
Cdd:NF041483 735 EQSEEllasARKRVEEAQAEAQRLVEEAdRRATELVSAAEQT-----AQQVRDSV-------------------AGLQEQ 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2100 AEREAALLRQQAEE-AERQKAaaeqeaanqaKAQEDAERLRKEAEfeaAKRAQAENAALKQKQQADAEMAKHKKLAEQTL 2178
Cdd:NF041483 791 AEEEIAGLRSAAEHaAERTRT----------EAQEEADRVRSDAY---AERERASEDANRLRREAQEETEAAKALAERTV 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2179 KQKFQvEQEltkvKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVK----VQMEELLKLKLRIEEENQRL 2254
Cdd:NF041483 858 SEAIA-EAE----RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAE 932
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2255 IKKDKDNTQKFLAKEADNMK-KLAEDAARLSVEAQ-EAARLRQIAEDDLNQqraladkmlkekmqAIQEASRLRAEAEml 2332
Cdd:NF041483 933 ARAEAERLRDEARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGS--------------AQQHAERIRTEAE-- 996
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2333 qRQKDLAQEQAQKLLEDKQLMQQR-LDEETEEYQK--SLEAERKRQLEIIAESEKLKLqvsqLSEAQAKAQEEAKKFKKQ 2409
Cdd:NF041483 997 -RVKAEAAAEAERLRTEAREEADRtLDEARKDANKrrSEAAEQADTLITEAAAEADQL----TAKAQEEALRTTTEAEAQ 1071
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2410 ADSI-------ASRLHETelATQEKMTVVEK--------LEVARLTSS---KEADDLRKAI-ADLEKEKSRLKKEAEDLQ 2470
Cdd:NF041483 1072 ADTMvgaarkeAERIVAE--ATVEGNSLVEKartdadelLVGARRDATairERAEELRDRItGEIEELHERARRESAEQM 1149
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2471 NKSKEMADAQQKQIEHektvlQQTFLSEKEMLLKKEKLIEEEKKRLESqfeeeVKKAKALKDEQERQKQQMEDEKKKLQA 2550
Cdd:NF041483 1150 KSAGERCDALVKAAEE-----QLAEAEAKAKELVSDANSEASKVRIAA-----VKKAEGLLKEAEQKKAELVREAEKIKA 1219
|
1290 1300 1310
....*....|....*....|....*....|....*....
gi 1927222988 2551 TMDAalnkqkEAEKEMHNKQKEMKELERKRleqERILAE 2589
Cdd:NF041483 1220 EAEA------EAKRTVEEGKRELDVLVRRR---EDINAE 1249
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
44-261 |
1.74e-41 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 164.73 E-value: 1.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 44 RVQKKTFTKWVNKHLIKS-QRQVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLV 120
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 121 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQingQSEDMTAKEKLLLWSQRMTDGYQ-GIRCDNFTTSWRDGKLFNAVI 199
Cdd:COG5069 88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222988 200 HKHYPRLVDmgrvYRQTNLE------NLEQAFGVAERDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLY 261
Cdd:COG5069 165 HDSRPDTLD----PNVLDLQkknkalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
41-148 |
2.51e-41 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 149.26 E-value: 2.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 41 ERDRVQKKTFTKWVNKHLIK--SQRQVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 116
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKlsQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1927222988 117 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
29-144 |
5.17e-41 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 149.05 E-value: 5.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 29 QGMLKAMdgrKDERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQI 107
Cdd:cd21317 18 RSRIKAL---ADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDK 94
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222988 108 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21317 95 ALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
40-144 |
7.00e-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: 149.02 E-value: 7.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 40 DERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQVK 118
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQRVH 112
|
90 100
....*....|....*....|....*.
gi 1927222988 119 LVNIRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21318 113 LENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
157-261 |
1.10e-39 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 144.38 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 157 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTR 236
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1927222988 237 LLDPEDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
895-972 |
2.63e-39 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 141.97 E-value: 2.63e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 895 LSWQYLMRDYTQIRSWNITMLKTMKPEEYRLVMRNLELHYQDYMRDSQDSQLFGPDDRMQIEEDYTKSTQHFDSLIRS 972
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
160-265 |
1.29e-38 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 141.30 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 160 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLD 239
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1927222988 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 |
2.85e-38 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 140.35 E-value: 2.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 41 ERDRVQKKTFTKWVNKHLIKSQ--RQVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 118
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1927222988 119 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
43-144 |
3.99e-38 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 139.45 E-value: 3.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 43 DRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQVKLVN 121
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1927222988 122 IRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
45-146 |
4.26e-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: 139.46 E-value: 4.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 45 VQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 122
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1927222988 123 RNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
148-263 |
8.08e-38 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 139.03 E-value: 8.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 148 ISDIQIngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGV 227
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222988 228 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
160-261 |
3.95e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 136.92 E-value: 3.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 160 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLD 239
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1927222988 240 PEDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1782-2613 |
5.05e-37 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 155.68 E-value: 5.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1782 KAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAI--AEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKT 1859
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKkkAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1860 EAEIALKEKEAENERLRRQAEDeayQRKALEDQANQHKQQIE-----EKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEE 1934
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEaarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1935 EIRIlklnfEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQ 2014
Cdd:PTZ00121 1242 AKKA-----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2015 ---------AAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSvlAQQKEDTImqTKLKEEYEK 2085
Cdd:PTZ00121 1317 adeakkkaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE--AKKKADAA--KKKAEEKKK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2086 AKKLAKQAEAAKEKAE--REAALLRQQAEEAERQKAAAEQEAANQAKAQE--DAERLRKEAEfeaaKRAQAENAALKQKQ 2161
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADelKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEakKADEAKKKAE----EAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2162 QADAEMAKHKklAEQTLKQKfQVEQELTKVKLKLDETDKQksvldEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELL 2241
Cdd:PTZ00121 1469 AKKADEAKKK--AEEAKKAD-EAKKKAEEAKKKADEAKKA-----AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2242 KlklriEEEnqrliKKDKDNTQKflakeADNMKKLAEdaARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQE 2321
Cdd:PTZ00121 1541 K-----AEE-----KKKADELKK-----AEELKKAEE--KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2322 ASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEII-AESEKLKLQVSQLSEAQAKAQ 2400
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkAAEEAKKAEEDKKKAEEAKKA 1683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2401 EEAKkfKKQADSIASRLHETELATQEKMTVVEklEVARLTSSKEADDLRKAIAD-LEKEKSRLKKEAEDLQNKSKEMADA 2479
Cdd:PTZ00121 1684 EEDE--KKAAEALKKEAEEAKKAEELKKKEAE--EKKKAEELKKAEEENKIKAEeAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2480 QQKQIEHEKTVlqQTFLSEKEMLLKKEKLIEEEKKRLESQfeeevKKAKALKDEQE--------------RQKQQMEDEK 2545
Cdd:PTZ00121 1760 AHLKKEEEKKA--EEIRKEKEAVIEEELDEEDEKRRMEVD-----KKIKDIFDNFAniieggkegnlvinDSKEMEDSAI 1832
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2546 KKLQATMDAALNKQKEAEKEMHNKQKEMKELERKR--LEQERILAEENQKLREKLQQLEEAQKDQPDKEV 2613
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEadFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
157-261 |
6.20e-36 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 134.03 E-value: 6.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 157 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTR 236
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1927222988 237 LLDPEDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1347-2274 |
3.37e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 149.52 E-value: 3.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1347 TDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEkeaqelKLRMQEEVNRREDAVVDAEKQKHN 1426
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAE------EARKAEDARKAEEARKAEDAKRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1427 IQLELHELKNLSEQQIMDKSKQVDDALQS-RVKIEEEIRlirlqlettvKQKSTAESELKQLRDRAAEAEKLRKAAQE-E 1504
Cdd:PTZ00121 1156 IARKAEDARKAEEARKAEDAKKAEAARKAeEVRKAEELR----------KAEDARKAEAARKAEEERKAEEARKAEDAkK 1225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1505 AEKLRKQvnEETQKKrmaEEELKRKAEAEKEAAKQKQKALEDLENLKRQ----AEEAERQVKQAEIEKERQIQVAHVAAQ 1580
Cdd:PTZ00121 1226 AEAVKKA--EEAKKD---AEEAKKAEEERNNEEIRKFEEARMAHFARRQaaikAEEARKADELKKAEEKKKADEAKKAEE 1300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1581 KSAAAELQSKhmsfVEKTSKLEESLKQEHgavlQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANealrlrlQAEEE 1660
Cdd:PTZ00121 1301 KKKADEAKKK----AEEAKKADEAKKKAE----EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE-------AAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1661 AHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRlRADFDNAEQQRSL 1740
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEEAK 1444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1741 LEDELYRLKNEVVAAQQQRKQLE-----DELAKVRSEMDVLIQLKSKAEKETMSNSERSKqlleveATKMRDLAEEASKl 1815
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEeakkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKK------AAEAKKKADEAKK- 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1816 raiAEEAKHQRQVAEEEAARQRAEAerilkEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQ 1895
Cdd:PTZ00121 1518 ---AEEAKKADEAKKAEEAKKADEA-----KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1896 HKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRV-VEEEIRilklnfEKASSGKLDLELELNKLKNIAEETQQSKLRA 1974
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkKAEEEK------KKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1975 EEEAEKLRKLALEEEKRRREAEEKVKKiaaaeEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQK 2054
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKA-----AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2055 CSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAA-KEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQE 2133
Cdd:PTZ00121 1739 AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAViEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGN 1818
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2134 DAERLRKEAEFEAAKraQAENAALKQKQQADaEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLK 2213
Cdd:PTZ00121 1819 LVINDSKEMEDSAIK--EVADSKNMQLEEAD-AFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDK 1895
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 2214 DEVDDAVKQRGQVEE--ELLKVKVQMEELLKLKlrIEEENQRLIKKDKDN--TQKFLAKEADNMK 2274
Cdd:PTZ00121 1896 DDIEREIPNNNMAGKnnDIIDDKLDKDEYIKRD--AEETREEIIKISKKDmcINDFSSKFCDYMK 1958
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
40-148 |
5.02e-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: 131.20 E-value: 5.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 40 DERDRVQKKTFTKWVNKHLIKSQRQ-VTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 118
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKPpIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1927222988 119 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
145-261 |
1.47e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 130.56 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 145 HFQISDIQINGQSEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQA 224
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222988 225 FGVAERDLGVTRLLDPEDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
164-265 |
4.07e-34 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 128.31 E-value: 4.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 164 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED 242
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1927222988 243 VDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1868-2643 |
6.83e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 145.28 E-value: 6.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1868 KEAENERLRRQAEDEAYQ--RKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVE----EEIRILKL 1941
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEeaFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEarkaEDAKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1942 NFEKASSGKLDLELELNKLKNIAEETQQSKLRaeeEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELD 2021
Cdd:PTZ00121 1157 ARKAEDARKAEEARKAEDAKKAEAARKAEEVR---KAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2022 RLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSvlaQQKEDTIMQTKLKEEYEKAKKL--AKQAEAAKEK 2099
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE---ARKADELKKAEEKKKADEAKKAeeKKKADEAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2100 AE--REAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQt 2177
Cdd:PTZ00121 1311 AEeaKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE- 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2178 lkqkfqveqeltkvKLKLDETDKQKsvldEELQRLKDEVDDAVKQRGQVEEellkVKVQMEEllklKLRIEEENQRLIKK 2257
Cdd:PTZ00121 1390 --------------KKKADEAKKKA----EEDKKKADELKKAAAAKKKADE----AKKKAEE----KKKADEAKKKAEEA 1443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2258 DKDNTQKFLAKEadnmKKLAEDAARLSVEAQEAARLRQIAEddlnqQRALADKMLKEKMQAIQEASRLRAEAEMLQRQkd 2337
Cdd:PTZ00121 1444 KKADEAKKKAEE----AKKAEEAKKKAEEAKKADEAKKKAE-----EAKKADEAKKKAEEAKKKADEAKKAAEAKKKA-- 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2338 laqEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRL 2417
Cdd:PTZ00121 1513 ---DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2418 HETELatQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLS 2497
Cdd:PTZ00121 1590 EEARI--EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2498 EKEmllkkeklieeekkrlesqfEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELE 2577
Cdd:PTZ00121 1668 KKA--------------------EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 2578 RK-RLEQERILAEENQKlreklqQLEEAQKDQPDK-EVIHVTMVETTKNVYNGQNVGDVVDSAEKKPD 2643
Cdd:PTZ00121 1728 NKiKAEEAKKEAEEDKK------KAEEAKKDEEEKkKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
161-261 |
2.68e-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: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDP 240
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1927222988 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 |
3.02e-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: 127.47 E-value: 3.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 40 DERDRVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQVK 118
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 127
|
90 100
....*....|....*....|....*.
gi 1927222988 119 LVNIRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21316 128 LENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1498-2363 |
2.79e-32 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 139.42 E-value: 2.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1498 RKAAQEEA---EKLRKQVNEETQKKRMAEEELKRkaeaekeaakqkqkaLED--------LENLKRQAEEAER--QVKQA 1564
Cdd:TIGR02168 157 RRAIFEEAagiSKYKERRKETERKLERTRENLDR---------------LEDilnelerqLKSLERQAEKAERykELKAE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1565 EIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWR 1644
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1645 QKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQEL 1724
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1725 IRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDvliqlkSKAEKETMSNSERSKQLLEVEATK 1804
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE------EAELKELQAELEELEEELEELQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1805 MRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAErILKEKLAAISDATRlktEAEIALKEKEAEN-------ERLRR 1877
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSE---GVKALLKNQSGLSgilgvlsELISV 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1878 QAEDEAYQRKALEDQANQ----HKQQIEEKIVLLKKSS-------EAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKA 1946
Cdd:TIGR02168 532 DEGYEAAIEAALGGRLQAvvveNLNAAKKAIAFLKQNElgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFD 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1947 SSGKLDLELELNKL---KNIAEETQQSKLRAEEE-------------------AEKLRKLALEEEKRRREAEEKVKKIAA 2004
Cdd:TIGR02168 612 PKLRKALSYLLGGVlvvDDLDNALELAKKLRPGYrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEE 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2005 AEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYE 2084
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2085 KAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKaaaeqeaanqAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQAD 2164
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREAL----------DELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2165 AEMAKHKKLAEQTLK---QKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKvqmEELL 2241
Cdd:TIGR02168 842 DLEEQIEELSEDIESlaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR---RELE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2242 KLKLRIEEENQRLikkdkdntQKFLAKEADNMKKLAEDAarlSVEAQEAARLRQIAEDDLNQQRALADKmLKEK------ 2315
Cdd:TIGR02168 919 ELREKLAQLELRL--------EGLEVRIDNLQERLSEEY---SLTLEEAEALENKIEDDEEEARRRLKR-LENKikelgp 986
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2316 --MQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEdkqlMQQRLDEETEE 2363
Cdd:TIGR02168 987 vnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE----AIEEIDREARE 1032
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
45-148 |
3.07e-32 |
|
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: 122.78 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 45 VQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 122
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1927222988 123 RNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1478-2367 |
7.35e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 138.74 E-value: 7.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1478 STAESELKQLRD-RAAEAEKLRKAAQEEAEKLRKQVNEETQKKrmaEEELKRKAEAEKEAAKQKQKALEDLENlKRQAEE 1556
Cdd:PTZ00121 1075 SYKDFDFDAKEDnRADEATEEAFGKAEEAKKTETGKAEEARKA---EEAKKKAEDARKAEEARKAEDARKAEE-ARKAED 1150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1557 AERQVKQAEIEKERQIQVAHVAAQ-KSAAAELQSKHMSFVEKTSKLEESLKQEhgavlqlqheaAALKKQQEdaeraree 1635
Cdd:PTZ00121 1151 AKRVEIARKAEDARKAEEARKAEDaKKAEAARKAEEVRKAEELRKAEDARKAE-----------AARKAEEE-------- 1211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1636 aekelekwrQKANEALRLRLQAEEEAHKKSlaqEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQ 1715
Cdd:PTZ00121 1212 ---------RKAEEARKAEDAKKAEAVKKA---EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK 1279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1716 QKLTAEQELIRLRADFDNAEQQRSLleDELYRLKNEVVAAQQQRKQLE------DELAKVRSEMDVLIQLKSKAEKETMS 1789
Cdd:PTZ00121 1280 ADELKKAEEKKKADEAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEeakkkaDAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1790 NSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQvAEEEAARQRAEAERiLKEKLAAISDATRLKTEAEIALKEKE 1869
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE-AKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEEKKKADE 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1870 AENERLRRQAEDEAYQRKALEDQANQHKQQIEEKivllKKSSEAEMERQRAIVDDTLKQRrvvEEEIRILKLNFEKASSG 1949
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA----KKADEAKKKAEEAKKADEAKKK---AEEAKKKADEAKKAAEA 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1950 KLDLElelnKLKNIAEETQQSKLRAEEEAEKLRKLaleeekrrrEAEEKVKKiaaaeeeaarqrqaaQDELDRLK--KKA 2027
Cdd:PTZ00121 1509 KKKAD----EAKKAEEAKKADEAKKAEEAKKADEA---------KKAEEKKK---------------ADELKKAEelKKA 1560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2028 EEARKqKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALL 2107
Cdd:PTZ00121 1561 EEKKK-AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2108 RQQAEEAER-------QKAAAEQEAANQAKAQED---AERLRKEaefEAAKRAQAENAALKQKQQADAEMAKHKKLAEQT 2177
Cdd:PTZ00121 1640 KKEAEEKKKaeelkkaEEENKIKAAEEAKKAEEDkkkAEEAKKA---EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2178 LKQKFQVEQELTKVKL----KLDETDKQKSvldEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQR 2253
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAeeakKEAEEDKKKA---EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2254 L-----IKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAArlrqiaeDDLNQQRALADKMLKEKMQAIQEASRLRAE 2328
Cdd:PTZ00121 1794 MevdkkIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVA-------DSKNMQLEEADAFEKHKFNKNNENGEDGNK 1866
|
890 900 910
....*....|....*....|....*....|....*....
gi 1927222988 2329 AEMLQRQKDLAQEQAQKLLEDKqlMQQRLDEETEEYQKS 2367
Cdd:PTZ00121 1867 EADFNKEKDLKEDDEEEIEEAD--EIEKIDKDDIEREIP 1903
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
45-148 |
1.17e-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: 121.27 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 45 VQKKTFTKWVNKHLIKSQR-QVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 123
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1927222988 124 NDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
44-149 |
3.49e-31 |
|
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: 120.63 E-value: 3.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 44 RVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQ-VKLV 120
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1927222988 121 NIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
41-150 |
4.15e-31 |
|
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: 119.99 E-value: 4.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 41 ERDRVQKKTFTKWVNKHLIKSQR--QVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQ 116
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1927222988 117 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 150
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
160-258 |
6.71e-31 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 119.07 E-value: 6.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 160 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLD 239
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1927222988 240 PEDVDVPHPDEKSIITYVS 258
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
164-266 |
1.68e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 118.11 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 164 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTN-LENLEQAFGVAERDLGVTRLLDPE 241
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1927222988 242 DVDVPHPDEKSIITYVSSLYDAMPR 266
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
44-146 |
1.77e-30 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 117.97 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 44 RVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 120
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1927222988 121 NIRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1323-2113 |
3.62e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 132.49 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1323 QEYVTLRTKYSEL-MTLTSQYIKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELdkqkqlaEVHAKAIAKAEKEAQE 1401
Cdd:TIGR02168 213 ERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL-------EELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1402 LklrmQEEVNRREDAVVDAEKQKHNIQLELHELknlsEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAE 1481
Cdd:TIGR02168 286 L----QKELYALANEISRLEQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1482 SELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQV 1561
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1562 KQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEH-------------GAVLQLQHEAAALKKQQED 1628
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAqlqarldslerlqENLEGFSEGVKALLKNQSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1629 AERAREEAEKEL---EKWRQKANEALRLRLQAeeeahkksLAQEDAEKQKEEAEreakkrakaedsALKQKE-----MAE 1700
Cdd:TIGR02168 518 LSGILGVLSELIsvdEGYEAAIEAALGGRLQA--------VVVENLNAAKKAIA------------FLKQNElgrvtFLP 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1701 NELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLK--NEVVAAQQQRKQLEDELAKVRSEMDVLIQ 1778
Cdd:TIGR02168 578 LDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLDGDLVRP 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1779 ---LKSKAEKETMSNSERSKQLLEVEAtKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDAT 1855
Cdd:TIGR02168 658 ggvITGGSAKTNSSILERRREIEELEE-KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1856 RLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEdQANQHKQQIEEKIVLLkkssEAEMERQRAIVDDTLKQRRVVEEE 1935
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEEL----EAQIEQLKEELKALREALDELRAE 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1936 IRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQA 2015
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2016 AQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMqtklkeEYEKAKKLAKQAEA 2095
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL------TLEEAEALENKIED 965
|
810
....*....|....*...
gi 1927222988 2096 AKEKAEREAALLRQQAEE 2113
Cdd:TIGR02168 966 DEEEARRRLKRLENKIKE 983
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
160-258 |
3.74e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 116.86 E-value: 3.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 160 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLD 239
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1927222988 240 PEDVDVPHPDEKSIITYVS 258
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1350-1902 |
1.13e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 130.44 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1350 QRRLEDEEKAAEKLKAEEqkkmammqAELDKQKQLAEvhaKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQL 1429
Cdd:COG1196 238 EAELEELEAELEELEAEL--------EELEAELAELE---AELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1430 ELHELKNLSEQQimdkskqvDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLR 1509
Cdd:COG1196 307 LEERRRELEERL--------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1510 KQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQvaHVAAQKSAAAELQS 1589
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--ALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1590 KHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRL-QAEEEAHKKSLAQ 1668
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLaGAVAVLIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1669 EDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDEL--Y 1746
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAryY 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1747 RLKNEVV----------AAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETmsnsERSKQLLEVEATKMRDLAEEASKLR 1816
Cdd:COG1196 617 VLGDTLLgrtlvaarleAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR----RELLAALLEAEAELEELAERLAEEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1817 AIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQH 1896
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
....*.
gi 1927222988 1897 KQQIEE 1902
Cdd:COG1196 773 EREIEA 778
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
148-263 |
1.18e-29 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 115.70 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 148 ISDIQingqSEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGV 227
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222988 228 AERDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLYDA 263
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1489-2589 |
1.62e-29 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 130.33 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1489 DRAAEAEKLRKAAQEEAEKLRKqvneetqkkrmaeeelkrkaeaekeaakqkqkaledlenlkrqaeEAERQVKQAEIEK 1568
Cdd:NF041483 69 DIGYQAEQLLRNAQIQADQLRA---------------------------------------------DAERELRDARAQT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1569 ERQIQvAHVAAQKSAAAELqskHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQqeDAERAREEAEKELEKWRQKAN 1648
Cdd:NF041483 104 QRILQ-EHAEHQARLQAEL---HTEAVQRRQQLDQELAERRQTVESHVNENVAWAEQ--LRARTESQARRLLDESRAEAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1649 EALrlrlqAEEEAHKKSLAQEDAEKQKEEAEreaKKRAKAEDSALKQKEMAENELErqrkvAESTAQQKLTAEQELIR-- 1726
Cdd:NF041483 178 QAL-----AAARAEAERLAEEARQRLGSEAE---SARAEAEAILRRARKDAERLLN-----AASTQAQEATDHAEQLRss 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1727 LRADFDNAEQQRSlledELYRlknevvAAQQQRKQLEDELAKVRSEMD-VLIQLKSKAEKETMS----NSERSKQL---- 1797
Cdd:NF041483 245 TAAESDQARRQAA----ELSR------AAEQRMQEAEEALREARAEAEkVVAEAKEAAAKQLASaesaNEQRTRTAkeei 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1798 --LEVEATKMRD-LAEEASKLRA---------IAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKT-----E 1860
Cdd:NF041483 315 arLVGEATKEAEaLKAEAEQALAdaraeaeklVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTraaaeE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1861 AEIALKEKEAENERLRRQAEDEAYQRK--ALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDtlkqRRVVEEEIRI 1938
Cdd:NF041483 395 AERIRREAEAEADRLRGEAADQAEQLKgaAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEG----ERIRGEARRE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1939 LKLNFEKASSGKLDLeleLNKLKNIAEETQQSklrAEEEAEKLRKLALEEEKRRREAEEkvkkiaaaeeeaarqrqaaqd 2018
Cdd:NF041483 471 AVQQIEEAARTAEEL---LTKAKADADELRST---ATAESERVRTEAIERATTLRRQAE--------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2019 elDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSaaEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEA-AK 2097
Cdd:NF041483 524 --ETLERTRAEAERLRAEAEEQAEEVRAAAERAARELR--EETERAIAARQAEAAEELTRLHTEAEERLTAAEEALAdAR 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2098 EKAEReaaLLRQQAEEAERQKAAAEQEAAN-QAKAQEDAERLRKEAEFEA-AKRAQAENAALKQKQQADAEMAKHKKLAE 2175
Cdd:NF041483 600 AEAER---IRREAAEETERLRTEAAERIRTlQAQAEQEAERLRTEAAADAsAARAEGENVAVRLRSEAAAEAERLKSEAQ 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2176 QTlKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELL-KLKLRIEE---EN 2251
Cdd:NF041483 677 ES-ADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLaSARKRVEEaqaEA 755
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2252 QRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQE------------AARLRQIAEDDLNQQRALAdkmLKEKMQAI 2319
Cdd:NF041483 756 QRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEeiaglrsaaehaAERTRTEAQEEADRVRSDA---YAERERAS 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2320 QEASRLRAEAemlQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKrqlEIIAESEKlklqvsQLSEAQAKA 2399
Cdd:NF041483 833 EDANRLRREA---QEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEAS---DTLASAEQ------DAARTRADA 900
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2400 QEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTS--SKEADDLR-KAIADLEKEKSRLKKEAEDLQNKSKEM 2476
Cdd:NF041483 901 REDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDeaRAEAERVRaDAAAQAEQLIAEATGEAERLRAEAAET 980
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2477 ADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQ-ERQKQQMEDEKKKLQA-TMDA 2554
Cdd:NF041483 981 VGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQaDTLITEAAAEADQLTAkAQEE 1060
|
1130 1140 1150
....*....|....*....|....*....|....*
gi 1927222988 2555 ALNKQKEAEKEmhnkQKEMKELERKrlEQERILAE 2589
Cdd:NF041483 1061 ALRTTTEAEAQ----ADTMVGAARK--EAERIVAE 1089
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1358-2240 |
3.91e-29 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 129.18 E-value: 3.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1358 KAAEKLKAEEQKKMAMMQAELDK---------QKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVD-AEKQKHNI 1427
Cdd:NF041483 323 KEAEALKAEAEQALADARAEAEKlvaeaaekaRTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEeAERIRREA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1428 QLELHELKNLSEQQIMD-KSKQVDDALQSR---VKIEEEIRLIRLQLET-------------------TVKQ----KSTA 1480
Cdd:NF041483 403 EAEADRLRGEAADQAEQlKGAAKDDTKEYRaktVELQEEARRLRGEAEQlraeavaegerirgearreAVQQieeaARTA 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1481 ESELKQLRDRA--------AEAEKLRKAAQEEAEKLRKQVnEETQKKRMAEEELKRKAEAekeaakqkqkalEDLENLKR 1552
Cdd:NF041483 483 EELLTKAKADAdelrstatAESERVRTEAIERATTLRRQA-EETLERTRAEAERLRAEAE------------EQAEEVRA 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1553 QAEEAERQVKQaeiEKERQIQvahvAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERA 1632
Cdd:NF041483 550 AAERAARELRE---ETERAIA----ARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLRTEAAE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1633 -----REEAEKELEKWRQKA------------NEALRLRLQAEEEAHK-KSLAQEDAEKQKEE----AER----EAKKRA 1686
Cdd:NF041483 623 rirtlQAQAEQEAERLRTEAaadasaaraegeNVAVRLRSEAAAEAERlKSEAQESADRVRAEaaaaAERvgteAAEALA 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1687 KAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELI---RLRADFDNAEQQRsLLEDELYRLKNEVVAAQQQRKQLE 1763
Cdd:NF041483 703 AAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasaRKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVR 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1764 DELAKVRSEMDVLIQ-LKSKAEKEtmsnSERSKQLLEVEATKMRDLAeEASKLRAiAEEAKHQRQVAEEEAARQRAEAER 1842
Cdd:NF041483 782 DSVAGLQEQAEEEIAgLRSAAEHA----AERTRTEAQEEADRVRSDA-YAERERA-SEDANRLRREAQEETEAAKALAER 855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1843 ILKEKLA--------AISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAleDQANQHKQQIEEkivllkKSSEAE 1914
Cdd:NF041483 856 TVSEAIAeaerlrsdASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRS--DAAAQADRLIGE------ATSEAE 927
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1915 MERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSklrAEEEAEKLRKLALEEEKRRRE 1994
Cdd:NF041483 928 RLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGS---AQQHAERIRTEAERVKAEAAA 1004
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1995 AEEKVKKiAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSA-AEQQVQSVL--AQQKE 2071
Cdd:NF041483 1005 EAERLRT-EAREEADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTeAEAQADTMVgaARKEA 1083
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2072 DTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAeRQKAAAEQEAANQAKAQEDAERLRKEAE-----FEA 2146
Cdd:NF041483 1084 ERIVAEATVEGNSLVEKARTDADELLVGARRDATAIRERAEEL-RDRITGEIEELHERARRESAEQMKSAGErcdalVKA 1162
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2147 AKRAQAENAALKQKQQADAEMAKHK------KLAEQTLKQKFQVEQELTKvklkldETDKQKSVLDEELQRL----KDEV 2216
Cdd:NF041483 1163 AEEQLAEAEAKAKELVSDANSEASKvriaavKKAEGLLKEAEQKKAELVR------EAEKIKAEAEAEAKRTveegKREL 1236
|
970 980
....*....|....*....|....
gi 1927222988 2217 DDAVKQRGQVEEELLKVKVQMEEL 2240
Cdd:NF041483 1237 DVLVRRREDINAEISRVQDVLEAL 1260
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
164-265 |
1.64e-28 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 112.36 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 164 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED 242
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1927222988 243 VDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
166-261 |
1.97e-28 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 112.06 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 166 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED-VD 244
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1927222988 245 VPHPDEKSIITYVSSLY 261
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1364-1983 |
2.51e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 126.20 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1364 KAEEQKKMAMMQAELDK--------QKQLAEVHAKAiAKAEKeAQELKLRMQE---EVNRREDAVVDAEKQKHNIQLELH 1432
Cdd:COG1196 174 KEEAERKLEATEENLERledilgelERQLEPLERQA-EKAER-YRELKEELKEleaELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1433 ELKNLSEQ-QIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQ 1511
Cdd:COG1196 252 EAELEELEaELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1512 VNEETQKKRMAEEELKRKAEAekeaakqkqkaLEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELqskh 1591
Cdd:COG1196 332 LEELEEELEELEEELEEAEEE-----------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA---- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1592 msfvEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDA 1671
Cdd:COG1196 397 ----ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1672 EKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEqQRSLLEDELYRLKNE 1751
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY-EAALEAALAAALQNI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1752 VVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAE- 1830
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAr 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1831 -EEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKK 1909
Cdd:COG1196 632 lEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1910 sSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKAssgkLDLELELNKLKNIAEETQQSK---------------LRA 1974
Cdd:COG1196 712 -AEEERLEEELEEEALEEQLEAEREELLEELLEEEEL----LEEEALEELPEPPDLEELERElerlereiealgpvnLLA 786
|
....*....
gi 1927222988 1975 EEEAEKLRK 1983
Cdd:COG1196 787 IEEYEELEE 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1791-2466 |
2.90e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.82 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1791 SERSKQL--LEVEATKmrdlAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAisdaTRLKTEAEIALKEK 1868
Cdd:COG1196 196 GELERQLepLERQAEK----AERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA----ELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1869 EAENERLRRQAEDEAYQRK-ALEDQANQHKQQIEEKI-VLLKKSSEAEMERQRAivddtlkqrrvvEEEIRILKLNFEKA 1946
Cdd:COG1196 268 ELEELRLELEELELELEEAqAEEYELLAELARLEQDIaRLEERRRELEERLEEL------------EEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1947 SSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKK 2026
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2027 AEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAAL 2106
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2107 LRQQAEEAE---RQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAqAENAALKQKQQADAEMAKHKKLAEQTLKQKFQ 2183
Cdd:COG1196 496 LLEAEADYEgflEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA-ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2184 VEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKL-RIEEENQRLIKKDKDNT 2262
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALrRAVTLAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2263 QKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQ 2342
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2343 AQklLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKlKLQ----VSQLSEAQAKAQEEAKKFkkqadsiasrlh 2418
Cdd:COG1196 735 EE--LLEELLEEEELLEEEALEELPEPPDLEELERELERLER-EIEalgpVNLLAIEEYEELEERYDF------------ 799
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1927222988 2419 eteLATQekmtvVEKLEVARltsskeaDDLRKAIADLEKEKSRLKKEA 2466
Cdd:COG1196 800 ---LSEQ-----REDLEEAR-------ETLEEAIEEIDRETRERFLET 832
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1507-2223 |
4.59e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.43 E-value: 4.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1507 KLRKqvnEETQKK-RMAEEELKRkaeaekeaakqkqkaLED--------LENLKRQAEEAERQVKQAEIEKERQIQV--- 1574
Cdd:COG1196 171 KERK---EEAERKlEATEENLER---------------LEDilgelerqLEPLERQAEKAERYRELKEELKELEAELlll 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1575 ------AHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKAN 1648
Cdd:COG1196 233 klreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1649 EALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLR 1728
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1729 ADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDvliqlkskaeketmsnsERSKQLLEVEATKMRDL 1808
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE-----------------EEEEALEEAAEEEAELE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1809 AEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKA 1888
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1889 LEDqanqhkqqieekivllkkssEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSgkldlELELNKLKNIAEETQ 1968
Cdd:COG1196 536 YEA--------------------ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT-----FLPLDKIRARAALAA 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1969 QSKLRAEEEAEKLRKLALEEEKRRREAEEKVkkiaaaeeeaarqRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMA 2048
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDT-------------LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2049 QQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQ 2128
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2129 AKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKK---LAeqtlkqkfqvEQELTKVKLKLDETDKQKSVL 2205
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnlLA----------IEEYEELEERYDFLSEQREDL 807
|
730 740
....*....|....*....|.
gi 1927222988 2206 DEELQRLKD---EVDDAVKQR 2223
Cdd:COG1196 808 EEARETLEEaieEIDRETRER 828
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1831-2611 |
5.14e-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: 5.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1831 EEAA------RQRAEAERilkeKLAAISDA-TRLkteaEIALKEKEAENERLRRQAEdEAYQRKALEDQANQHKQQIeek 1903
Cdd:TIGR02168 162 EEAAgiskykERRKETER----KLERTRENlDRL----EDILNELERQLKSLERQAE-KAERYKELKAELRELELAL--- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1904 IVLLKKSSEAEMERQRAIVDDTLKQRR-------VVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEE 1976
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEeltaelqELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1977 EAEKLRKlaleeekrrreaeeKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCS 2056
Cdd:TIGR02168 310 RLANLER--------------QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2057 AAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAE 2136
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2137 RLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQE----LTKVKLKLD----------ETDKQK 2202
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkaLLKNQSGLSgilgvlseliSVDEGY 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2203 S-----VLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLA 2277
Cdd:TIGR02168 536 EaaieaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2278 ----------------EDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAI---QEASRLRAEAEMLQRQKDL 2338
Cdd:TIGR02168 616 kalsyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILerrREIEELEEKIEELEEKIAE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2339 AQEQAQKLLEDkqlmQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLH 2418
Cdd:TIGR02168 696 LEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2419 ETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKsKEMADAQQKQIEHEKTVLQQTfLSE 2498
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLEEQ-IEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2499 KEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELER 2578
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1927222988 2579 K--RLEQER-----ILAEENQKLREKLQQLEEAQKDQPDK 2611
Cdd:TIGR02168 930 RleGLEVRIdnlqeRLSEEYSLTLEEAEALENKIEDDEEE 969
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1672-2363 |
8.68e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 124.28 E-value: 8.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1672 EKQKEEAEREAKK----RAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYR 1747
Cdd:COG1196 199 ERQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1748 LKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEketmsnsERSKQLLEVEATKMRDLAEEASKLRAIAEEakhqrq 1827
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELE-------ERLEELEEELAELEEELEELEEELEELEEE------ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1828 vaEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEkivll 1907
Cdd:COG1196 346 --LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER----- 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1908 KKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALE 1987
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1988 EEKRRREAEEKVKKiaAAEEEAARQRQAAQDELDRLKKKAEEARkqkddadkEAEKQILMAQQAAQKCSAAEQQVqsvla 2067
Cdd:COG1196 499 AEADYEGFLEGVKA--ALLLAGLRGLAGAVAVLIGVEAAYEAAL--------EAALAAALQNIVVEDDEVAAAAI----- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2068 qqkedtimqtklkeEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAErqkaaaeqeaanqakaqEDAERLRKEAEFEAA 2147
Cdd:COG1196 564 --------------EYLKAAKAGRATFLPLDKIRARAALAAALARGAI-----------------GAAVDLVASDLREAD 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2148 KRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVE 2227
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2228 EELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAArlrqIAEDDLNQQRAL 2307
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL----PEPPDLEELERE 768
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 2308 ADKmLKEKMQ--------AIQEASRLRAEAEMLQRQK-DLaqEQAQKLLEDkqlMQQRLDEETEE 2363
Cdd:COG1196 769 LER-LEREIEalgpvnllAIEEYEELEERYDFLSEQReDL--EEARETLEE---AIEEIDRETRE 827
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1669-2596 |
3.13e-27 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 122.77 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1669 EDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRaDFDNAEQQRSLLEDELYRL 1748
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALE-YYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1749 KNEVVaaQQQRKQLEDELAKVRSEMDVLIQLKSKAEKEtmsnSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQV 1828
Cdd:pfam02463 231 YLKLN--EERIDLLQELLRDEQEEIESSKQEIEKEEEK----LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1829 AEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEaENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLK 1908
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELK-ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1909 KSSEAEMERQRaivddtlKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEE 1988
Cdd:pfam02463 384 ERLSSAAKLKE-------EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1989 EKRRREAEEKVKKIAAAEEeaarqrqaaqdeldrLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQ 2068
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLK---------------ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2069 QKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEaak 2148
Cdd:pfam02463 522 GRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE--- 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2149 RAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEE 2228
Cdd:pfam02463 599 IDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEI 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2229 ELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKfLAKEADNMKklaedaarlsveaqeaARLRQIAEDDLNQQRALA 2308
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKK-LKLEAEELL----------------ADRVQEAQDKINEELKLL 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2309 DKMLKEKMQAIQEASRLRAEAEMLQRQkdlaQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQ 2388
Cdd:pfam02463 742 KQKIDEEEEEEEKSRLKKEEKEEEKSE----LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2389 VSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAED 2468
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE 897
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2469 LQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKL 2548
Cdd:pfam02463 898 EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNL 977
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1927222988 2549 QATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQErilaEENQKLRE 2596
Cdd:pfam02463 978 MAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIE----ETCQRLKE 1021
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
24-148 |
3.95e-27 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 109.08 E-value: 3.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 24 DEGYYQGMLKAMdgrKDERDRVQKKTFTKWVNKHLIKSQRQV--TDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFH 100
Cdd:cd21247 2 DTEYEKGHIRKL---QEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVH 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1927222988 101 KLQNVQIALDFLKHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21247 79 FLENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
44-149 |
4.92e-27 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 108.96 E-value: 4.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 44 RVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLKHRQVKLV 120
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1927222988 121 NIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1394-2223 |
8.16e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 121.32 E-value: 8.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1394 KAEKEAQELKL-RMQEEVNRREDAVVDAEKQKHNIQL------ELHELKN-LSEQQIMDKSKQVDDALQSRVKIEEEIRL 1465
Cdd:TIGR02168 171 KERRKETERKLeRTRENLDRLEDILNELERQLKSLERqaekaeRYKELKAeLRELELALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1466 IRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAkqkqkalE 1545
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE-------A 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1546 DLENLKRQAEEAERQVkqAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQ 1625
Cdd:TIGR02168 324 QLEELESKLDELAEEL--AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1626 QEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAE-DSALKQKEMAENELE 1704
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEElREELEEAEQALDAAE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1705 RQrkvaESTAQQKLTAEQELIR--------LRADFDNAEQQR-------SLLE-DELY----------RLKNEVVAAQQQ 1758
Cdd:TIGR02168 482 RE----LAQLQARLDSLERLQEnlegfsegVKALLKNQSGLSgilgvlsELISvDEGYeaaieaalggRLQAVVVENLNA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1759 RKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLR----------AIAEEAKHQRQV 1828
Cdd:TIGR02168 558 AKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvLVVDDLDNALEL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1829 AEEEAARQR---AEAERILKEKL----AAISDATRLKTEAEIA--------LKEKEAENERLRRQAEDEAYQRKALEDQA 1893
Cdd:TIGR02168 638 AKKLRPGYRivtLDGDLVRPGGVitggSAKTNSSILERRREIEeleekieeLEEKIAELEKALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1894 NQHKQQIEEKIVLLKKS---SEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQS 1970
Cdd:TIGR02168 718 RKELEELSRQISALRKDlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1971 KLRAEEEAEKLRKlaleeekrrreaeeKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQ 2050
Cdd:TIGR02168 798 LKALREALDELRA--------------ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2051 AAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKaaaeqeAANQAK 2130
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL------EGLEVR 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2131 AQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQ 2210
Cdd:TIGR02168 938 IDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
890
....*....|....*.
gi 1927222988 2211 RLK---DEVDDAVKQR 2223
Cdd:TIGR02168 1018 TLEeaiEEIDREARER 1033
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
148-263 |
1.62e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 107.09 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 148 ISDIQIngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGV 227
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222988 228 AERDLGVTRLLDPED-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 |
1.64e-26 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 106.42 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 44 RVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 120
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1927222988 121 NIRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
146-263 |
1.95e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 107.09 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 146 FQISDIQIngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAF 225
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1927222988 226 GVAERDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2019-2607 |
3.44e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 119.27 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2019 ELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQsvlAQQKEDTIMQtklKEEYEKAKKLAkQAEAAKE 2098
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE---ELELELEEAQ---AEEYELLAELA-RLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2099 KAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTL 2178
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2179 KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKD 2258
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2259 KDNTQKFLAKEAdnmkklAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDL 2338
Cdd:COG1196 466 AELLEEAALLEA------ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2339 AQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLH 2418
Cdd:COG1196 540 LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2419 ETELATQEkmtVVEKLEVARLTSSKEADDLRKAIADLE-----KEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQ 2493
Cdd:COG1196 620 DTLLGRTL---VAARLEAALRRAVTLAGRLREVTLEGEggsagGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2494 TFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEM 2573
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
570 580 590
....*....|....*....|....*....|....*..
gi 1927222988 2574 KELER---KRLEQERILAEENQKLREKLQQLEEAQKD 2607
Cdd:COG1196 777 EALGPvnlLAIEEYEELEERYDFLSEQREDLEEARET 813
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1350-2300 |
1.37e-25 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 117.38 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1350 QRRLEDEEKAAEKL--KAEEQKKMAMMQAELDKQKQLAEVH-----AKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEK 1422
Cdd:pfam02463 153 ERRLEIEEEAAGSRlkRKKKEALKKLIEETENLAELIIDLEelklqELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1423 QKHNIQLELHELKNLSEQQIMDKSKQVDDalqsrvKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQ 1502
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIE------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1503 EEAEKLRKQVNEETQKKRMAEEELKRkaeaeKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKS 1582
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKK-----EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1583 AAAELQSKHMSFVEKTSKLEESLKQehgavlqlQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAH 1662
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKE--------AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1663 KKslaqEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKltAEQELIRLRADFDNAEQQRSLLE 1742
Cdd:pfam02463 454 EK----QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESK--ARSGLKVLLALIKDGVGGRIISA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1743 DELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEA 1822
Cdd:pfam02463 528 HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1823 KHQRQVAEEEAARQRAEAERILKEKlaaisdatrLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEE 1902
Cdd:pfam02463 608 LDKATLEADEDDKRAKVVEGILKDT---------ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEI 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1903 KIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKldLELELNKLKNIAEETQQSKLRAEEEAEKLR 1982
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR--VQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1983 KlaleeekrrreaeekvKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKcsAAEQQV 2062
Cdd:pfam02463 757 L----------------KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKE--EAELLE 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2063 QSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEA 2142
Cdd:pfam02463 819 EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEE 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2143 EFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQ--TLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAv 2220
Cdd:pfam02463 899 KKELEEESQKLNLLEEKENEIEERIKEEAEILLKyeEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNL- 977
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2221 KQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQeaARLRQIAEDD 2300
Cdd:pfam02463 978 MAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGS--AELRLEDPDD 1055
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
164-263 |
4.21e-25 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 102.36 E-value: 4.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 164 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED- 242
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1927222988 243 VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1672-2467 |
9.75e-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: 114.77 E-value: 9.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1672 EKQKEEAER----EAKKRAKAEDSALKQKEMAENELERQRKVAEStaqqkltAEQELIRLRADFDNAEQQRSLLEDELYR 1747
Cdd:TIGR02168 206 ERQAEKAERykelKAELRELELALLVLRLEELREELEELQEELKE-------AEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1748 LKNEVVAAQQqrkqledelakvrsEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKlRAIAEEAKHQRQ 1827
Cdd:TIGR02168 279 LEEEIEELQK--------------ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK-LDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1828 VAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQ----HKQQIEEK 1903
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERledrRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1904 IVLLKKSSEAEMERQRAIVD-------DTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEE 1976
Cdd:TIGR02168 424 EELLKKLEEAELKELQAELEeleeeleELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1977 EAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAE-------------- 2042
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNElgrvtflpldsikg 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2043 -----------KQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAE--------------AAK 2097
Cdd:TIGR02168 584 teiqgndreilKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdlvrpggvITG 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2098 EKAEREAALLRQQAE--EAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAE 2175
Cdd:TIGR02168 664 GSAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2176 QTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKvqmEELLKLKLRIEEENQRLI 2255
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR---EALDELRAELTLLNEEAA 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2256 KK--DKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQ 2333
Cdd:TIGR02168 821 NLreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2334 RQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKsLEAERKRQLEIIAESEKLKLQ-----VSQLSEAQAKAQEEAKKFKK 2408
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLEeaealENKIEDDEEEARRRLKRLEN 979
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222988 2409 QADsiasRLHETELATQEKMtvvEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAE 2467
Cdd:TIGR02168 980 KIK----ELGPVNLAAIEEY---EELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAR 1031
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1715-2606 |
1.11e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.38 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1715 QQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQrKQLEDELAKVRSEMDVLiQLKSKAEKEtmsnsERS 1794
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVL-RLEELREEL-----EEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1795 KQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAArqraEAERILKEKLAAISDATRLKTEAEIALKEKEAENER 1874
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE----ELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1875 LRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKkSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLE 1954
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELE-SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1955 LELNKLKNIAEETQQSKLRAEEEAEKLRKlaleeekrrreaeekvkkiaAAEEEAARQRQAAQDELDRLKKKAEEARKQK 2034
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLK--------------------KLEEAELKELQAELEELEEELEELQEELERL 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2035 DDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAqqkedtiMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEA 2114
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLD-------SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2115 ERQKaaaeqeaanqaKAQEDAERLRKEA----EFEAAKRAQAenaALKQKQQADAEM-----AKHKKLAEQTLKQKFQVE 2185
Cdd:TIGR02168 533 EGYE-----------AAIEAALGGRLQAvvveNLNAAKKAIA---FLKQNELGRVTFlpldsIKGTEIQGNDREILKNIE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2186 QELTkVKLKLDETDKQ-KSVLDEELQRLK--DEVDDAVKQRGQVEEELLKVKVQMEELLK----LKLRIEEENQRLikkd 2258
Cdd:TIGR02168 599 GFLG-VAKDLVKFDPKlRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLDGDLVRPggviTGGSAKTNSSIL---- 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2259 kdNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDL 2338
Cdd:TIGR02168 674 --ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2339 AQEQAQKLLEDKQLMQQRLDEETEEYQkslEAERKRQleiiaeseklklqvsQLSEAQAKAQEEAKKFKKQADSIASRLH 2418
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELA---EAEAEIE---------------ELEAQIEQLKEELKALREALDELRAELT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2419 ETELATQEKMTVVEKLEvarltssKEADDLRKAIADLEKEKSRLKKEAEDLqnkSKEMADAQQKQIEHEKTVlqQTFLSE 2498
Cdd:TIGR02168 814 LLNEEAANLRERLESLE-------RRIAATERRLEDLEEQIEELSEDIESL---AAEIEELEELIEELESEL--EALLNE 881
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2499 KEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQA------------------TMDAALNKQK 2560
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevridnlqerlseeyslTLEEAEALEN 961
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1927222988 2561 EAEKEMHNKQKEMKELERKR-------LEQERILAEENQKLREKLQQLEEAQK 2606
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
148-263 |
1.89e-24 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 101.34 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 148 ISDIQIngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGV 227
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222988 228 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1673-2572 |
3.77e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 112.84 E-value: 3.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1673 KQKEEAEReakKRAKAEDsALKQKEMAENELERQRKVAESTAQQKltaeQELIRLRADFDNAEQQRSL-----LEDELYR 1747
Cdd:TIGR02168 172 ERRKETER---KLERTRE-NLDRLEDILNELERQLKSLERQAEKA----ERYKELKAELRELELALLVlrleeLREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1748 LKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKEtmsnserskqlLEVEATKMRDLAEEASKLRAIAEEAKHQRQ 1827
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1828 VAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLL 1907
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1908 KKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLale 1987
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE--- 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1988 eekrrreaeekvkkiaaaeeeaarqrqAAQDELDRLKKKAEEARKQkddADKEAEKQILMAQQAAQKCSAAEQQVQSVLA 2067
Cdd:TIGR02168 470 ---------------------------LEEAEQALDAAERELAQLQ---ARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2068 QQKEDTIMQTKLKEEYEKA----------------KKLAKQAEAAKEKAE--REAALLRQQAEEAERQKAAAEQEAANQA 2129
Cdd:TIGR02168 520 GILGVLSELISVDEGYEAAieaalggrlqavvvenLNAAKKAIAFLKQNElgRVTFLPLDSIKGTEIQGNDREILKNIEG 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2130 KAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKK-------LAEQTLKQKFQVEQELTKVKLKLDETDKQK 2202
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRpgyrivtLDGDLVRPGGVITGGSAKTNSSILERRREI 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2203 SVLDEELQRLKDEVDDAVKQRGQVEEELLkvkvQMEELLKLKLRIEEENQRLIkkdkDNTQKFLAKEADNMKKLAEDAAR 2282
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELE----ELEEELEQLRKELEELSRQI----SALRKDLARLEAEVEQLEERIAQ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2283 LSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKL---LEDKQLMQQRLDE 2359
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLER 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2360 ETEEYQKSLEaERKRQLEIIAES-EKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVAR 2438
Cdd:TIGR02168 832 RIAATERRLE-DLEEQIEELSEDiESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2439 LTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNK-SKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLE 2517
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 2518 SqfEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDaalnkqkEAEKEMHNKQKE 2572
Cdd:TIGR02168 991 A--IEEYEELKERYDFLTAQKEDLTEAKETLEEAIE-------EIDREARERFKD 1036
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
160-266 |
6.93e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 99.28 E-value: 6.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 160 MTAKEKLLLWSQRMTDGY-QGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVY--RQTNLENLEQAFGVAERDLGVTR 236
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1927222988 237 -LLDPEDVDvpHPDEKSIITYVSSLYDAMPR 266
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
166-261 |
8.31e-24 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 98.76 E-value: 8.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 166 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED-VD 244
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1927222988 245 VPHPDEKSIITYVSSLY 261
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
164-264 |
8.72e-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: 8.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 164 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPEDV 243
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1927222988 244 DVPHPDEKSIITYVSSLYDAM 264
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
161-265 |
8.89e-24 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 98.71 E-value: 8.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQRMTDGYqGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDP 240
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1927222988 241 EDVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
48-145 |
1.02e-23 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 98.16 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 48 KTFTKWVNKHLIKSQRQ-VTDLYEDLRDGHNLISLLEVLSGETLPREK---GRMRFHKLQNVQIALDFLKHRQVKLVNIR 123
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPpVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1927222988 124 NDDIADGnPKLTLGLIWTIILH 145
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1830-2608 |
1.37e-23 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 110.83 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1830 EEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQAnqhkqqiEEKIVLLKK 1909
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA-------KKALEYYQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1910 SSEAEMERQRAIVDDTLKqrrvveEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQS-KLRAEEEAEKLRKLALEE 1988
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLK------LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVlKENKEEEKEKKLQEEELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1989 EKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQ 2068
Cdd:pfam02463 290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2069 QKEDTIMqTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAK 2148
Cdd:pfam02463 370 QLEEELL-AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2149 RAQAEN--AALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVldEELQRLKDEVDDAVKQRGQV 2226
Cdd:pfam02463 449 EKEELEkqELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKAR--SGLKVLLALIKDGVGGRIIS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2227 EEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRA 2306
Cdd:pfam02463 527 AHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2307 LADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLK 2386
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAE 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2387 LQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEA 2466
Cdd:pfam02463 687 SELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2467 EDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKK 2546
Cdd:pfam02463 767 SELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQ 846
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 2547 KLQatmdaalnkqKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQ 2608
Cdd:pfam02463 847 KLE----------KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEE 898
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1831-2493 |
4.46e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.87 E-value: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1831 EEAA------RQRAEAERilkeKLAAISDatRLkTEAEIALKEKEAENERLRRQAED-EAYQrkALEDQANQHKQQIeek 1903
Cdd:COG1196 162 EEAAgiskykERKEEAER----KLEATEE--NL-ERLEDILGELERQLEPLERQAEKaERYR--ELKEELKELEAEL--- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1904 IVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKassgkldLELELNKLKNIAEETQQSKLRAEEEAEKLRK 1983
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE-------LRLELEELELELEEAQAEEYELLAELARLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1984 laleeekrrreaeekvkkiaaaeeeaarqrqaaqdELDRLKKKAEEARKQKDDADKEAEkqilmaqQAAQKCSAAEQQVQ 2063
Cdd:COG1196 303 -----------------------------------DIARLEERRRELEERLEELEEELA-------ELEEELEELEEELE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2064 SVLAQQKEdtimqtkLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAE 2143
Cdd:COG1196 341 ELEEELEE-------AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2144 FEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVkqr 2223
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA--- 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2224 gQVEEELLKVKVQMEELLK-LKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLN 2302
Cdd:COG1196 491 -ARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2303 QQRAL----ADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEI 2378
Cdd:COG1196 570 KAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2379 IAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKE 2458
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
650 660 670
....*....|....*....|....*....|....*
gi 1927222988 2459 KSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQ 2493
Cdd:COG1196 730 LEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
148-263 |
5.29e-23 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 97.07 E-value: 5.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 148 ISDIQIngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGV 227
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1927222988 228 AERDLGVTRLLDPED-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 |
8.67e-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: 95.82 E-value: 8.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 45 VQKKTFTKWVNKHLIKSQ--RQVTDLYEDLRDGHNLISLLEVLSGETLP-REKGRMRFHKLQNVQIALDFLKHRQ-VKLV 120
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1927222988 121 NIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
161-261 |
1.13e-22 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 95.57 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERdLGVTRLLDP 240
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1927222988 241 EDV---DVphPDEKSIITYVSSLY 261
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
794-860 |
2.11e-22 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 93.10 E-value: 2.11e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222988 794 QLKPRN--PTHSIkgklPIQAVCDFKQQEITVHKGDECALLNNSQPFKWKVLNRSGHEAVVPSVCFMVP 860
Cdd:pfam17902 1 PLKQRRspVTRPI----PVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
44-149 |
6.84e-22 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 94.38 E-value: 6.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 44 RVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 120
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1927222988 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 |
9.94e-22 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 93.61 E-value: 9.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 44 RVQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 120
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1927222988 121 NIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
162-261 |
3.10e-21 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 91.47 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 162 AKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPE 241
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1927222988 242 D-VDVPHPDEKSIITYVSSLY 261
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1156-2046 |
3.12e-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: 3.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1156 DSLEAELKKATAVSDKMSRvhsERDAELDHYRQLLSSLQDRWKAVFSQIDLRQRELEQLGRQLgyyresydwlirwinda 1235
Cdd:TIGR02168 203 KSLERQAEKAERYKELKAE---LRELELALLVLRLEELREELEELQEELKEAEEELEELTAEL----------------- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1236 kqrqekiqavtitdsKTLKEQLAQEKKLLEEVEgnkDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLASPLKKTkld 1315
Cdd:TIGR02168 263 ---------------QELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL--- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1316 sasdniiqeyvtlrtkyselmtltsqyikfitdsQRRLEDEEKAAEKLKAEEqkkmAMMQAELDKQKQLAEVHAKAIAKA 1395
Cdd:TIGR02168 322 ----------------------------------EAQLEELESKLDELAEEL----AELEEKLEELKEELESLEAELEEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1396 EKEAQELKLRM---QEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQQIMDKSKQVDDALQSRVKIEE-EIRLIRLQLE 1471
Cdd:TIGR02168 364 EAELEELESRLeelEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELE 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1472 TTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMaeeelkrkaeaekeaakqkqkaLEDLENLK 1551
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS----------------------LERLQENL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1552 RQAEEAERQVKQAEIEKERQIQVA----HVAAQKSAAAE------LQSKHMSFVEKTSKLEESLKQ-EHGAVLQL----- 1615
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVLseliSVDEGYEAAIEaalggrLQAVVVENLNAAKKAIAFLKQnELGRVTFLpldsi 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1616 -QHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRL----------QAEEEAHKKSLAQEDAEKQKEEAERE--- 1681
Cdd:TIGR02168 582 kGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvvddldNALELAKKLRPGYRIVTLDGDLVRPGgvi 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1682 AKKRAKAEDSAL-KQKEMAenELERQRKVAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRK 1760
Cdd:TIGR02168 662 TGGSAKTNSSILeRRREIE--ELEEKIEELEEKIAE---LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1761 QLEDELAKVRSEMDVLIQLKSKAEKETMSNSERskqlLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEA 1840
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1841 ERiLKEKLAaisDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEE------KIVLLKKSSEAE 1914
Cdd:TIGR02168 813 TL-LNEEAA---NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleseleALLNERASLEEA 888
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1915 MERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNiAEETQQSKLRAEE--EAEKLRKLALEEEKRR 1992
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV-RIDNLQERLSEEYslTLEEAEALENKIEDDE 967
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 1927222988 1993 REAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADkEAEKQIL 2046
Cdd:TIGR02168 968 EEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLT-EAKETLE 1020
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
161-260 |
2.45e-20 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 88.69 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERdLGVTRLLDP 240
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1927222988 241 ED-VDVPHPDEKSIITYVSSL 260
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
161-261 |
4.39e-20 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 88.17 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDP 240
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1927222988 241 EDVDV--PHPDEKSIITYVSSLY 261
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
165-262 |
2.16e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 86.25 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 165 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLD-PEDV 243
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1927222988 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 ... |
1552-2606 |
3.41e-19 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 96.40 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1552 RQAEEAERQVKQAEIEKERQIQVAhvaaqkSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAAL--KKQQEDA 1629
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAE------SELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLaaRKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1630 ERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAER---EAKKRAKAEDSALKqkEMAENELERQ 1706
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvttEAKIKKLEEDILLL--EDQNSKLSKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1707 RKVAE---STAQQKLTAEQELIRLRADFDNaeQQRSLLEDELYRLKNEVVAAQQQRK---QLEDELAKVRSEMdvlIQLK 1780
Cdd:pfam01576 154 RKLLEeriSEFTSNLAEEEEKAKSLSKLKN--KHEAMISDLEERLKKEEKGRQELEKakrKLEGESTDLQEQI---AELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1781 SKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKH----QRQVAEEEAARQRAEAE-RILKEKLAAisdat 1855
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQiselQEDLESERAARNKAEKQrRDLGEELEA----- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1856 rLKTEAEIALKEKEAENErLRRQAEDEAYQ-RKALEDQANQHKQQIEEkivLLKKSSEAEMERQRAIvddtlkqrrvveE 1934
Cdd:pfam01576 304 -LKTELEDTLDTTAAQQE-LRSKREQEVTElKKALEEETRSHEAQLQE---MRQKHTQALEELTEQL------------E 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1935 EIRILKLNFEKAssgKLDLELELNKLKNIAEETQQSKLRAEEEAEKLrklaleeekrrreaEEKVKKIAAAEEEAARQRQ 2014
Cdd:pfam01576 367 QAKRNKANLEKA---KQALESENAELQAELRTLQQAKQDSEHKRKKL--------------EGQLQELQARLSESERQRA 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2015 AAQDELDRLKKKAEEARKQKDDADKEAEKqilmaqqAAQKCSAAEQQVQSVLAQQKEDT----IMQTKLKEEYEKAKKLA 2090
Cdd:pfam01576 430 ELAEKLSKLQSELESVSSLLNEAEGKNIK-------LSKDVSSLESQLQDTQELLQEETrqklNLSTRLRQLEDERNSLQ 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2091 KQAE---AAKEKAEREAALLRQQAEEAERqkaaaeqeaanqaKAQEDAERLrkEAEFEAAKRAQAENAALKQKQQADAEM 2167
Cdd:pfam01576 503 EQLEeeeEAKRNVERQLSTLQAQLSDMKK-------------KLEEDAGTL--EALEEGKKRLQRELEALTQQLEEKAAA 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2168 AkhkklaEQTLKQKFQVEQELTKVKLKLDETDKQKSVLdEELQRLKDEV---DDAVKQRGQVEEELLKVKVQMEELLKLK 2244
Cdd:pfam01576 568 Y------DKLEKTKNRLQQELDDLLVDLDHQRQLVSNL-EKKQKKFDQMlaeEKAISARYAEERDRAEAEAREKETRALS 640
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2245 LRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAAR-LRQIAEDDLNQQRALADKMlkekmQAIQEAs 2323
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRaLEQQVEEMKTQLEELEDEL-----QATEDA- 714
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2324 RLRAEAEM----LQRQKDLAQEQAQKLLEDKQLMQQRLDEETEeyqksLEAERKRQLEIIAESEKLKLQVSQLS---EAQ 2396
Cdd:pfam01576 715 KLRLEVNMqalkAQFERDLQARDEQGEEKRRQLVKQVRELEAE-----LEDERKQRAQAVAAKKKLELDLKELEaqiDAA 789
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2397 AKAQEEA----KKFKKQADSIASRLHETELATQEKmtvveklevarLTSSKEADdlrKAIADLEKEKSRLKkeaEDLQnk 2472
Cdd:pfam01576 790 NKGREEAvkqlKKLQAQMKDLQRELEEARASRDEI-----------LAQSKESE---KKLKNLEAELLQLQ---EDLA-- 850
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2473 skeMADAQQKQIEHEKTVLQQTF---LSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDekkklq 2549
Cdd:pfam01576 851 ---ASERARRQAQQERDELADEIasgASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQ------ 921
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222988 2550 atmdaaLNKQKEAEKEMHNKQkemkELERKRLEQErilaeeNQKLREKLQQLEEAQK 2606
Cdd:pfam01576 922 ------LTTELAAERSTSQKS----ESARQQLERQ------NKELKAKLQEMEGTVK 962
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1362-2115 |
9.92e-19 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 94.65 E-value: 9.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1362 KLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELKNL--SE 1439
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAlqQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1440 QQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKStAESELKQLRDRAAEAEKL--RKAAQEEAEKLRKQVNEETQ 1517
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEA-VLEETQERINRARKAAPLaaHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1518 KKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEI---EKERQIQVAH----VAAQKSAAAELQSK 1590
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSireISCQQHTLTQhihtLQQQKTTLTQKLQS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1591 HMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQ--KANEAL------RLRLQAEEEAH 1662
Cdd:TIGR00618 398 LCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQceKLEKIHlqesaqSLKEREQQLQT 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1663 KKSLAQEDAEKQKEEAEReaKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLE 1742
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLAR--LLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSER 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1743 DELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAeea 1822
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL--- 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1823 kHQRQVAEEEAarqraeaerilKEKLAaisdatrLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQiee 1902
Cdd:TIGR00618 633 -HLQQCSQELA-----------LKLTA-------LHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE--- 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1903 KIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILklnfekaSSGKLDLELE---LNKLKNIAEETQQSKLRAEEEAE 1979
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS-------SSLGSDLAARedaLNQSLKELMHQARTVLKARTEAH 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1980 KLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELdrlkkKAEEARKQKDDADKEAEKQILMAQQaaqkcsaaE 2059
Cdd:TIGR00618 764 FNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTL-----EAEIGQEIPSDEDILNLQCETLVQE--------E 830
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 2060 QQVQSVLAQQKEDTIMQTKLKEEYEKAKKlaKQAEAAKEKAEreaalLRQQAEEAE 2115
Cdd:TIGR00618 831 EQFLSRLEEKSATLGEITHQLLKYEECSK--QLAQLTQEQAK-----IIQLSDKLN 879
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
46-146 |
1.36e-18 |
|
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: 83.79 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 46 QKKTFTKWVNKHLIKS--QRQVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQVKLVN 121
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1927222988 122 IRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1757-2604 |
1.41e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 94.36 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1757 QQRKQLEDELAKVrSEMDVLIQlKSKAEKETMS-NSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAAR 1835
Cdd:TIGR02169 153 VERRKIIDEIAGV-AEFDRKKE-KALEELEEVEeNIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1836 QRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAL-EDQANQHKQQIEEkivllkksSEAE 1914
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGE--------LEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1915 MERQRAIVDDTLKQRRVVEEEIRILklnfekassgkldlELELNKLKNIAEEtqqskLRAEEEAEKLRKLALEEEKRRRE 1994
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKL--------------EAEIDKLLAEIEE-----LEREIEEERKRRDKLTEEYAELK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1995 AEEKvkKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTI 2074
Cdd:TIGR02169 364 EELE--DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2075 MQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAER---QKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQ 2151
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKelsKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2152 AENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKV--------------------KLKLDETDKQKSVLDEELQR 2211
Cdd:TIGR02169 522 GVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKeaiellkrrkagratflplnKMRDERRDLSILSEDGVIGF 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2212 LKDEVDDAVKQRGQVeEELLKVKVQMEEL-----LKLKLRIEEENQRLIKKDKDNTQKFLAKE--ADNMKKLAEDAARLS 2284
Cdd:TIGR02169 602 AVDLVEFDPKYEPAF-KYVFGDTLVVEDIeaarrLMGKYRMVTLEGELFEKSGAMTGGSRAPRggILFSRSEPAELQRLR 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2285 VEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQkdlaQEQAQKLLEDKQLMQQRLDEETEEY 2364
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE----EEKLKERLEELEEDLSSLEQEIENV 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2365 QKSLEAERKRQLEIIAESEKLKLQVSQL--SEAQAKAQE---EAKKFKKQADSIASRLHETELATQEKMTVVEKLEvarl 2439
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEiqaELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE---- 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2440 tssKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMadaQQKQIEHEKTVLqqtflsekemllkkeklieeekkrlesQ 2519
Cdd:TIGR02169 833 ---KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL---EEELEELEAALR---------------------------D 879
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2520 FEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEEN--QKLREK 2597
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELslEDVQAE 959
|
....*..
gi 1927222988 2598 LQQLEEA 2604
Cdd:TIGR02169 960 LQRVEEE 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1131-1891 |
1.56e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 94.35 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1131 VKEVETYRTKLKKMRAEAEGEQPVFDSLEAELKKATAVSDKMSRVHSERDAELDHYRQLLSSLQDRWKAVFSQIDLRQRE 1210
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1211 LEQLGRQLGYYRESYDWLIRWINDAKQRQEKIQAVTITDSKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKD 1290
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1291 YELQLVAYKAQVEPLASplKKTKLDSASDNIIQEYVTLRTKYSELMtltsqyikfITDSQRRLEDEEKAAEKLKAEEqkk 1370
Cdd:TIGR02168 391 LELQIASLNNEIERLEA--RLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEEL--- 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1371 mAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLR------MQEEVNRREDAVVDAEKQKHNIQLELHELKNLSE----- 1439
Cdd:TIGR02168 457 -ERLEEALEELREELEEAEQALDAAERELAQLQARldslerLQENLEGFSEGVKALLKNQSGLSGILGVLSELISvdegy 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1440 ------------QQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTA---------ESELKQLRDRAAEAEKLR 1498
Cdd:TIGR02168 536 eaaieaalggrlQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGndreilkniEGFLGVAKDLVKFDPKLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1499 KAAQ------------EEAEKLRKQVNEE---------------------------TQKKRMAEEELKRKAEAEKEAAKQ 1539
Cdd:TIGR02168 616 KALSyllggvlvvddlDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELEEKIAE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1540 KQKALEDLENLKRQAEEAERQVKQAEIEKERQIqvahvaaqksaaaelqskhmsfvektSKLEESLKQEHGAVLQLQHEA 1619
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQI--------------------------SALRKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1620 AALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMA 1699
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1700 ENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQL 1779
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1780 KSKAEKETMS-NSERSKQLLEVEATKMRdLAEEASKLRA----IAEEAKHQRQVAEEEAARQRAEAERiLKEKLAAISDA 1854
Cdd:TIGR02168 910 RSELRRELEElREKLAQLELRLEGLEVR-IDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPV 987
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1927222988 1855 TRLkteaeiALKEKEAENER---LRRQAEDEAYQRKALED 1891
Cdd:TIGR02168 988 NLA------AIEEYEELKERydfLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1695-2607 |
1.83e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 93.98 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1695 QKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLL----EDELYRLKNEVVAAQQQRKQLEDELAKVR 1770
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1771 SEMDVLIQLKSKAEKEtmsnSERSKQLLEVEATKMRDLAEEasklraiaEEAKHQRQVAEEEAarQRAEAERILKEKLAA 1850
Cdd:TIGR02169 251 EELEKLTEEISELEKR----LEEIEQLLEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1851 ISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQAnqhkqqieekivllkKSSEAEMERQRAIVDDtlkqrr 1930
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY---------------AELKEELEDLRAELEE------ 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1931 vVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRklaleeekrrreaeekvkkiaaaeeeaa 2010
Cdd:TIGR02169 376 -VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN---------------------------- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2011 rqrqaaqDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQsvlaqqkedtimqtKLKEEYEKAKKla 2090
Cdd:TIGR02169 427 -------AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY--------------DLKEEYDRVEK-- 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2091 KQAEAAKEKAEREAAllRQQAEEAERQKAAAEQEAANQAK------AQEDAERLRKEAEFEAAKRAQAENAALKQKQQAD 2164
Cdd:TIGR02169 484 ELSKLQRELAEAEAQ--ARASEERVRGGRAVEEVLKASIQgvhgtvAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAK 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2165 A--EMAKHKKLAEQT---LKQKFQVEQELTKVKLK--------LDETDKQ-----KSVLDEELqrLKDEVDDAVKQRGQV 2226
Cdd:TIGR02169 562 EaiELLKRRKAGRATflpLNKMRDERRDLSILSEDgvigfavdLVEFDPKyepafKYVFGDTL--VVEDIEAARRLMGKY 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2227 -----EEELLK---------VKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAAR 2292
Cdd:TIGR02169 640 rmvtlEGELFEksgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2293 LRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRA---------EAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEE 2363
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEnvkselkelEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAE 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2364 YQKsLEAERKRQLEIIAESE----KLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEvarl 2439
Cdd:TIGR02169 800 LSK-LEEEVSRIEARLREIEqklnRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE---- 874
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2440 tsskeaddlrKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQK---QIEHEKTVLQQTflsekemllkkeklieeeKKRL 2516
Cdd:TIGR02169 875 ----------AALRDLESRLGDLKKERDELEAQLRELERKIEEleaQIEKKRKRLSEL------------------KAKL 926
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2517 ESQFEEEVKKAKALKDEQERQKQQM-----EDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRleqeRILAEEN 2591
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEEELsledvQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKR----AKLEEER 1002
|
970
....*....|....*.
gi 1927222988 2592 QKLREKLQQLEEAQKD 2607
Cdd:TIGR02169 1003 KAILERIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1419-2389 |
1.88e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 93.98 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1419 DAEKQKHNIQLELHElKNLSEQQIM--DKSKQVDDALQSRVKIEE--EIRLIRLQLETT--VKQKSTAESELKQLRDRAA 1492
Cdd:TIGR02169 169 DRKKEKALEELEEVE-ENIERLDLIidEKRQQLERLRREREKAERyqALLKEKREYEGYelLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1493 EAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALE-DLENLKRQAEEAERQVKQAEieKERQ 1571
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELEDAE--ERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1572 IQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEAL 1651
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1652 RLRLQAEEEAHKKSLAQEDAekqkeeaeREAKKRAKAEDSALK-QKEMAENELERQRKVAESTAQQKLTAEQELIRLRAD 1730
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADL--------NAAIAGIEAKINELEeEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1731 FDNaeqqrslLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLiqlksKAEKETMSNSERskQLLEVEatkmrdlaE 1810
Cdd:TIGR02169 478 YDR-------VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVL-----KASIQGVHGTVA--QLGSVG--------E 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1811 EASKLRAIAEEAKHQRQVAEEEAARQRAEAerILKEKlaAISDATRLKTEAeiaLKEKEAENERLRRQ-AEDEAYQRKAL 1889
Cdd:TIGR02169 536 RYATAIEVAAGNRLNNVVVEDDAVAKEAIE--LLKRR--KAGRATFLPLNK---MRDERRDLSILSEDgVIGFAVDLVEF 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1890 EDQ-ANQHKQQIEEKIVLlkksseAEMERQRAIVDdtlkQRRVVEEEIRIlklnFEKASSgkldLELELNKLKNIAEETQ 1968
Cdd:TIGR02169 609 DPKyEPAFKYVFGDTLVV------EDIEAARRLMG----KYRMVTLEGEL----FEKSGA----MTGGSRAPRGGILFSR 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1969 QSKLRAEEEAEKLRKLaleeekrrreaeekvkkiaaaeeeaARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMA 2048
Cdd:TIGR02169 671 SEPAELQRLRERLEGL-------------------------KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2049 QQAAQKcsaaEQQVQSVLAQQKEDtimQTKLKEEYEKAKklAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQ 2128
Cdd:TIGR02169 726 EQLEQE----EEKLKERLEELEED---LSSLEQEIENVK--SELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI 796
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2129 AKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDEtdkqksvLDEE 2208
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE-------LEEE 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2209 LQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEaDNMKKLAEDAARLSVEAQ 2288
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE-EELSEIEDPKGEDEEIPE 948
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2289 EAARLRQIAEDDLNQQRALaDKMLKEKMQAIQEAsrlraeAEMLQRQKDLaqeqaqklledkqlmqqrldeetEEYQKSL 2368
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEI-RALEPVNMLAIQEY------EEVLKRLDEL-----------------------KEKRAKL 998
|
970 980
....*....|....*....|.
gi 1927222988 2369 EAERKRQLEIIAESEKLKLQV 2389
Cdd:TIGR02169 999 EEERKAILERIEEYEKKKREV 1019
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
164-260 |
2.07e-18 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 83.13 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 164 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTN----LENLEQAFGVAERDLGVTRLLD 239
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1927222988 240 PEDVDVPHPDEKSIITYVSSL 260
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2266-2614 |
3.07e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.08 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2266 LAKEAdnmkKLAEDAARLSVEAQEA-ARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQ 2344
Cdd:COG1196 205 LERQA----EKAERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2345 KLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELAT 2424
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2425 QEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQtflsekemllk 2504
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA----------- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2505 keklieeekkrlESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQE 2584
Cdd:COG1196 430 ------------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350
....*....|....*....|....*....|
gi 1927222988 2585 RILAEENQKLREKLQQLEEAQKDQPDKEVI 2614
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
47-144 |
1.10e-17 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 81.23 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 47 KKTFTKWVNKHL-IKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQV-KLVNI 122
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1927222988 123 RNDDI-ADGNPKLTLGLIWTIIL 144
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
161-259 |
1.10e-17 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 81.13 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQRMTDGYqgiRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVY-RQTNLENLEQAFGVAERDLGVTRLLD 239
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1927222988 240 PEDVDVPHPDEKSIITYVSS 259
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1181-1767 |
4.01e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1181 AELDHYRQLLSSLQDRW-----KAVFSQIDLRQRELEQLGRQLgyyresydwlirwindaKQRQEKIQavtitdskTLKE 1255
Cdd:COG1196 220 EELKELEAELLLLKLREleaelEELEAELEELEAELEELEAEL-----------------AELEAELE--------ELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1256 QLAQEKKLLEEVEGNkdkvdecqkyakayidtikdyELQLVAYKAQVEplasplkkTKLDSASDNIIQEYVTLRTKYSEL 1335
Cdd:COG1196 275 ELEELELELEEAQAE---------------------EYELLAELARLE--------QDIARLEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1336 MTLTSQyikfitdsQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRRED 1415
Cdd:COG1196 326 AELEEE--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1416 AVVDAEKQKHNIQLELHELKNLSEQQImDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAE 1495
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELE-ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1496 KLRKAAQEEAEKLRKQvnEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQVA 1575
Cdd:COG1196 477 AALAELLEELAEAAAR--LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1576 HVAAQKSAAAELQSKH---MSFVEKTSKLEESLKQ---EHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANE 1649
Cdd:COG1196 555 DDEVAAAAIEYLKAAKagrATFLPLDKIRARAALAaalARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1650 ALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRa 1729
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE- 713
|
570 580 590
....*....|....*....|....*....|....*...
gi 1927222988 1730 dfdnAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELA 1767
Cdd:COG1196 714 ----EERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
163-261 |
4.47e-17 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 80.03 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 163 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED 242
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1927222988 243 -VDVPHPDEKSIITYVSSLY 261
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
157-262 |
4.56e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 79.61 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 157 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTR 236
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1927222988 237 LLDPEDV-DVPHPDEKSIITYVSSLYD 262
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
161-260 |
5.12e-17 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 79.51 E-value: 5.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERdLGVTRLLDP 240
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1927222988 241 ED-VDVPHPDEKSIITYVSSL 260
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1361-2118 |
7.75e-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: 7.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1361 EKLKAEEQKKMammqaeldkQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELknlsEQ 1440
Cdd:TIGR02169 206 EREKAERYQAL---------LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI----EQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1441 QIMDKSKQVDDALQSR-VKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKK 1519
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEqLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1520 RMAEEELKrkaeaekeaakqkqkaledlenlKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTS 1599
Cdd:TIGR02169 353 DKLTEEYA-----------------------ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1600 KLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAE 1679
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1680 REAKkRAKAEDSALKQkemAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAeqqrslLEDEL-YRLKNEVVA---- 1754
Cdd:TIGR02169 490 RELA-EAEAQARASEE---RVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATA------IEVAAgNRLNNVVVEddav 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1755 AQQQRKQLEDE---------LAKVRSE----------------MDvLIQLKSKAEKE---------TMSNSERSKQL--- 1797
Cdd:TIGR02169 560 AKEAIELLKRRkagratflpLNKMRDErrdlsilsedgvigfaVD-LVEFDPKYEPAfkyvfgdtlVVEDIEAARRLmgk 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1798 -----LEVE------ATKMRDLAEEASKLRAIAEEAKHQRQVAEEEA--------ARQRAEAERILKEKLAAISDATR-- 1856
Cdd:TIGR02169 639 yrmvtLEGElfeksgAMTGGSRAPRGGILFSRSEPAELQRLRERLEGlkrelsslQSELRRIENRLDELSQELSDASRki 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1857 --LKTEAEIALKEKEAENERLRRQAEDEAYQRKALE------DQANQHKQQIEEKIVLLKKS---------------SEA 1913
Cdd:TIGR02169 719 geIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEnvkselKELEARIEELEEDLHKLEEAlndlearlshsripeIQA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1914 EMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNiaeetQQSKLRAEEEAEKLRKLALEEEkrrr 1993
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE-----QIKSIEKEIENLNGKKEELEEE---- 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1994 eaeekVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKED- 2072
Cdd:TIGR02169 870 -----LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDe 944
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 2073 ----------TIMQTKLK----------------EEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQK 2118
Cdd:TIGR02169 945 eipeeelsleDVQAELQRveeeiralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1346-2253 |
1.19e-16 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 87.92 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1346 ITDSQRRLEDEEKAAEKLKAE---------------------------EQKKMAMMQAELDKQKQLAEVHAKAIAKAEKE 1398
Cdd:pfam01576 105 IQDLEEQLDEEEAARQKLQLEkvtteakikkleedillledqnsklskERKLLEERISEFTSNLAEEEEKAKSLSKLKNK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1399 AQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELKnlseQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKS 1478
Cdd:pfam01576 185 HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ----EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1479 TAESELKQLRDRAAEAEK---LRKAAQEEAEKLRKQVNEETQKKRMaeeELKRKAEAEKEAAKQKQKALEDLENLKRQAE 1555
Cdd:pfam01576 261 NALKKIRELEAQISELQEdleSERAARNKAEKQRRDLGEELEALKT---ELEDTLDTTAAQQELRSKREQEVTELKKALE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1556 EaERQVKQAEIEKERQiqvahvaAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREE 1635
Cdd:pfam01576 338 E-ETRSHEAQLQEMRQ-------KHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1636 AEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENEL--ERQRKVAEST 1713
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLqeETRQKLNLST 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1714 AQQKLTAEQEliRLRADFDNAEQQRSLLEDELYRLKNEVvaaQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSER 1793
Cdd:pfam01576 490 RLRQLEDERN--SLQEQLEEEEEAKRNVERQLSTLQAQL---SDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEK 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1794 SKQLLEVEATKMRdLAEEaskLRAIAEEAKHQRQVAEEEAARQRaEAERILKEKLAAISDATRLKTEAEIALKEKEAENE 1873
Cdd:pfam01576 565 AAAYDKLEKTKNR-LQQE---LDDLLVDLDHQRQLVSNLEKKQK-KFDQMLAEEKAISARYAEERDRAEAEAREKETRAL 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1874 RLRRQAEDEAYQRKALEDQANQHKQQIEEkIVLLKKS---SEAEMERQRAIVDDTLKQRRVVEEEiriLKLNFEKASSGK 1950
Cdd:pfam01576 640 SLARALEEALEAKEELERTNKQLRAEMED-LVSSKDDvgkNVHELERSKRALEQQVEEMKTQLEE---LEDELQATEDAK 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1951 LDLELELNKLKNIAEETQQSKlraEEEAEKLRKLALEEEKRRREAEEKVKKiaaAEEEAARQRQAAQDELDRLKKKAEEA 2030
Cdd:pfam01576 716 LRLEVNMQALKAQFERDLQAR---DEQGEEKRRQLVKQVRELEAELEDERK---QRAQAVAAKKKLELDLKELEAQIDAA 789
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2031 RKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDT---------IMQtkLKEEYEKAKKLAKQAEAAK---- 2097
Cdd:pfam01576 790 NKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEkklknleaeLLQ--LQEDLAASERARRQAQQERdela 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2098 --------------EKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQA 2163
Cdd:pfam01576 868 deiasgasgksalqDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQN 947
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2164 DAEMAKHKKLaEQTLKQKFQ-----VEQELTKVKLKLDETDKQKSVLDEELQR----LKD---EVDDAVKQRGQVEEELL 2231
Cdd:pfam01576 948 KELKAKLQEM-EGTVKSKFKssiaaLEAKIAQLEEQLEQESRERQAANKLVRRtekkLKEvllQVEDERRHADQYKDQAE 1026
|
970 980
....*....|....*....|..
gi 1927222988 2232 KVKVQMEELLKLKLRIEEENQR 2253
Cdd:pfam01576 1027 KGNSRMKQLKRQLEEAEEEASR 1048
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
163-266 |
1.53e-16 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 78.17 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 163 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED 242
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1927222988 243 VDV--PHPDEKSIITYVSSLYDAMPR 266
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
163-262 |
2.14e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 77.70 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 163 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED 242
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1927222988 243 VDV--PHPDEKSIITYVSSLYD 262
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2020-2613 |
4.43e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 86.26 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2020 LDRLKKKAEEARKQKDDADKEAEKqilmAQQAAQKcSAAEQQVQ-SVLAQQKEDtimqtkLKEEYEKAKKLAKQAEAAKE 2098
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEK----AERYKEL-KAELRELElALLVLRLEE------LREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2099 KAEREAALLRQQAEEAERQKAAAEQEAANQAK----AQEDAERLRKEAEFEAAKRAQAENaalkQKQQADAEMAKHKKLA 2174
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKelyaLANEISRLEQQKQILRERLANLER----QLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2175 EQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRL 2254
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2255 iKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAE-DDLNQQRALADKMLKEKMQAIQEA--------SRL 2325
Cdd:TIGR02168 413 -EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEElERLEEALEELREELEEAEQALDAAerelaqlqARL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2326 RAEAEMLQRQKDLAQEQAQKLLEDKQLMQQR-----LDEETEEYQKSLEA---------------ERKRQLEIIAESEKL 2385
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSGLSGILgvlseLISVDEGYEAAIEAalggrlqavvvenlnAAKKAIAFLKQNELG 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2386 KLQVSQL----------SEAQAKAQEE------------AKKFKK----------------QADSIASRLH--------- 2418
Cdd:TIGR02168 572 RVTFLPLdsikgteiqgNDREILKNIEgflgvakdlvkfDPKLRKalsyllggvlvvddldNALELAKKLRpgyrivtld 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2419 ---------------ETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQ----NKSKEMADA 2479
Cdd:TIGR02168 652 gdlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkeleELSRQISAL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2480 QQKQIEHEKTVlqQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQ 2559
Cdd:TIGR02168 732 RKDLARLEAEV--EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222988 2560 KEA---EKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQPDKEV 2613
Cdd:TIGR02168 810 AELtllNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
163-264 |
6.66e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 76.66 E-value: 6.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 163 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED 242
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1927222988 243 -VDVPHPDEKSIITYVSSLYDAM 264
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
165-262 |
8.32e-16 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 76.07 E-value: 8.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 165 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLD-PEDV 243
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1927222988 244 DVPHPDEKSIITYVSSLYD 262
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1130-1787 |
1.18e-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: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1130 DVKEVETYRTKLKKMRAEAEgeqpvfdSLEAELKKATAVSDKMSRVHSERDAELDHYRQLLSSLQDrwkavfsQIDLRQR 1209
Cdd:COG1196 223 KELEAELLLLKLRELEAELE-------ELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------ELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1210 ELEQLGRQlgyyresydwLIRWINDAKQRQEKIQAVtitdSKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIK 1289
Cdd:COG1196 289 EEYELLAE----------LARLEQDIARLEERRREL----EERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1290 DYELQLVAYKAQVEplasplkktKLDSASDNIIQEYVTLRTKYSELMTLTSQYIKFITDSQRRLEDEEKAAEKLKAEEQk 1369
Cdd:COG1196 355 EAEAELAEAEEALL---------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1370 kmAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQQIMDKSKQV 1449
Cdd:COG1196 425 --ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1450 DDALQSRVKIEEEIRLIRLQLEttvkqkstaesELKQLRDRAAEAEKLrkAAQEEAEKLRKQVNEETQKKRMAEEELKRk 1529
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAG-----------AVAVLIGVEAAYEAA--LEAALAAALQNIVVEDDEVAAAAIEYLKA- 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1530 aeaekeaakqkqkalEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEH 1609
Cdd:COG1196 569 ---------------AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1610 GAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAE 1689
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1690 DSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVA-------------AQ 1756
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllaieeyeEL 793
|
650 660 670
....*....|....*....|....*....|..
gi 1927222988 1757 QQRKQ-LEDELAKVRSEMDVLIQLKSKAEKET 1787
Cdd:COG1196 794 EERYDfLSEQREDLEEARETLEEAIEEIDRET 825
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
43-142 |
1.83e-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: 75.26 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 43 DRVQKKTFTKWVNKHLIKSQ-RQVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFL-KHRQV 117
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIeEDLKI 81
|
90 100
....*....|....*....|....*
gi 1927222988 118 KLVNIRNDDIADGNPKLTLGLIWTI 142
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
46-146 |
2.97e-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: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 46 QKKTFTKWVNKHLIK--SQRQVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMRfhklQNVQIALDFLKHRQV 117
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1927222988 118 KLVNIRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1461-2267 |
4.08e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 83.09 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1461 EEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKrkaeaekeaakqk 1540
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELK------------- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1541 qkaledlenlkrQAEEAERQVKQAEIEKERQIQVAhvaaqksaaaelqskhmsfvEKTSKLEESLKQEHGAVLQLQHEAA 1620
Cdd:TIGR00618 230 ------------HLREALQQTQQSHAYLTQKREAQ--------------------EEQLKKQQLLKQLRARIEELRAQEA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1621 ALKKQQedaerareeaeKELEKWRQKANEAlrlrlqaeeeAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMA- 1699
Cdd:TIGR00618 278 VLEETQ-----------ERINRARKAAPLA----------AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKq 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1700 ENELERQRKVaestaQQKLTAEQELIRlradfDNAEQQRSLLE--DELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLI 1777
Cdd:TIGR00618 337 QSSIEEQRRL-----LQTLHSQEIHIR-----DAHEVATSIREisCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1778 QLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAkhQRQVAEEEAARQRAEAERILKEKLAAISDATRL 1857
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA--QCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1858 KTE---AEIALKEKEAENERL--RRQAEDEAYQRKALEDQANQHK-QQIEEKIVLLKKsseaEMERQRAIVDDTLKQRRV 1931
Cdd:TIGR00618 485 ETRkkaVVLARLLELQEEPCPlcGSCIHPNPARQDIDNPGPLTRRmQRGEQTYAQLET----SEEDVYHQLTSERKQRAS 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1932 VEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQsKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAAR 2011
Cdd:TIGR00618 561 LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD-LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2012 QRQAAQDELDRLKKK-AEEARKQKDDADKEAEKQILMAQQAAQKcsAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLA 2090
Cdd:TIGR00618 640 ELALKLTALHALQLTlTQERVREHALSIRVLPKELLASRQLALQ--KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYD 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2091 KQAEaakekaEREAALLRQQAEEAERqkaaAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALK---QKQQADAEM 2167
Cdd:TIGR00618 718 REFN------EIENASSSLGSDLAAR----EDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgaELSHLAAEI 787
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2168 AKHKKLAEQTLKQKFQVEQEL-TKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKV---KVQMEELLKL 2243
Cdd:TIGR00618 788 QFFNRLREEDTHLLKTLEAEIgQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYeecSKQLAQLTQE 867
|
810 820 830
....*....|....*....|....*....|.
gi 1927222988 2244 KLRIEEE-------NQRLIKKDKDNTQKFLA 2267
Cdd:TIGR00618 868 QAKIIQLsdklngiNQIKIQFDGDALIKFLH 898
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1331-2115 |
5.53e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 82.53 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1331 KYSELMTLTSQYIKFITDSQRRLEDEEKA---AEKLKAEEQKKMAMMQAEL-DKQKQLAEVHAKaIAKAEKEAQELKLRM 1406
Cdd:pfam01576 174 KAKSLSKLKNKHEAMISDLEERLKKEEKGrqeLEKAKRKLEGESTDLQEQIaELQAQIAELRAQ-LAKKEEELQAALARL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1407 QEEVNRREDAVvdaeKQKHNIQLELHELKNLSEQQIMDKSKqvddALQSRVKIEEEIRLIRLQLETTVkQKSTAESELKQ 1486
Cdd:pfam01576 253 EEETAQKNNAL----KKIRELEAQISELQEDLESERAARNK----AEKQRRDLGEELEALKTELEDTL-DTTAAQQELRS 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1487 LRDRaaEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLE--NLKRQAEEAERQVKQA 1564
Cdd:pfam01576 324 KREQ--EVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALEseNAELQAELRTLQQAKQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1565 EIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKEL-EKW 1643
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLqEET 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1644 RQKANEALRLR-----------LQAEEEAHKKSLAQE---------DAEKQKE------EAEREAKKRAKAEDSALKQ-- 1695
Cdd:pfam01576 482 RQKLNLSTRLRqledernslqeQLEEEEEAKRNVERQlstlqaqlsDMKKKLEedagtlEALEEGKKRLQRELEALTQql 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1696 --KEMAENELERQRK-------------------VAESTAQQK----LTAEQELIRLRA--DFDNAEQQRSLLEDELYRL 1748
Cdd:pfam01576 562 eeKAAAYDKLEKTKNrlqqelddllvdldhqrqlVSNLEKKQKkfdqMLAEEKAISARYaeERDRAEAEAREKETRALSL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1749 KNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKeTMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAK----- 1823
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGK-NVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKlrlev 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1824 -------------HQRQVAEEEAARQRA----EAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQR 1886
Cdd:pfam01576 721 nmqalkaqferdlQARDEQGEEKRRQLVkqvrELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1887 KALEDQANQHKQQIEE------KIVLLKKSS-------EAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDL 1953
Cdd:pfam01576 801 KKLQAQMKDLQRELEEarasrdEILAQSKESekklknlEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1954 ELELNKLK----NIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKvkkiaaaeEEAARQRQAAQDELDRLKKKAEE 2029
Cdd:pfam01576 881 QDEKRRLEariaQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAE--------RSTSQKSESARQQLERQNKELKA 952
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2030 ARKQKDDADKEAEKQILMAQQAaqKCSAAEQQvqsvLAQQKEDTIMQTKLKEEYEKAKKLA--------KQAEAAKEKAE 2101
Cdd:pfam01576 953 KLQEMEGTVKSKFKSSIAALEA--KIAQLEEQ----LEQESRERQAANKLVRRTEKKLKEVllqvederRHADQYKDQAE 1026
|
890
....*....|....*..
gi 1927222988 2102 REAALLRQ---QAEEAE 2115
Cdd:pfam01576 1027 KGNSRMKQlkrQLEEAE 1043
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4034-4072 |
6.49e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.20 E-value: 6.49e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1927222988 4034 LLEAQIATGGIIDPEESHRVPVEVAYKRGFFDEEMNEIL 4072
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
166-261 |
8.16e-15 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 73.55 E-value: 8.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 166 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAErDLGVTRLLDPED-VD 244
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1927222988 245 VPHPDEKSIITYVSSLY 261
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2317-2626 |
1.01e-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: 81.32 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2317 QAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEdkQLMQQRLDEETEEyqKSLEAERKRQLEiiaESEK-----LKLQVSQ 2391
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFE--KMEQERLRQEKEE--KAREVERRRKLE---EAEKarqaeMDRQAAI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2392 LSEAQAKAQEEAKKFKK----QADSIASRLHETELATQ-EKMTVVEKLEVARLTSS----KEADDLRKaIADLEKEKSR- 2461
Cdd:pfam17380 336 YAEQERMAMERERELERirqeERKRELERIRQEEIAMEiSRMRELERLQMERQQKNervrQELEAARK-VKILEEERQRk 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2462 LKKEAEDLQNKSKEMADAQQKQIEhektVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQM 2541
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEARQREVR----RLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2542 EDEKKKLQATMDA-------ALNKQKEAEKEMHNKQKEMKELERKRL------------------EQERILAEENQKL-- 2594
Cdd:pfam17380 491 EQRRKILEKELEErkqamieEERKRKLLEKEMEERQKAIYEEERRREaeeerrkqqemeerrriqEQMRKATEERSRLea 570
|
330 340 350
....*....|....*....|....*....|....*.
gi 1927222988 2595 ----REKLQQLEEAQKDQPDKEVihVTMVETTKNVY 2626
Cdd:pfam17380 571 mereREMMRQIVESEKARAEYEA--TTPITTIKPIY 604
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1281-1928 |
1.11e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 81.50 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1281 AKAYIDTIKDYELQLVAYKAQVEPLAsPLKKTKldsasdniiQEYVTLRTKYSELMTLtsqyikfitDSQRRLEDEEKAA 1360
Cdd:COG4913 230 LVEHFDDLERAHEALEDAREQIELLE-PIRELA---------ERYAAARERLAELEYL---------RAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1361 EKLKAEEQKkmamMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDavvDAEKQKHNIQLELHELKNLSEQ 1440
Cdd:COG4913 291 ELLEAELEE----LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE---QLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1441 QimdkSKQVDDALQSRVKIEEEIRLIRLQLETTVKQkstAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNE-ETQKK 1519
Cdd:COG4913 364 L----EALLAALGLPLPASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIASlERRKS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1520 RMAEEELKRkaeaekeaakqkqkaledLENLKRQAEEAER---------QVKQAE------IEK---------------- 1568
Cdd:COG4913 437 NIPARLLAL------------------RDALAEALGLDEAelpfvgeliEVRPEEerwrgaIERvlggfaltllvppehy 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1569 ------------ERQIQVAHVAAQKSAAAELQSKHMSFVEK-TSK-------LEESLKQEHGAVL-----QLQHEAAALK 1623
Cdd:COG4913 499 aaalrwvnrlhlRGRLVYERVRTGLPDPERPRLDPDSLAGKlDFKphpfrawLEAELGRRFDYVCvdspeELRRHPRAIT 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1624 KQ-QEDAERAREeaekelEKWRQKA----------NEALRLRLQAEEEAHKKSLAQedAEKQKEEAEREAKKRAKAEDSA 1692
Cdd:COG4913 579 RAgQVKGNGTRH------EKDDRRRirsryvlgfdNRAKLAALEAELAELEEELAE--AEERLEALEAELDALQERREAL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1693 LKQKEMAENELErqrkvAESTAQQKLTAEQELIRLRADFDNAEQqrslLEDELYRLKNEVVAAQQQRKQLEDELAKVRSE 1772
Cdd:COG4913 651 QRLAEYSWDEID-----VASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1773 MDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKE-KLAAI 1851
Cdd:COG4913 722 LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWP 801
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222988 1852 SDATRLKTEAEiALKEKEAENERLRRQAEDEAYQR--KALEDQANQHKQQIEEKIvllkKSSEAEMERQRAIVDDTLKQ 1928
Cdd:COG4913 802 AETADLDADLE-SLPEYLALLDRLEEDGLPEYEERfkELLNENSIEFVADLLSKL----RRAIREIKERIDPLNDSLKR 875
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3720-3758 |
1.16e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.43 E-value: 1.16e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1927222988 3720 LLEAQAATGFIVDPVKNETLTVDEAVRKGIVGPEIHDKL 3758
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1207-1977 |
1.38e-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: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1207 RQRELEQLGRQLGYYRESYDWLIRW-IND-----AKQRQEKIQAVTITDSKTLKEQLAQEKklLEEVEGNKDKVDECQKY 1280
Cdd:TIGR02169 118 RLSEIHDFLAAAGIYPEGYNVVLQGdVTDfismsPVERRKIIDEIAGVAEFDRKKEKALEE--LEEVEENIERLDLIIDE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1281 AKAYIDTIKDYELQLVAYKAqveplaspLKKTKLDSASDNIIQEYVTLRTKYSELMTLTSQYIKFITDSQRRLEDEEK-- 1358
Cdd:TIGR02169 196 KRQQLERLRREREKAERYQA--------LLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKrl 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1359 --AAEKLKAEEQKKMAMMQAE-LDKQKQLAEVHAKaIAKAEKEAQELKLRMQeevnrredavvDAEKQKHNIQLELHELK 1435
Cdd:TIGR02169 268 eeIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAE-IASLERSIAEKERELE-----------DAEERLAKLEAEIDKLL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1436 nlseQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEE 1515
Cdd:TIGR02169 336 ----AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1516 TQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQ-------------------AEIEKER---QIQ 1573
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaadlskyeqelydlkeeyDRVEKELsklQRE 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1574 VAHVAAQKSAAAELQSkhmSFVEKTSKLEESLKQEHGAVLQL-----QH----EAAALKKQQEDAERAREEAEKELEKWR 1644
Cdd:TIGR02169 492 LAEAEAQARASEERVR---GGRAVEEVLKASIQGVHGTVAQLgsvgeRYataiEVAAGNRLNNVVVEDDAVAKEAIELLK 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1645 QK-------------ANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAER------------EAKKRAKAE------DSAL 1693
Cdd:TIGR02169 569 RRkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKyvfgdtlvvediEAARRLMGKyrmvtlEGEL 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1694 KQKEMAENELERQRKVAESTAQQKltaEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEM 1773
Cdd:TIGR02169 649 FEKSGAMTGGSRAPRGGILFSRSE---PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1774 DVLIQlKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAE--------RILK 1845
Cdd:TIGR02169 726 EQLEQ-EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelSKLE 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1846 EKLAAISDATRlktEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEkIVLLKKSSEAEMERQRAIVDDT 1925
Cdd:TIGR02169 805 EEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN-LNGKKEELEEELEELEAALRDL 880
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 1926 LKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEE 1977
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1772-2589 |
1.46e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 81.17 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1772 EMDVLIQLKSKAEKETMSNSERSKQLlEVEATKMRDLAEEA-SKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAA 1850
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQY-TQLALMEFAKKKSLhGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1851 ISDATRLKTEAEIALKEKEAENERLRRQ-------AEDEAY--QRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAI 1921
Cdd:TIGR00618 232 REALQQTQQSHAYLTQKREAQEEQLKKQqllkqlrARIEELraQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1922 VDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLkniaeETQQSKLRAEEEAEKLRKlaleeekrrreaeekvkk 2001
Cdd:TIGR00618 312 IHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTL-----HSQEIHIRDAHEVATSIR------------------ 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2002 iaaaeeeaaRQRQAAQDELDRLKKKAEEarKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKE 2081
Cdd:TIGR00618 369 ---------EISCQQHTLTQHIHTLQQQ--KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQ 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2082 EYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQ 2161
Cdd:TIGR00618 438 RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2162 QADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELL 2241
Cdd:TIGR00618 518 QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2242 KLKLRIEEENQRLIKKDKDNTQKfLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEdDLNQQRALADKMLKEKMQAIQE 2321
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRK-LQPEQDLQDVRLHLQQCSQELALKLTALHALQL-TLTQERVREHALSIRVLPKELL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2322 ASRLRAEAEMlqrqkdlaQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQ---LEIIAESEKLKLQVSQLSEAQAK 2398
Cdd:TIGR00618 676 ASRQLALQKM--------QSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNeieNASSSLGSDLAAREDALNQSLKE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2399 AQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMAD 2478
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2479 AQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFE--EEVKKAKALkdeqeRQKQQMEDEKKKLQATMDAAL 2556
Cdd:TIGR00618 828 QEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKiiQLSDKLNGI-----NQIKIQFDGDALIKFLHEITL 902
|
810 820 830
....*....|....*....|....*....|...
gi 1927222988 2557 NKQKEAEKEMHNKQKEMKELERKRLEQERILAE 2589
Cdd:TIGR00618 903 YANVRLANQSEGRFHGRYADSHVNARKYQGLAL 935
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1676-2406 |
2.63e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 80.34 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1676 EEAEREAKKrakaedsALKQKEMAENELERQRKVAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAA 1755
Cdd:COG4913 238 ERAHEALED-------AREQIELLEPIRELAERYAAARERL---AELEYLRAALRLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1756 QQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEE-ASKLRAIAEEAKHQRQVAEE--- 1831
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARlEALLAALGLPLPASAEEFAAlra 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1832 EAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAE--DEAYQ--RKALEDQANQHKQQIeeKIV-- 1905
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniPARLLalRDALAEALGLDEAEL--PFVge 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1906 LLK-KSSEAEME----------RQRAIVDDTLKQ--RRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAE--ETQQS 1970
Cdd:COG4913 466 LIEvRPEEERWRgaiervlggfALTLLVPPEHYAaaLRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGklDFKPH 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1971 KLRAEEEAEKLRKLALeeekrrreaeekvkkiaaaeeeaarQRQAAQDELDRLKK--------KAEEARKQKDDADKEAE 2042
Cdd:COG4913 546 PFRAWLEAELGRRFDY-------------------------VCVDSPEELRRHPRaitragqvKGNGTRHEKDDRRRIRS 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2043 KQILmAQQAAQKCSAAEQQVQsvlaqqkedtimqtKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAae 2122
Cdd:COG4913 601 RYVL-GFDNRAKLAALEAELA--------------ELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV-- 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2123 qeaanqakAQEDAERLRKEAEFEAAKRAQAENAALKQKQQadaemakhkklaeqtlkqkfQVEQELTKVKLKLDETDKQK 2202
Cdd:COG4913 664 --------ASAEREIAELEAELERLDASSDDLAALEEQLE--------------------ELEAELEELEEELDELKGEI 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2203 SVLDEELQRLKDEVDDAvkqRGQVEEELLKVKVQMEELLKLKLRiEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAAR 2282
Cdd:COG4913 716 GRLEKELEQAEEELDEL---QDRLEAAEDLARLELRALLEERFA-AALGDAVERELRENLEERIDALRARLNRAEEELER 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2283 L-----------------SVEAQE--AARLRQIAEDDLNQQRALADKMLKEkmQAIQEASRLRAEaemLQRQKDLAQEQA 2343
Cdd:COG4913 792 AmrafnrewpaetadldaDLESLPeyLALLDRLEEDGLPEYEERFKELLNE--NSIEFVADLLSK---LRRAIREIKERI 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2344 QKL---LEDKQ---------LMQQRLDEETEEYQKSL-EAERKRQLEIIAESEKLKLQVSQL-----SEAQAKAQEEAKK 2405
Cdd:COG4913 867 DPLndsLKRIPfgpgrylrlEARPRPDPEVREFRQELrAVTSGASLFDEELSEARFAALKRLierlrSEEEESDRRWRAR 946
|
.
gi 1927222988 2406 F 2406
Cdd:COG4913 947 V 947
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3387-3425 |
3.21e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 69.28 E-value: 3.21e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1927222988 3387 LLEAQAATGFMVDPVKKQCLSVDEAVKSGLVGPELHEKL 3425
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2027-2618 |
3.54e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 79.83 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2027 AEEARKQK--------DDADKEAEKQILMAQQAAQKCSAAEQQVQ-------SVLAQQKEDTIMQTKLKEEYE------- 2084
Cdd:pfam01576 114 EEEAARQKlqlekvttEAKIKKLEEDILLLEDQNSKLSKERKLLEeriseftSNLAEEEEKAKSLSKLKNKHEamisdle 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2085 ----KAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKaaaeqeaanqakAQEDAERLRKEAEFEAA-----KRAQAENA 2155
Cdd:pfam01576 194 erlkKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQI------------AELRAQLAKKEEELQAAlarleEETAQKNN 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2156 ALKQKQQADAEMAkhkklaeqtlkqkfQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDD-----AVKQ--RGQVEE 2228
Cdd:pfam01576 262 ALKKIRELEAQIS--------------ELQEDLESERAARNKAEKQRRDLGEELEALKTELEDtldttAAQQelRSKREQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2229 ELLKVKVQMEE--------LLKLKLR----IEEENQRL--IKKDKDNTQKF-LAKEADNmKKLAEDAARLSVEAQEAARL 2293
Cdd:pfam01576 328 EVTELKKALEEetrsheaqLQEMRQKhtqaLEELTEQLeqAKRNKANLEKAkQALESEN-AELQAELRTLQQAKQDSEHK 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2294 RQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDK-------QLMQQRLDEETEeyQK 2366
Cdd:pfam01576 407 RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVsslesqlQDTQELLQEETR--QK 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2367 SLEAERKRQLEiiaeSEKLKLQvSQLSEaqakaQEEAKK-FKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEA 2445
Cdd:pfam01576 485 LNLSTRLRQLE----DERNSLQ-EQLEE-----EEEAKRnVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2446 DDLRK-------AIADLEKEKSRLKKEAEDLQnkskeMADAQQKQI----EHEKTVLQQTFLSEKEMllkkEKLIEEEKK 2514
Cdd:pfam01576 555 EALTQqleekaaAYDKLEKTKNRLQQELDDLL-----VDLDHQRQLvsnlEKKQKKFDQMLAEEKAI----SARYAEERD 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2515 RLESQFEEEVKKAKALK---DEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHnkqkemkELERKRleqeRILAEEN 2591
Cdd:pfam01576 626 RAEAEAREKETRALSLAralEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVH-------ELERSK----RALEQQV 694
|
650 660
....*....|....*....|....*...
gi 1927222988 2592 QKLREKLQQLE-EAQKDQPDKEVIHVTM 2618
Cdd:pfam01576 695 EEMKTQLEELEdELQATEDAKLRLEVNM 722
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
161-258 |
4.99e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 70.87 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTN-LENLEQAFGVAERDLGVTRLLD 239
Cdd:cd21230 1 TPKQRLLGWIQ---NKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1927222988 240 PEDVDVPHPDEKSIITYVS 258
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1251-1822 |
5.39e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.34 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1251 KTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDYELQLvayKAQVEPLASPLKKTKLDSAsdnIIQEYVTLRT 1330
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL---EEKVKELKELKEKAEEYIK---LSEFYEEYLD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1331 KYSELMTLTSQYIKFITDSQRRLEDEEKAAEKLKaEEQKKMAMMQAELDKQKQLAEVHAKAIAKaEKEAQELKLRMQ-EE 1409
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAK-KEELERLKKRLTgLT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1410 VNRREDAVVDAEKQKHNIQLELHEL---KNLSEQQIMDKSKQVDDALQSRVKI---------EEEIRLIR---LQLETTV 1474
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKCpvcgrelteEHRKELLEeytAELKRIE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1475 KQKSTAESELKQLRDRAAEAEKLRKAaQEEAEKLRKQVNEetqkKRMAEEELKRKaeaekeaakqkqkaleDLENLKRQA 1554
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQ----LKELEEKLKKY----------------NLEELEKKA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1555 EEAERqVKQAEIEKERQIQVahVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGavlqlqheaaalkkqqedaerare 1634
Cdd:PRK03918 525 EEYEK-LKEKLIKLKGEIKS--LKKELEKLEELKKKLAELEKKLDELEEELAELLK------------------------ 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1635 eaekELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKvaesta 1714
Cdd:PRK03918 578 ----ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK------ 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1715 qqkltaeqELIRLRADFDNAEQQRslLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLiqlksKAEKETMSNSERS 1794
Cdd:PRK03918 648 --------ELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-----KEELEEREKAKKE 712
|
570 580
....*....|....*....|....*...
gi 1927222988 1795 KQLLEVEATKMRDLAEEASKLRAIAEEA 1822
Cdd:PRK03918 713 LEKLEKALERVEELREKVKKYKALLKER 740
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2341-2608 |
6.02e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2341 EQAQKLLEDkqlMQQRLD------EETEEYQKSLE-----AERKRQLEIIAESEKLKLQVSQLSEAQAK---AQEEAKKF 2406
Cdd:COG1196 175 EEAERKLEA---TEENLErledilGELERQLEPLErqaekAERYRELKEELKELEAELLLLKLRELEAEleeLEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2407 KKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEH 2486
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2487 EKTVLQQtfLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEM 2566
Cdd:COG1196 332 LEELEEE--LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1927222988 2567 HNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQ 2608
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2019-2614 |
7.97e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 78.86 E-value: 7.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2019 ELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLA-QQKEDTIMQTKLKEEYEKAKKLAKQAEAAK 2097
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQvLEKELKHLREALQQTQQSHAYLTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2098 EKAEREAALLRQQAEEAERQkaaaeQEAANQAKAQEDAERLRKEAefeaakRAQAENAALKQKQQADAEMAKHKKLAEQT 2177
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELR-----AQEAVLEETQERINRARKAA------PLAAHIKAVTQIEQQAQRIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2178 LKQKFQVEQELTKVKLKLDETDKqksvLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLikk 2257
Cdd:TIGR00618 323 RAKLLMKRAAHVKQQSSIEEQRR----LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKL--- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2258 dKDNTQKFLAKEADNMKKLAEDAARlSVEAQEAARLR---QIAEDDLNQQRALADKMLKEKMQAIQEASR----LRAEAE 2330
Cdd:TIGR00618 396 -QSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKkqqELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqsLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2331 MLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLeiIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQA 2410
Cdd:TIGR00618 474 QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQD--IDNPGPLTRRMQRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2411 DSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTV 2490
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2491 LQQTFLSEKEMLLKKEKLIEEekkrLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKE---MH 2567
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQ----LTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCqtlLR 707
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 2568 NKQKEMKELERKRLEQERILAEENQKL------------------REKLQQLEEAQKDQPDKEVI 2614
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSSLGSDLaaredalnqslkelmhqaRTVLKARTEAHFNNNEEVTA 772
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1902-2611 |
9.03e-14 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 78.22 E-value: 9.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1902 EKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASsgkLDLELELNKLKNIAEETQQS-------KLRA 1974
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVS---LKLEEEIQENKDLIKENNATrhlcnllKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1975 EEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEaarqrqaaqdeLDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQK 2054
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNIEKMILA-----------FEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2055 -CSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEaakEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQE 2133
Cdd:pfam05483 234 eINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE---EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2134 DAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLK 2213
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2214 DEVDDAVKQRGQVE---EELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEA 2290
Cdd:pfam05483 391 SELEEMTKFKNNKEvelEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2291 ARLRQIAEDDLNQQ------RALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLedKQLmqQRLDEETEEY 2364
Cdd:pfam05483 471 KEVEDLKTELEKEKlknielTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERML--KQI--ENLEEKEMNL 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2365 QKSLEAERKrqlEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKE 2444
Cdd:pfam05483 547 RDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2445 ADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKtvlqqtfLSEKEMLlkkeklieeekkrlesqfeEEV 2524
Cdd:pfam05483 624 GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK-------ISEEKLL-------------------EEV 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2525 KKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQK-EAEKEMHNKQKEMKELERKRLEQERI---LAEENQKLREKLQQ 2600
Cdd:pfam05483 678 EKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKhQYDKIIEERDSELGLYKNKEQEQSSAkaaLEIELSNIKAELLS 757
|
730
....*....|....
gi 1927222988 2601 LE---EAQKDQPDK 2611
Cdd:pfam05483 758 LKkqlEIEKEEKEK 771
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2080-2612 |
1.07e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 78.47 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2080 KEEYEKAKKLAKQAEAAKEK----AEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENA 2155
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELiidlEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2156 ALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLK-------DEVDDAVKQRGQVEE 2228
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLErrkvddeEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2229 ELLKVKVQMEELLKLKL---RIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQR 2305
Cdd:pfam02463 329 ELKKEKEEIEELEKELKeleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2306 ALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQA--QKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESE 2383
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLteEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2384 KLKLQVSQLSEAQA-KAQEEAKKFKKQADSIASRLHETELATQEKM-TVVEKLEVARLTSSKEADDLRKAIADLEKEKSR 2461
Cdd:pfam02463 489 LLSRQKLEERSQKEsKARSGLKVLLALIKDGVGGRIISAHGRLGDLgVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2462 LKKEAEDLQNK-----SKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQER 2536
Cdd:pfam02463 569 ALTELPLGARKlrlliPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGL 648
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 2537 QKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQPDKE 2612
Cdd:pfam02463 649 RKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
40-145 |
1.68e-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: 69.62 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 40 DERDrvqKKTFTKWVNKHLIKsqRQVTDLYEDLRDGhnlISLLEVL--------SGETLPREKGRMRFHKLQNVQIALDF 111
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLD--PLINNLYEDLRDG---LVLLQVLdkiqpgcvNWKKVNKPKPLNKFKKVENCNYAVDL 73
|
90 100 110
....*....|....*....|....*....|....
gi 1927222988 112 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 145
Cdd:cd21219 74 AKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
161-261 |
2.08e-13 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 69.72 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAErDLGVTRLLDP 240
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1927222988 241 ED-VDVPHPDEKSIITYVSSLY 261
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1114-1861 |
2.60e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 77.03 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1114 LKQYEDCLREVHTVPNDVKEVETYRTKLKKMRAEAEGE----QPVFDSLEAELKKAT-----AVSDKMSRVHSER---DA 1181
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRleeiEQLLEELNKKIKDLGeeeqlRVKEKIGELEAEIaslER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1182 ELDHYRQLLSSLQDRWKAVFSQIDLRQRELEQLGRQLGYYRESYDWLIRWINDAKQRQEKIQAVTITDSKTLKEQLAQEK 1261
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1262 KLLEEVEGNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLASplKKTKLDSASDNIIQEYVTLRTKYSELMTLTSQ 1341
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA--KINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1342 YIKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQK---------------------QLAEVHAKAIAKAEKEAQ 1400
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggraveevlkasiqgvhgtvaQLGSVGERYATAIEVAAG 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1401 ElklRMQEEVnrREDAVVDAE-----KQK----------HNIQLELHELKNLSEQQIMDKSKQV---DDALQSRVK---- 1458
Cdd:TIGR02169 547 N---RLNNVV--VEDDAVAKEaiellKRRkagratflplNKMRDERRDLSILSEDGVIGFAVDLvefDPKYEPAFKyvfg 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1459 -------IEEEIRL---IRL-QLETTVKQKSTA------------------ESELKQLRDRAAEAEKLRKAAQEEAEKLR 1509
Cdd:TIGR02169 622 dtlvvedIEAARRLmgkYRMvTLEGELFEKSGAmtggsraprggilfsrsePAELQRLRERLEGLKRELSSLQSELRRIE 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1510 KQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIqvAHVAAQKSAAAELQs 1589
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE--ARIEELEEDLHKLE- 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1590 khmsfvEKTSKLEESLKQEHgaVLQLQHEAAALKKQqedaeraREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQE 1669
Cdd:TIGR02169 779 ------EALNDLEARLSHSR--IPEIQAELSKLEEE-------VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1670 DAEKQKEEAERE---AKKRAKAEDSALKQKEMAENELerqrkvaestaqqkltaEQELIRLRADFDNAEQQRSLLEDELY 1746
Cdd:TIGR02169 844 DLKEQIKSIEKEienLNGKKEELEEELEELEAALRDL-----------------ESRLGDLKKERDELEAQLRELERKIE 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1747 RLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAE---KETMSNSERSKQLLEVEAtKMRDLaeEASKLRAIAEEAK 1823
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipEEELSLEDVQAELQRVEE-EIRAL--EPVNMLAIQEYEE 983
|
810 820 830
....*....|....*....|....*....|....*...
gi 1927222988 1824 HQRQVAEEEAARQRAEAERilKEKLAAISDATRLKTEA 1861
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEER--KAILERIEEYEKKKREV 1019
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2258-2584 |
2.69e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 76.70 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2258 DKDNTQKFLAKEADNMKKLAEDAARlsveaqEAARLRQIAEDD------LNQQRALADKMLKEKMQAIQEASRLRAEA-- 2329
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAR------EVERRRKLEEAEkarqaeMDRQAAIYAEQERMAMERERELERIRQEErk 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2330 -EMLQ-RQKDLAQEQAQ-KLLEDKQLMQQRldeETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKaQEEAKKF 2406
Cdd:pfam17380 360 rELERiRQEEIAMEISRmRELERLQMERQQ---KNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE-QEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2407 KKQADSiASRLHETELATQEKMTVVEKLEVARltsSKEADDLRKAIaDLEKEKsRLKKEAEDLQNK--SKEMADAQQKQI 2484
Cdd:pfam17380 436 EVRRLE-EERAREMERVRLEEQERQQQVERLR---QQEEERKRKKL-ELEKEK-RDRKRAEEQRRKilEKELEERKQAMI 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2485 EHEKtvlqQTFLSEKEMLLkkeklieeekkRLESQFEEEVKKakalKDEQERQKQQMEDEKKKLQATMDAALNKQK---- 2560
Cdd:pfam17380 510 EEER----KRKLLEKEMEE-----------RQKAIYEEERRR----EAEEERRKQQEMEERRRIQEQMRKATEERSrlea 570
|
330 340
....*....|....*....|....*
gi 1927222988 2561 -EAEKEMhnkQKEMKELERKRLEQE 2584
Cdd:pfam17380 571 mEREREM---MRQIVESEKARAEYE 592
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1770-2491 |
4.83e-13 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 76.42 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1770 RSEMDVLIQLKSKAEKETMSNSERSKQLL---EVEATKMRDLAEEASKLR-AIAEEA-------KHQRQVAEEEAARQRA 1838
Cdd:pfam12128 205 ILEDDGVVPPKSRLNRQQVEHWIRDIQAIagiMKIRPEFTKLQQEFNTLEsAELRLShlhfgykSDETLIASRQEERQET 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1839 EAE-----RILKEKLAAISDATRL-KTEAEIALKEKEAENERLRRQA----EDEAYQRKALEDQANQHKQQIEEkivlLK 1908
Cdd:pfam12128 285 SAElnqllRTLDDQWKEKRDELNGeLSAADAAVAKDRSELEALEDQHgaflDADIETAAADQEQLPSWQSELEN----LE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1909 KSSEAEMERQRAIVD--DTLKQRRVVEEEIRILKLN------FEKASSGKLDLELELNKLKN-IAEETQQSKLRAEEEAE 1979
Cdd:pfam12128 361 ERLKALTGKHQDVTAkyNRRRSKIKEQNNRDIAGIKdklakiREARDRQLAVAEDDLQALESeLREQLEAGKLEFNEEEY 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1980 KLrKLALEEEKRRREAEEKvkkiaaaEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKE---AEKQILMAQQAAQKCS 2056
Cdd:pfam12128 441 RL-KSRLGELKLRLNQATA-------TPELLLQLENFDERIERAREEQEAANAEVERLQSElrqARKRRDQASEALRQAS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2057 AAEQQVQSVLAQQKEDTIMQTKLKEEYekakkLAKQAEAAKEKAEREAA---LLRQ----QAEEAERQKAAAEQEAANQA 2129
Cdd:pfam12128 513 RRLEERQSALDELELQLFPQAGTLLHF-----LRKEAPDWEQSIGKVISpelLHRTdldpEVWDGSVGGELNLYGVKLDL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2130 KAQEDAERLRKEAEFEAaKRAQAENAAlkqkqqaDAEMAKHKKLAEQTLKQKFQVEQ---ELTKVKLKLDETDKQKSVLD 2206
Cdd:pfam12128 588 KRIDVPEWAASEEELRE-RLDKAEEAL-------QSAREKQAAAEEQLVQANGELEKasrEETFARTALKNARLDLRRLF 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2207 EELQRLKDEVDDAVKQR-GQVEEELLKVKVQMEELL-KLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAE-DAARL 2283
Cdd:pfam12128 660 DEKQSEKDKKNKALAERkDSANERLNSLEAQLKQLDkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALlKAAIA 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2284 SVEAQEAARLRQIAEDdlnQQRALADKMLKEkmqaiQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEE 2363
Cdd:pfam12128 740 ARRSGAKAELKALETW---YKRDLASLGVDP-----DVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPR 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2364 YQKSLEAERKRQLEIiaeseklklqVSQLSEAQAKAQEEAKKFKKQADSIASRLHETElatqEKMTVVeKLEVARLTSSK 2443
Cdd:pfam12128 812 LATQLSNIERAISEL----------QQQLARLIADTKLRRAKLEMERKASEKQQVRLS----ENLRGL-RCEMSKLATLK 876
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1927222988 2444 EADDlrkaIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVL 2491
Cdd:pfam12128 877 EDAN----SEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVI 920
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2324-2608 |
4.93e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2324 RLRAEAEMLQRQKDLAQEQAQKLledKQLMQQRldEETEEYQKSLEAERKRQLEIIAeseklkLQVSQLSEAQAKAQEEA 2403
Cdd:COG1196 180 KLEATEENLERLEDILGELERQL---EPLERQA--EKAERYRELKEELKELEAELLL------LKLRELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2404 KKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQ 2483
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2484 IEHEKTVLQQTFLSEKEmllkkEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAE 2563
Cdd:COG1196 329 EEELEELEEELEELEEE-----LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1927222988 2564 KEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQ 2608
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1666-2593 |
5.03e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 76.24 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1666 LAQEDAEKQKEEAEREAKKRAKAEDSALK-----QKEMAENELERQrkVAESTAQQKLTAEQELIRLRADFDNAEQQRSL 1740
Cdd:TIGR00606 165 LSEGKALKQKFDEIFSATRYIKALETLRQvrqtqGQKVQEHQMELK--YLKQYKEKACEIRDQITSKEAQLESSREIVKS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1741 LEDELYRLKNevvaaqqQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAE 1820
Cdd:TIGR00606 243 YENELDPLKN-------RLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1821 EAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEI---ALKEKEAENERLRRQAEDEAYQRKALEDQanqhk 1897
Cdd:TIGR00606 316 EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqeHIRARDSLIQSLATRLELDGFERGPFSER----- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1898 qQIEEKIVLLKKSSEAEMERQRAIVDD-----TLKQRRVVEEEIRILKLNfEKASSGKLDLELELNKLKNIAEETQQ--- 1969
Cdd:TIGR00606 391 -QIKNFHTLVIERQEDEAKTAAQLCADlqskeRLKQEQADEIRDEKKGLG-RTIELKKEILEKKQEELKFVIKELQQleg 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1970 SKLRAEEEAEKLRKLALEEEKRRREAEEKVKKiaaaeeeaARQRQAAQDELDRLKKKAEEARKQKD-DADKEAEKQILMA 2048
Cdd:TIGR00606 469 SSDRILELDQELRKAERELSKAEKNSLTETLK--------KEVKSLQNEKADLDRKLRKLDQEMEQlNHHTTTRTQMEML 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2049 qqaAQKCSAAEQQVQSVLAQQKEDTIMQT-------KLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAA 2121
Cdd:TIGR00606 541 ---TKDKMDKDEQIRKIKSRHSDELTSLLgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2122 EQEAANQAKA----------QEDAERLRKEAEfEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKV 2191
Cdd:TIGR00606 618 EEQLSSYEDKlfdvcgsqdeESDLERLKEEIE-KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEF 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2192 KLKLDET-----DKQKSvLDEELQRLKDEVDDA-VKQRGQVEEELLKVKvQMEELLKLKLRIEEENQRLikKDKDNTQKF 2265
Cdd:TIGR00606 697 ISDLQSKlrlapDKLKS-TESELKKKEKRRDEMlGLAPGRQSIIDLKEK-EIPELRNKLQKVNRDIQRL--KNDIEEQET 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2266 LAKEADNMKKLAEDA-------ARLSVEAQEAAR--LRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQK 2336
Cdd:TIGR00606 773 LLGTIMPEEESAKVCltdvtimERFQMELKDVERkiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLI 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2337 DLAQEQAQKLledkqlmQQRLDE-ETEEYQKSLEAERKRQLE-----IIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQA 2410
Cdd:TIGR00606 853 QDQQEQIQHL-------KSKTNElKSEKLQIGTNLQRRQQFEeqlveLSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2411 DSIASRLHETELATQEKMTVVEKlEVARLTSSKEadDLRKAIADlEKEKSRLKKEAE-DLQNKSKEMADAQQKQIEHEKT 2489
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIKE-KVKNIHGYMK--DIENKIQD-GKDDYLKQKETElNTVNAQLEECEKHQEKINEDMR 1001
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2490 VLQQTFLSEKEMLLKKEKLIEEEKKRLESQfEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNK 2569
Cdd:TIGR00606 1002 LMRQDIDTQKIQERWLQDNLTLRKRENELK-EVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGY 1080
|
970 980
....*....|....*....|....
gi 1927222988 2570 QKEMKELERKRLEQERILAEENQK 2593
Cdd:TIGR00606 1081 EKEIKHFKKELREPQFRDAEEKYR 1104
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2020-2553 |
5.19e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 75.93 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2020 LDRLKKKAEEARKQKDDADKEAEKQILMAQqaAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEK 2099
Cdd:pfam15921 326 VSQLRSELREAKRMYEDKIEELEKQLVLAN--SELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2100 AEREAA------LLRQQAEEAERQkaaaeqeaanqakaQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKL 2173
Cdd:pfam15921 404 WDRDTGnsitidHLRRELDDRNME--------------VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2174 AEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVD----DAVKQRGQVE---EELLKVKVQMEELLKLKlr 2246
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEatnaEITKLRSRVDlklQELQHLKNEGDHLRNVQ-- 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2247 IEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQ-EAARLrqiaEDDLNQQRALAD--KMLKEKMQA----- 2318
Cdd:pfam15921 548 TECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKAQL----EKEINDRRLELQefKILKDKKDAkirel 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2319 --------IQEASRLRAEAEMLQRQKDLAQEQAQkLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQvs 2390
Cdd:pfam15921 624 earvsdleLEKVKLVNAGSERLRAVKDIKQERDQ-LLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ-- 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2391 qLSEAQAKAQEEAKKFKKQADSIAsrlHETELAT-QEKMTVVEKLEVARLTSSKEAddLRKAIADLEKEKSRLKKEAEDL 2469
Cdd:pfam15921 701 -LKSAQSELEQTRNTLKSMEGSDG---HAMKVAMgMQKQITAKRGQIDALQSKIQF--LEEAMTNANKEKHFLKEEKNKL 774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2470 QNKSKEMADAQQKQI-EHEKTVLQQTFLSEKemllkkeklieeeKKRLESQFEEEVKKAKALKDEQERQKQqmEDEKKKL 2548
Cdd:pfam15921 775 SQELSTVATEKNKMAgELEVLRSQERRLKEK-------------VANMEVALDKASLQFAECQDIIQRQEQ--ESVRLKL 839
|
....*
gi 1927222988 2549 QATMD 2553
Cdd:pfam15921 840 QHTLD 844
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
64-143 |
5.98e-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: 68.00 E-value: 5.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 64 QVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM----RFHKLQNVQIALDFLKHRQV----KLVNIRNDDIADGNPKLT 135
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1927222988 136 LGLIWTII 143
Cdd:cd21223 105 LALLWRII 112
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2018-2613 |
6.60e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 6.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2018 DELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAK 2097
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2098 EK---AEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEaefeaakraqaenaaLKQKQQADAEMAKHKKLA 2174
Cdd:PRK03918 238 EEieeLEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE---------------LKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2175 EQTLKQKFQVEQELTKVKLKLDETDKQKsvldEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKlRIEEENQRL 2254
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2255 IKKDKDNTQKFLAKEADNMKKlaedaARLSVEAqeaarlrqiAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQR 2334
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEK-----AKEEIEE---------EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2335 QkdLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEA--ERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADS 2412
Cdd:PRK03918 444 E--LTEEHRKELLEEYTAELKRIEKELKEIEEKERKlrKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELE 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2413 IASRLHET---ELATQEKMTVVEKLEVARLTS-SKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIE--- 2485
Cdd:PRK03918 522 KKAEEYEKlkeKLIKLKGEIKSLKKELEKLEElKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEpfy 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2486 ----------HEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESqFEEEVKKAKALKDEQE-----RQKQQMEDEKKKLQA 2550
Cdd:PRK03918 602 neylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEE-LRKELEELEKKYSEEEyeelrEEYLELSRELAGLRA 680
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 2551 TMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERI--LAEENQKLREKLQQLEEAQKDQPDKEV 2613
Cdd:PRK03918 681 ELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLekALERVEELREKVKKYKALLKERALSKV 745
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2729-2766 |
8.45e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.04 E-value: 8.45e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1927222988 2729 LLEAQAATGSILDPIKNQKLSVNEAVKEGVIGPELHNK 2766
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2108-2425 |
1.11e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 74.77 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2108 RQQAEEAERQKAAAEQEAANQaKAQEdAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKL----AEQTLKQKFQ 2183
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEE-KARE-VERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELerirQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2184 VEQELTKVKL-KLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIkkdkdnt 2262
Cdd:pfam17380 365 IRQEEIAMEIsRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV------- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2263 QKFLAKEADNMKKLAEDAARlsvEAQEAARLRQIAEDdlNQQRALADKMLKEKMQAIQEASRLRAEAEMLQR-QKDLAQE 2341
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQE---RQQQVERLRQQEEE--RKRKKLELEKEKRDRKRAEEQRRKILEKELEERkQAMIEEE 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2342 QAQKLLEDKQLMQQRLDEETEEYQKSlEAERKRQLEiIAESEKLKLQVSQLSEAQAK--AQEEAKKFKKQADSIASRLHE 2419
Cdd:pfam17380 513 RKRKLLEKEMEERQKAIYEEERRREA-EEERRKQQE-MEERRRIQEQMRKATEERSRleAMEREREMMRQIVESEKARAE 590
|
....*.
gi 1927222988 2420 TELATQ 2425
Cdd:pfam17380 591 YEATTP 596
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
161-261 |
1.32e-12 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 66.98 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAErDLGVTRLLDP 240
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1927222988 241 ED-VDVPHPDEKSIITYVSSLY 261
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
619-808 |
1.38e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 70.17 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 619 LHAFVSAATKELMWLNDKEEEEVNFDWSDRNSNMTAKKDNYSGLMRELELREKKVNDIQATGDKLVRDGHPGKKTVESFT 698
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 699 AALQTQWSWILQLCCCIEAHLKENTAYYQFFADVKEAQDKMKKMQENMKkkySCDRSTTATRLEDLLQDAVEEREQLNEF 778
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 1927222988 779 KTLATGLNKRAKSIIQLKPRNPTHSIKGKL 808
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1678-1880 |
1.43e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.87 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1678 AEREAKKRAKAEDSALKQK-EMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQ 1756
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1757 QQRKQLEDELAKV---------RSEMDVLiqLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQR- 1826
Cdd:COG4942 97 AELEAQKEELAELlralyrlgrQPPLALL--LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERa 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 1827 --QVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAE 1880
Cdd:COG4942 175 elEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1343-1968 |
2.11e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 74.10 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1343 IKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEK 1422
Cdd:pfam12128 137 NLLNTREYRSIIQNDRTLLGRERVELRSLARQFALCDSESPLRHIDKIAKAMHSKEGKFRDVKSMIVAILEDDGVVPPKS 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1423 QKHNIQLE--LHELKNLseQQIMDKSKQVDdalqsrvKIEEEIRlirlQLETTVKQKSTAESELKQLRDRAAEAEKLRKA 1500
Cdd:pfam12128 217 RLNRQQVEhwIRDIQAI--AGIMKIRPEFT-------KLQQEFN----TLESAELRLSHLHFGYKSDETLIASRQEERQE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1501 AQEEAEKLRKQVNEETQKKRmaeEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQvAHVAAQ 1580
Cdd:pfam12128 284 TSAELNQLLRTLDDQWKEKR---DELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQ-SELENL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1581 KSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQqedaerareeaekelEKWRQKAN-----EALRLRL 1655
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIRE---------------ARDRQLAVaeddlQALESEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1656 QAEEEAHKKSLaqEDAEKQKEEAEREAKKR---AKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFD 1732
Cdd:pfam12128 425 REQLEAGKLEF--NEEEYRLKSRLGELKLRlnqATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1733 NAEQQRSLLEDELYRLKNEVVAAQQQ------------RKQL---EDELAKVRSEmdvliQLKSKAEKETMSNSERSKQL 1797
Cdd:pfam12128 503 QASEALRQASRRLEERQSALDELELQlfpqagtllhflRKEApdwEQSIGKVISP-----ELLHRTDLDPEVWDGSVGGE 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1798 LEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRR 1877
Cdd:pfam12128 578 LNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRR 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1878 QAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRvveeEIRILKLNFEKASSGKLDLELEL 1957
Cdd:pfam12128 658 LFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKR----EARTEKQAYWQVVEGALDAQLAL 733
|
650
....*....|.
gi 1927222988 1958 NKLKNIAEETQ 1968
Cdd:pfam12128 734 LKAAIAARRSG 744
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4308-4346 |
2.29e-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: 2.29e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1927222988 4308 LLEAQACTGGIIDPTTGERFSVTDATEKGLVDKVMVDRL 4346
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1165-1985 |
3.59e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 73.46 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1165 ATAVSDKMSRVHSERDAELDHYRQLLSSLQDRWKAVFSQIDLRQRELEQLGRQLGYYRESYDWLIRWINDAKQRQEKIQA 1244
Cdd:TIGR00618 182 ALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1245 vtitdsktLKEQLAQEKKL---LEEVEGNKDKVDECQKYAKayidtikdyelqLVAYKAQVEPLasplkktkldsaSDNI 1321
Cdd:TIGR00618 262 --------LKQLRARIEELraqEAVLEETQERINRARKAAP------------LAAHIKAVTQI------------EQQA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1322 IQEYVTLRTKYSELMTLTSQYIKFITDS-----QRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAE-VHAKAIAKA 1395
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQssieeQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1396 EKEAQELKLRMQEEVNRREDAVVDAEKQKHNI--QLELHELKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETt 1473
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSAFRDlqGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL- 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1474 vKQKSTAESELKQLRDRAAeaeklRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQ 1553
Cdd:TIGR00618 469 -KEREQQLQTKEQIHLQET-----RKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLET 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1554 AEEAERQVKQAEIEkerqiqvaHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQedaerar 1633
Cdd:TIGR00618 543 SEEDVYHQLTSERK--------QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE------- 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1634 eeaekelekwRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAEST 1713
Cdd:TIGR00618 608 ----------DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLAS 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1714 AQQKLTAEQELIR-LRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKEtmsnse 1792
Cdd:TIGR00618 678 RQLALQKMQSEKEqLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ------ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1793 rskqlleveatkmrdlAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKlaaisdaTRLKTEAEIALKEKEAEN 1872
Cdd:TIGR00618 752 ----------------ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF-------NRLREEDTHLLKTLEAEI 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1873 ERLRRQAED--EAYQRKALEDQANQHkQQIEEKIVLLkksseAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSgk 1950
Cdd:TIGR00618 809 GQEIPSDEDilNLQCETLVQEEEQFL-SRLEEKSATL-----GEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG-- 880
|
810 820 830
....*....|....*....|....*....|....*
gi 1927222988 1951 ldleleLNKLKNIAEETQQSKLRAEEEAEKLRKLA 1985
Cdd:TIGR00618 881 ------INQIKIQFDGDALIKFLHEITLYANVRLA 909
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
48-149 |
4.61e-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: 65.72 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 48 KTFTKWVNKHLIKSQrqVTDLYEDLRDGHNLISLLEVL-------SGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLV 120
Cdd:cd21298 9 KTYRNWMNSLGVNPF--VNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1927222988 121 NIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1484-1985 |
4.86e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.77 E-value: 4.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1484 LKQLRDRAAEA----EKLRKAAQEEAEKLRKQVNEETQK---KRMAEEELKRKAEAekeaakqkqkalEDLENLKRQAEE 1556
Cdd:PRK02224 164 LEEYRERASDArlgvERVLSDQRGSLDQLKAQIEEKEEKdlhERLNGLESELAELD------------EEIERYEEQREQ 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1557 AERQVKQAE--IEKERQIQvAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALkkqqedaerare 1634
Cdd:PRK02224 232 ARETRDEADevLEEHEERR-EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL------------ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1635 EAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQE--DAEKQKEEAEREAKKRAKAEDSALKQKEMA---ENELERQRKV 1709
Cdd:PRK02224 299 LAEAGLDDADAEAVEARREELEDRDEELRDRLEECrvAAQAHNEEAESLREDADDLEERAEELREEAaelESELEEAREA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1710 AESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRsemdvliqlKSKAEKETM- 1788
Cdd:PRK02224 379 VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR---------ERVEEAEALl 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1789 --SNSERSKQLLE----VEATKMRDlaEEASKLRAIAEEAKHQRQVAEE--EAARQRAEAERILKEKLAAISDATRLKTE 1860
Cdd:PRK02224 450 eaGKCPECGQPVEgsphVETIEEDR--ERVEELEAELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDLEELIAE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1861 AEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLkksseAEMERQRAIVDDTLKQRRVVEEEirilk 1940
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV-----AELNSKLAELKERIESLERIRTL----- 597
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1927222988 1941 lnFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLA 1985
Cdd:PRK02224 598 --LAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELE 640
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1384-1846 |
5.87e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1384 LAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQQimdkskqvDDALQSRVKIEEEI 1463
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL--------EELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1464 RLIR--LQLETTVKQKSTAESELKQLRDRA----------AEAEKLRKAAQEEAEKLRKQVNEETQKKR-MAEEELKRKA 1530
Cdd:COG4717 119 EKLEklLQLLPLYQELEALEAELAELPERLeeleerleelRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1531 EAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQK------SAAAELQSKHMSFVEKTSKLEES 1604
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1605 LkQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQ--------EDAEKQKE 1676
Cdd:COG4717 279 L-FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLElldrieelQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1677 EAEREAK-KRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELI--RLRADFDNAEQQ-----RSLLEDELYRL 1748
Cdd:COG4717 358 ELEEELQlEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELeeQLEELLGELEELlealdEEELEEELEEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1749 KNEVVAAQQQRKQLEDELAKVRSEMDVLiqlkskaekETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEE-AKHQRQ 1827
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQL---------EEDGELAELLQELEELKAELRELAEEWAALKLALELlEEAREE 508
|
490
....*....|....*....
gi 1927222988 1828 VAEEEAARQRAEAERILKE 1846
Cdd:COG4717 509 YREERLPPVLERASEYFSR 527
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3132-3170 |
5.90e-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: 5.90e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1927222988 3132 LLDAQMATGGIIDPVNSHHIPHDVACKRNYFDDEMKQNL 3170
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
41-140 |
6.23e-12 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 65.52 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 41 ERDRvQKKTFTKWVNKhlIKSQRQVTDLYEDLRDGHNLISLLE-VLSGE-------TLPREKGRMRFHKLQNVQIALDFL 112
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1927222988 113 KHRQVKLVNIRNDDIADGNPKLTLGLIW 140
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1020-1979 |
8.32e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 72.31 E-value: 8.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1020 VEKEPLKECVQKTTEQKKVQVELEGLKKDLNKVSAKTKEVLASPQQTAsapvlrsELDLTVEKMdhthmlssVYLEKLKT 1099
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE-------KLELEEEYL--------LYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1100 VEMVIRNTQgaegvlkqyedclrevhtvpndvKEVETYRTKLKKMRAEAEGEQPVFDSLEAELKKATAVSDKMSRVHSER 1179
Cdd:pfam02463 235 NEERIDLLQ-----------------------ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1180 DAELDHYRQLLSSLQDRWKAVFSQIDLRQRELEQLGRQLGYYRESYdwlirwinDAKQRQEKIQAVTITDSKTLKEQLAQ 1259
Cdd:pfam02463 292 AKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI--------EELEKELKELEIKREAEEEEEEELEK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1260 EKKLLEEVEGNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLASPLKKTKLDSASDNIIQEyvtlrtKYSELMTLT 1339
Cdd:pfam02463 364 LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE------LEILEEEEE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1340 SQYIKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVD 1419
Cdd:pfam02463 438 SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1420 AEK-----QKHNIQLELHELKNLSEQQIMDkSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEA 1494
Cdd:pfam02463 518 DGVggriiSAHGRLGDLGVAVENYKVAIST-AVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1495 EKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQV 1574
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELL 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1575 AHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQedaerareeaekeLEKWRQKANEALRLR 1654
Cdd:pfam02463 677 EIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQ-------------EAQDKINEELKLLKQ 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1655 LQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTaqqkLTAEQELIRLRADFDNA 1734
Cdd:pfam02463 744 KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE----LRALEEELKEEAELLEE 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1735 EQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMdvliqLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASK 1814
Cdd:pfam02463 820 EQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER-----LEEEITKEELLQELLLKEEELEEQKLKDELESKEEK 894
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1815 LRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQAN 1894
Cdd:pfam02463 895 EKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGK 974
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1895 QHKQQIEEKIVLLKKSSEAEMERQRAivddTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRA 1974
Cdd:pfam02463 975 VNLMAIEEFEEKEERYNKDELEKERL----EEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRL 1050
|
....*
gi 1927222988 1975 EEEAE 1979
Cdd:pfam02463 1051 EDPDD 1055
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1873-2604 |
8.32e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 72.07 E-value: 8.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1873 ERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKS------SEAEMERQRAIVDDTLKQRRVVEEEIRilklnfeka 1946
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSvidlqtKLQEMQMERDAMADIRRRESQSQEDLR--------- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1947 ssgkldlelelNKLKNIAEETQQSKLRAEE-------EAEKLRKLALEEEKRRREaeekVKKIAAAEEEAARQRQAAQDE 2019
Cdd:pfam15921 145 -----------NQLQNTVHELEAAKCLKEDmledsntQIEQLRKMMLSHEGVLQE----IRSILVDFEEASGKKIYEHDS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2020 LDRL--KKKAEEARKQKDDADKEA---EKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEkAKKLAKQAE 2094
Cdd:pfam15921 210 MSTMhfRSLGSAISKILRELDTEIsylKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE-ITGLTEKAS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2095 AAKEKAEREAALLRQQAEEAERQKAAAEQEAAnqaKAQEDAERLRkeAEFEAAKRAQAENAALKQKQQ--ADAEMAKHKK 2172
Cdd:pfam15921 289 SARSQANSIQSQLEIIQEQARNQNSMYMRQLS---DLESTVSQLR--SELREAKRMYEDKIEELEKQLvlANSELTEART 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2173 LAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKD--------------EVDD-------------AVKQ--R 2223
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsitidhlrrELDDrnmevqrleallkAMKSecQ 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2224 GQVEEELLKVKVQMEELLK---LKLRIEEENQRLIKKDKDNTQKFLAKEadNMKKLAEDaarLSVEAQEAARLRQIAEDD 2300
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKvssLTAQLESTKEMLRKVVEELTAKKMTLE--SSERTVSD---LTASLQEKERAIEATNAE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2301 LNQQRALADKMLKEKMQAIQEASRLR---AEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEyQKSLEAErKRQLE 2377
Cdd:pfam15921 519 ITKLRSRVDLKLQELQHLKNEGDHLRnvqTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRT-AGAMQVE-KAQLE 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2378 IIAESEKLKLQVSQLseaqAKAQEEAKKFKKQADSIASRLHETEL--ATQEKMTVVEKLEVARLTSSKEADDLRKAIADL 2455
Cdd:pfam15921 597 KEINDRRLELQEFKI----LKDKKDAKIRELEARVSDLELEKVKLvnAGSERLRAVKDIKQERDQLLNEVKTSRNELNSL 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2456 EKEKSRLKKeaeDLQNKSKEMADAQQK---QIEHEKTVLQQTFLSEKEMllkkeklieeekkrlESQFEEEVKKAKALKD 2532
Cdd:pfam15921 673 SEDYEVLKR---NFRNKSEEMETTTNKlkmQLKSAQSELEQTRNTLKSM---------------EGSDGHAMKVAMGMQK 734
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 2533 EQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKEL-----ERKRLEQE-RILAEENQKLREKLQQLEEA 2604
Cdd:pfam15921 735 QITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELstvatEKNKMAGElEVLRSQERRLKEKVANMEVA 812
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3958-3996 |
8.55e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 8.55e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1927222988 3958 LLEAQAATGYVIDPIKNLKLTVSEAVRMGIVGPEFKDKL 3996
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1860-2495 |
1.20e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.61 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1860 EAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVL---LKKSSE--AEMERQRAIVDDTLKQRRVVEE 1934
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLeaeIEDLREtiAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1935 EIR------ILKLNFEKASSGKL-----DLELELNKLKNIAEETQQSKLRAEEEAEKLRklaleeekrrreaeekvkkia 2003
Cdd:PRK02224 290 ELEeerddlLAEAGLDDADAEAVearreELEDRDEELRDRLEECRVAAQAHNEEAESLR--------------------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2004 aaeeeaarqrqaaqDELDRLKKKAEEARKQKDDADKEAEkqilmaqqaaqkcsAAEQQVQSVLAQQKEdtimqtkLKEEY 2083
Cdd:PRK02224 349 --------------EDADDLEERAEELREEAAELESELE--------------EAREAVEDRREEIEE-------LEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2084 EKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRkeaefEAAKRAQaenaalkqkqqa 2163
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL-----EAGKCPE------------ 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2164 daemakhkklAEQTLKQKFQVEqeltkvklKLDETDKQKSVLDEELQRLKDEVDDaVKQRGQVEEELLKVKVQMEELLKL 2243
Cdd:PRK02224 457 ----------CGQPVEGSPHVE--------TIEEDRERVEELEAELEDLEEEVEE-VEERLERAEDLVEAEDRIERLEER 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2244 KLRIEE--ENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRAladkMLKEKMQAIQE 2321
Cdd:PRK02224 518 REDLEEliAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA----ELKERIESLER 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2322 ASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETeeyqksleaERKRQLEIiaeseklKLQVSQLSEAQAKaQE 2401
Cdd:PRK02224 594 IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR---------ERKRELEA-------EFDEARIEEARED-KE 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2402 EAKKFKKQADSIASRLHETELATQEKMTVVEklevarlTSSKEADDLRKAIADLEKEKSRLK---KEAEDLQNKSKEM-A 2477
Cdd:PRK02224 657 RAEEYLEQVEEKLDELREERDDLQAEIGAVE-------NELEELEELRERREALENRVEALEalyDEAEELESMYGDLrA 729
|
650
....*....|....*...
gi 1927222988 2478 DAQQKQIEHEKTVLQQTF 2495
Cdd:PRK02224 730 ELRQRNVETLERMLNETF 747
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2018-2608 |
1.21e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2018 DELDRLKKKAEEARKQKD---DADKEAEKqilmAQQAAQKCSAAEQQVQSVLAQQKEDTImqTKLKEEYEKAKKLAKQAE 2094
Cdd:COG4913 235 DDLERAHEALEDAREQIEllePIRELAER----YAAARERLAELEYLRAALRLWFAQRRL--ELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2095 AAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQ-EDAERLRKEAEfeaAKRAQAENAALKQKQQADAEMAKHKKL 2173
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNGGDRLEQLEREiERLERELEERE---RRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2174 AEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLK--------- 2244
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDeaelpfvge 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2245 ---LRIEEEN-----QRLIkkdkdNTQKF--LAKEADnmkklaEDAARLSVEA-QEAARLR--QIAEDDLNQQR-ALADK 2310
Cdd:COG4913 466 lieVRPEEERwrgaiERVL-----GGFALtlLVPPEH------YAAALRWVNRlHLRGRLVyeRVRTGLPDPERpRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2311 MLKEKMQAiqEASRLRAEAEM-LQRQKDLAQ-EQAQKL-LEDKQLMQQRL-------------DEETEEYQKSLEAERKR 2374
Cdd:COG4913 535 SLAGKLDF--KPHPFRAWLEAeLGRRFDYVCvDSPEELrRHPRAITRAGQvkgngtrhekddrRRIRSRYVLGFDNRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2375 QlEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIA--SRLHETELATQEKMTVVEKLEVAR---LTSSKEADDLR 2449
Cdd:COG4913 613 A-ALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELerlDASSDDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2450 KAIADLEKEKSRLKKEAEDLQNKSKEmADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKA 2529
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2530 LKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELER--KRLEQERiLAEENQKLREKLQQLEEAQKD 2607
Cdd:COG4913 771 LEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLAllDRLEEDG-LPEYEERFKELLNENSIEFVA 849
|
.
gi 1927222988 2608 Q 2608
Cdd:COG4913 850 D 850
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1831-2468 |
1.26e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 71.29 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1831 EEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEekivLLKKS 1910
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCN----LLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1911 SEAEMERQRAIVDDTLKQRRV---VEEEIRILKLNFEKASSGKLDLELELN-KLKNIAEETQQSKLRAEEEAEKLRKLAL 1986
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVymdLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1987 EEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVL 2066
Cdd:pfam05483 244 LLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2067 AQQKEDTIMQTKLKEEYEKAKK----LAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLR--K 2140
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAahsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKnnK 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2141 EAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTL-----------------------------KQKFQVEQELTKV 2191
Cdd:pfam05483 404 EVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqarekeihdleiqltaiktseehylKEVEDLKTELEKE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2192 KLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKlKLRIEEENQRLIKKDKDNTQKFLAKEAD 2271
Cdd:pfam05483 484 KLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK-QIENLEEKEMNLRDELESVREEFIQKGD 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2272 NMK----KLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLL 2347
Cdd:pfam05483 563 EVKckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLE 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2348 EDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAK-----------KFKKQADSIA-- 2414
Cdd:pfam05483 643 LELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhkiaemvalmeKHKHQYDKIIee 722
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 2415 --SRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAED 2468
Cdd:pfam05483 723 rdSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
163-262 |
1.71e-11 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 63.51 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 163 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMgRVYRQTN----LENLEQAFGVAER-DLGVTRL 237
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPK-INKKPKSpfkkRENINLFLNACKKlGLPELDL 79
|
90 100
....*....|....*....|....*
gi 1927222988 238 LDPEDVdVPHPDEKSIITYVSSLYD 262
Cdd:cd00014 80 FEPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1765-2389 |
1.98e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1765 ELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAE--- 1841
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESleg 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1842 --RILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEdEAYQRKALEDQANQHKQQIEEKivllkkssEAEMERQR 1919
Cdd:PRK03918 253 skRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKR--------LSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1920 AIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLE---LELNKLKNIAEETQQ-SKLRAEEEAEKLRKLALEEEKRRREA 1995
Cdd:PRK03918 324 NGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1996 EEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAaqKCSAAEQQVQSVLAQQKEDTIM 2075
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2076 QTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAA--KRAQAE 2153
Cdd:PRK03918 482 LRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkKKLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2154 NAALKQKQQADAEMakHKKLAEQTLKQKFQVEQELTKVK------LKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVE 2227
Cdd:PRK03918 562 EKKLDELEEELAEL--LKELEELGFESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2228 EELLKVKVQMEELlkLKLRIEEENQRLIKKdkdntqkflakeadnMKKLAEDAARLSVEAQEAARLRQIAEDDLnqqral 2307
Cdd:PRK03918 640 KRLEELRKELEEL--EKKYSEEEYEELREE---------------YLELSRELAGLRAELEELEKRREEIKKTL------ 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2308 adKMLKEKMQAIQEAsrlRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAE---RKRQ-LEIIAESE 2383
Cdd:PRK03918 697 --EKLKEELEEREKA---KKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFEElteGKYSgVRVKAEEN 771
|
....*.
gi 1927222988 2384 KLKLQV 2389
Cdd:PRK03918 772 KVKLFV 777
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1352-1983 |
2.01e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 70.52 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1352 RLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLeL 1431
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNL-L 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1432 HELKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELK-QLRDRAAEAEKLRKAAQEEAEKLRK 1510
Cdd:pfam05483 161 KETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1511 QVN----EETQKK-RMAEEELKRKAEAEKEAAKQKQKALEDlENLKRQAEEAERQVKqaEIEKERQIQVAHVAAQKSAAA 1585
Cdd:pfam05483 241 QVSllliQITEKEnKMKDLTFLLEESRDKANQLEEKTKLQD-ENLKELIEKKDHLTK--ELEDIKMSLQRSMSTQKALEE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1586 ELQSKHMSFVEKTSKLEESLKQEHGAvlqlqHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKS 1665
Cdd:pfam05483 318 DLQIATKTICQLTEEKEAQMEELNKA-----KAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1666 LAQEDAEKQKEEAEREAKKRAKAEDSAL----KQKEMAENELE------------RQRKVAESTAQQKLTAEQELIRLRa 1729
Cdd:pfam05483 393 LEEMTKFKNNKEVELEELKKILAEDEKLldekKQFEKIAEELKgkeqelifllqaREKEIHDLEIQLTAIKTSEEHYLK- 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1730 dfdNAEQQRSLLEDElyRLKNEVVAAQQQRKQLEDElAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEA-----TK 1804
Cdd:pfam05483 472 ---EVEDLKTELEKE--KLKNIELTAHCDKLLLENK-ELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENleekeMN 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1805 MRDLAEEASK-LRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIA---LKEKEAENERLRRQAE 1880
Cdd:pfam05483 546 LRDELESVREeFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknIEELHQENKALKKKGS 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1881 DEAYQRKALEDQANQ-------HKQQIEE------KIVLLKKSSE----AEMERQRAIVDDTLKQR-------------- 1929
Cdd:pfam05483 626 AENKQLNAYEIKVNKlelelasAKQKFEEiidnyqKEIEDKKISEekllEEVEKAKAIADEAVKLQkeidkrcqhkiaem 705
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222988 1930 ------------RVVEE---EIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRK 1983
Cdd:pfam05483 706 valmekhkhqydKIIEErdsELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKM 774
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1388-1737 |
2.26e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.54 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1388 HAKAIAkaEKEAQELKLRMQEEVNRREDAVVDAEKQKHNiQLELHELknlSEQQIMDKSKQVDdALQSRVKIEEEIRLIR 1467
Cdd:pfam17380 280 HQKAVS--ERQQQEKFEKMEQERLRQEKEEKAREVERRR-KLEEAEK---ARQAEMDRQAAIY-AEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1468 LQLETTVKQ-KSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVnEETQKKRMAEEELKRKAEAEKEaakqkqkaleD 1546
Cdd:pfam17380 353 IRQEERKRElERIRQEEIAMEISRMRELERLQMERQQKNERVRQEL-EAARKVKILEEERQRKIQQQKV----------E 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1547 LENLKRQAEEA-ERQVKQAEIEKERQIQVAhvaaqksaaaelqskhmsfvektsKLEESLKQEHGAVLQLQHEAAALKKQ 1625
Cdd:pfam17380 422 MEQIRAEQEEArQREVRRLEEERAREMERV------------------------RLEEQERQQQVERLRQQEEERKRKKL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1626 QEDAERAREEAEKelEKWRQKANEALRLRLQA--EEEAHKKSLAQEDAEKQKEEAEREakKRAKAEDSALKQKEMAENE- 1702
Cdd:pfam17380 478 ELEKEKRDRKRAE--EQRRKILEKELEERKQAmiEEERKRKLLEKEMEERQKAIYEEE--RRREAEEERRKQQEMEERRr 553
|
330 340 350
....*....|....*....|....*....|....*..
gi 1927222988 1703 -LERQRKVAESTAQ-QKLTAEQELIRLRADFDNAEQQ 1737
Cdd:pfam17380 554 iQEQMRKATEERSRlEAMEREREMMRQIVESEKARAE 590
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2107-2605 |
2.27e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2107 LRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRaqaenaalkQKQQADAEMAKHkklaEQTLKQKFQVEQ 2186
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE---------TRDEADEVLEEH----EERREELETLEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2187 ELTKVKLKLDETDKQKSVLDEELQ-------RLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEE--ENQRLIKK 2257
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRdlrerleELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrlEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2258 DKDNTQKFLAKEADNM----KKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQ 2333
Cdd:PRK02224 339 AHNEEAESLREDADDLeeraEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2334 RQKDLAQEQAQKLLEDKQLMQQRLDE-----------------ETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLS--- 2393
Cdd:PRK02224 419 EERDELREREAELEATLRTARERVEEaealleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEerl 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2394 ---EAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKL-----------EVARLTSSK---EADDLRKAIADLE 2456
Cdd:PRK02224 499 eraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELreraaeleaeaEEKREAAAEaeeEAEEAREEVAELN 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2457 KEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKR-LESQFEEE-VKKAKALKDEQ 2534
Cdd:PRK02224 579 SKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKReLEAEFDEArIEEAREDKERA 658
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222988 2535 ERQKQQMEDEKKKLQATMDAALNKQKEAEKEMhnkqkemKELERKRLEQERiLAEENQKLREKLQQLEEAQ 2605
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEIGAVENEL-------EELEELRERREA-LENRVEALEALYDEAEELE 721
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1474-1890 |
2.42e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.15 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1474 VKQKSTAESELKQLRDRAAEAEKL--RKAAQEEAEKLRKQVNEETQK---KRMAEEEL--KRKAEAEKEAAKQKQKALED 1546
Cdd:pfam17380 213 IQMSTVAPKEVQGMPHTLAPYEKMerRKESFNLAEDVTTMTPEYTVRyngQTMTENEFlnQLLHIVQHQKAVSERQQQEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1547 LENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQ----KSAAAELQSKHMSfVEKTSKLEESLKQEHgavlqlQHEAAAL 1622
Cdd:pfam17380 293 FEKMEQERLRQEKEEKAREVERRRKLEEAEKARQaemdRQAAIYAEQERMA-MERERELERIRQEER------KRELERI 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1623 KKQQEDAERAREEAEKELEKWRQKANEALRLRLQAeeeAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSAlKQKEMAENE 1702
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQELEA---ARKVKILEEERQRKIQQQKVEMEQIRAEQEEA-RQREVRRLE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1703 LERQRKVaESTAQQKLTAEQELIRLRADfdnaeqqrslledelyrlknevvAAQQQRKQLEDElakvrsemdvliqlksK 1782
Cdd:pfam17380 442 EERAREM-ERVRLEEQERQQQVERLRQQ-----------------------EEERKRKKLELE----------------K 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1783 AEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVA-EEEAARQRAEAER---ILKEKLAAISDATRLK 1858
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAiYEEERRREAEEERrkqQEMEERRRIQEQMRKA 561
|
410 420 430
....*....|....*....|....*....|..
gi 1927222988 1859 TEAEIALKEKEAENERLRRQAEDEAyQRKALE 1890
Cdd:pfam17380 562 TEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1130-1945 |
2.46e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.48 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1130 DVKEVETYRTKLKKMRAEAEGEQPVFDSLEAELKKataVSDKMSRVHSERDaELDHYRQLLSSLQD-RWKAVFSQIDLRQ 1208
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEENIERLDLIIDE---KRQQLERLRRERE-KAERYQALLKEKREyEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1209 RELEQLGRQLGYYRESYDWLIRWINDAKQRQEKIQAVTITDSKTLK-----EQLAQEKKLLE---EVEGNKDKVDECQKY 1280
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeEQLRVKEKIGEleaEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1281 AKAYIDTIKDYELQLVAYKAQVEPLASPLKKTKLDSASdnIIQEYVTLRTKYSELmtltsqyikfitdsQRRLEDEEKAA 1360
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK--LTEEYAELKEELEDL--------------RAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1361 EKLKAEeqkkmammqaeldkqkqlaevhakaIAKAEKEAQELKLRMqEEVNRREDAVVDAEKQKHNIQLELH-ELKNLSE 1439
Cdd:TIGR02169 381 AETRDE-------------------------LKDYREKLEKLKREI-NELKRELDRLQEELQRLSEELADLNaAIAGIEA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1440 QQimdkskqvdDALQSRVK-IEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKL--RKQVNEET 1516
Cdd:TIGR02169 435 KI---------NELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAeaQARASEER 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1517 QKKRMAEEELKRKAEAEKEAAKQKQKALED-----LE-----NLKRQAEEAERQVKQA-EIEKERQ-----------IQV 1574
Cdd:TIGR02169 506 VRGGRAVEEVLKASIQGVHGTVAQLGSVGEryataIEvaagnRLNNVVVEDDAVAKEAiELLKRRKagratflplnkMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1575 AHVAAQKSAAAELQSKHMSFVEKTSKLE-------------ESL------------------------------------ 1605
Cdd:TIGR02169 586 ERRDLSILSEDGVIGFAVDLVEFDPKYEpafkyvfgdtlvvEDIeaarrlmgkyrmvtlegelfeksgamtggsraprgg 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1606 ----KQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRL---------RLQAEEEAHKKSLAQEDAE 1672
Cdd:TIGR02169 666 ilfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiekeieQLEQEEEKLKERLEELEED 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1673 KQKEEAEREAKKRAKAEDSA--------LKQKEMAENELER---QRKVAESTAQ-QKLTAEQELIRLRADFDNAEQQRSL 1740
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEArieeleedLHKLEEALNDLEArlsHSRIPEIQAElSKLEEEVSRIEARLREIEQKLNRLT 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1741 LEDELyrLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKEtmsnserskqlLEVEATKMRDLAEEASKLRAIAE 1820
Cdd:TIGR02169 826 LEKEY--LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-----------LEELEAALRDLESRLGDLKKERD 892
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1821 EAKHQRQVAEEEaaRQRAEAERILKEKLAAisdatRLKTEAEiALKEKEAENERLRRQAEDEAYQRKALEDQAnQHKQQI 1900
Cdd:TIGR02169 893 ELEAQLRELERK--IEELEAQIEKKRKRLS-----ELKAKLE-ALEEELSEIEDPKGEDEEIPEEELSLEDVQ-AELQRV 963
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1927222988 1901 EEKIVLLKK---SSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEK 1945
Cdd:TIGR02169 964 EEEIRALEPvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
163-263 |
3.36e-11 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 62.75 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 163 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPED 242
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1927222988 243 VdVPHPDEKSIITYVSSLYDA 263
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3797-3834 |
3.70e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.42 E-value: 3.70e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1927222988 3797 LEAQTATGGIIDPEFQFHLPADVAMQRGYINKETNEKL 3834
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1920-2480 |
4.78e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1920 AIVDDTLKQRRVVEEEIRILKlnFEKASSGKLDLELELNKLKniaeETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKV 1999
Cdd:PRK03918 139 AILESDESREKVVRQILGLDD--YENAYKNLGEVIKEIKRRI----ERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2000 KKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQ--- 2076
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKeka 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2077 ---TKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAE-FEAAKRAQA 2152
Cdd:PRK03918 293 eeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2153 ENAALKqKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEE--- 2229
Cdd:PRK03918 373 ELERLK-KRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrk 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2230 --LLKVKVQMEELLKLKLRIEEEnQRLIKKDKDNTQKFLAKE---------ADNMKKLAE-----DAARLSVEAQEAARL 2293
Cdd:PRK03918 452 elLEEYTAELKRIEKELKEIEEK-ERKLRKELRELEKVLKKEseliklkelAEQLKELEEklkkyNLEELEKKAEEYEKL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2294 RQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAER- 2372
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDa 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2373 KRQLEIIAES-EKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEA-----D 2446
Cdd:PRK03918 611 EKELEREEKElKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEElekrrE 690
|
570 580 590
....*....|....*....|....*....|....
gi 1927222988 2447 DLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQ 2480
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3057-3094 |
5.31e-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: 5.31e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1927222988 3057 LEAQAGTGYVVDPVDNKKYTVDEAVKAGVVGPELHEKL 3094
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2025-2191 |
6.09e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 67.91 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2025 KKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREA 2104
Cdd:PRK09510 95 KQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2105 ALLRQQAEEAERQKAAAEQEAANQAKAQEDAERlRKEAEFEAAKRAQAENAALKQKQQADAEmAKHKKLAEQTLKQKFQV 2184
Cdd:PRK09510 175 AAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA-KKKAAAEAKKKAAAEAKAAAAKAAAEAK-AAAEKAAAAKAAEKAAA 252
|
....*..
gi 1927222988 2185 EQELTKV 2191
Cdd:PRK09510 253 AKAAAEV 259
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
163-258 |
6.78e-11 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 62.02 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 163 KEKLLLWSQRMtdgYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLV-DMGRVYRQTNLENLEQAFGVAERDLGVTRLLDPE 241
Cdd:cd21229 5 KKLMLAWLQAV---LPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1927222988 242 DVDVPHPDEKSIITYVS 258
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
47-146 |
7.86e-11 |
|
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: 62.22 E-value: 7.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 47 KKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLP----REKGRMRFHKLQNVQIALDFLKHRQVKLVNI 122
Cdd:cd21222 18 KELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELMEDAGISTPKI 97
|
90 100
....*....|....*....|....
gi 1927222988 123 RNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21222 98 RPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2185-2612 |
8.67e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 68.51 E-value: 8.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2185 EQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEEnqrlIKKDKDNTQK 2264
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE----IKKKEKELEK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2265 fLAKEADNMKKLAEDaarlsVEAQEAARLRQIAE-----DDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLA 2339
Cdd:TIGR04523 157 -LNNKYNDLKKQKEE-----LENELNLLEKEKLNiqkniDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2340 QEQAQKLLEDKQLMQQRLDEETEEYQ--KSLEAERKRQL-EIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASR 2416
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNqlKDEQNKIKKQLsEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2417 LHETELATQEKmtvveKLEVARltssKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMadaqQKQIEhEKTVLQQTFL 2496
Cdd:TIGR04523 311 ELKSELKNQEK-----KLEEIQ----NQISQNNKIISQLNEQISQLKKELTNSESENSEK----QRELE-EKQNEIEKLK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2497 SEKEMLLKKEKLIEEEKKRLESQFEEeVKKAKALKDEQ----ERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKE 2572
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQN-QEKLNQQKDEQikklQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1927222988 2573 MKELERKRLEQERILAEENQKLREKLQQLEEAQKDQPDKE 2612
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE 495
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2312-2613 |
9.03e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 68.84 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2312 LKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIiaESEKLKLQVSQ 2391
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL--LQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2392 LSEAQAKAQEEAKKFKKQadsiaSRLHETELATQEKMTVVEK-LEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQ 2470
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQV-----LKENKEEEKEKKLQEEELKlLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2471 nKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQA 2550
Cdd:pfam02463 328 -KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222988 2551 tmdAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQPDKEV 2613
Cdd:pfam02463 407 ---AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1545-2180 |
9.16e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1545 EDLENLKRQAEEAERQVKQ-AEIEKERQiQVAHVAAQKSAAAELQSKHmsfvektskleeslkqehgAVLQLQHEAAALK 1623
Cdd:COG4913 235 DDLERAHEALEDAREQIELlEPIRELAE-RYAAARERLAELEYLRAAL-------------------RLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1624 KqqedaerareeaekelekwRQKANEALRLRLQAEEEAHKkslAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENEL 1703
Cdd:COG4913 295 A-------------------ELEELRAELARLEAELERLE---ARLDALREELDELEAQIRGNGGDRLEQLEREIERLER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1704 ERQRKVAESTAQQKLTA---------EQELIRLRADF----DNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAkvr 1770
Cdd:COG4913 353 ELEERERRRARLEALLAalglplpasAEEFAALRAEAaallEALEEELEALEEALAEAEAALRDLRRELRELEAEIA--- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1771 semdvliqlkskaeketmsNSERSKQLLEVEATKMRDLAEEA-----SKLRAIAEEAkhqrQVAEEEAARQRAeAERIL- 1844
Cdd:COG4913 430 -------------------SLERRKSNIPARLLALRDALAEAlgldeAELPFVGELI----EVRPEEERWRGA-IERVLg 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1845 ---------KEKLAAIS---DATRLKTEAEIaLKEKEAENERLRRQAEDEAYQRKaLEDQANQH----KQQIEEKIVLLK 1908
Cdd:COG4913 486 gfaltllvpPEHYAAALrwvNRLHLRGRLVY-ERVRTGLPDPERPRLDPDSLAGK-LDFKPHPFrawlEAELGRRFDYVC 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1909 KSSEAEMER-QRAIVDD-TLKQRRVVeeeirilklnFEKASSGKLDLELEL-----NKLKNIAEETQQSKLRAEEEAEKL 1981
Cdd:COG4913 564 VDSPEELRRhPRAITRAgQVKGNGTR----------HEKDDRRRIRSRYVLgfdnrAKLAALEAELAELEEELAEAEERL 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1982 RKLAleeekrrreaeekvkkiaaaeeeaarqrqaaqDELDRLKKKAEEARKQKDDADKEaekqiLMAQQAAQKCSAAEQQ 2061
Cdd:COG4913 634 EALE--------------------------------AELDALQERREALQRLAEYSWDE-----IDVASAEREIAELEAE 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2062 VQSVLAQQkeDTIMQtkLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKE 2141
Cdd:COG4913 677 LERLDASS--DDLAA--LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1927222988 2142 AEFEAAKRAQAENAALK----QKQQADAEMAKHKKLAEQTLKQ 2180
Cdd:COG4913 753 ERFAAALGDAVERELREnleeRIDALRARLNRAEEELERAMRA 795
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2018-2624 |
1.33e-10 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 68.28 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2018 DELDRLKKKAEEARKQKDDADK-----EAEKQILMAQ-QAAQKCSAAEQQVQSVLAQQKED-----TIMQTKLKEEYEKA 2086
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKkhqqlCEEKNALQEQlQAETELCAEAEEMRARLAARKQEleeilHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2087 KKLakQAEaaKEKAEREAALLRQQ--AEEAERQKAAAEQ--EAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQ 2162
Cdd:pfam01576 92 QQL--QNE--KKKMQQHIQDLEEQldEEEAARQKLQLEKvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2163 ADAEMAKHKKLAEQTLKQKF---QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDavkQRGQVEEELLKVKVQMEE 2239
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAmisDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAE---LQAQIAELRAQLAKKEEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2240 LLKLKLRIEEENqrlikkdkdntqkflAKEADNMKKLAEDAARLSvEAQEaarlrqiaedDLNQQRALADKMLKEKMQAI 2319
Cdd:pfam01576 245 LQAALARLEEET---------------AQKNNALKKIRELEAQIS-ELQE----------DLESERAARNKAEKQRRDLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2320 QEASRLRAEAEmlqrqKDLAQEQAQKLLEDKQlmqqrlDEETEEYQKSLEAERKRQleiiaeseklKLQVSQLSEAQAKA 2399
Cdd:pfam01576 299 EELEALKTELE-----DTLDTTAAQQELRSKR------EQEVTELKKALEEETRSH----------EAQLQEMRQKHTQA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2400 QEEAKKFKKQADSIASRLHETELAtqekmtvvekLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEmaDA 2479
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQA----------LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--SE 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2480 QQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQK-------QQMEDEKKKLQATM 2552
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlstrlRQLEDERNSLQEQL 505
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 2553 DAALNKQKEAEKEMHNKQKEMKELeRKRLEQERILAEENQKLREKLQQLEEAQKDQPDKEVIHVTMVETTKN 2624
Cdd:pfam01576 506 EEEEEAKRNVERQLSTLQAQLSDM-KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKN 576
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2133-2607 |
1.38e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.02 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2133 EDAERLRKEaeFEAAKRAqaENAALKQKQQAD------AEMAKHKKLAEQ-----TLKQKFQVEQELTKVKLKLDETDKq 2201
Cdd:COG4913 225 EAADALVEH--FDDLERA--HEALEDAREQIEllepirELAERYAAARERlaeleYLRAALRLWFAQRRLELLEAELEE- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2202 ksvLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQM-----EELLKLKLRIEEENQRLikKDKDNTQKFLAKEADNMK-K 2275
Cdd:COG4913 300 ---LRAELARLEAELERLEARLDALREELDELEAQIrgnggDRLEQLEREIERLEREL--EERERRRARLEALLAALGlP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2276 LAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQK---DLAQEQAQKLLEDK-- 2350
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDALAEAlg 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2351 ----------QLMQQRLDEEteEYQKSLE-------------AERKRQ-LEIIaESEKLKLQVSQLSEAQAKAQEEAKKF 2406
Cdd:COG4913 455 ldeaelpfvgELIEVRPEEE--RWRGAIErvlggfaltllvpPEHYAAaLRWV-NRLHLRGRLVYERVRTGLPDPERPRL 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2407 KkqADSIASRLH----------ETELATQEKMTVVEKLE----------VARLTSSK----EADDL-------------R 2449
Cdd:COG4913 532 D--PDSLAGKLDfkphpfrawlEAELGRRFDYVCVDSPEelrrhpraitRAGQVKGNgtrhEKDDRrrirsryvlgfdnR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2450 KAIADLEKEKSRLKKEAEDLQNKSKEmADAQQKQIEHEKTVLQQtfLSEKEMLLKKEKLIEEEKKRLESQ---------- 2519
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEA-LEAELDALQERREALQR--LAEYSWDEIDVASAEREIAELEAElerldassdd 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2520 ---FEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLRE 2596
Cdd:COG4913 687 laaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
570
....*....|.
gi 1927222988 2597 KLQQLEEAQKD 2607
Cdd:COG4913 767 LRENLEERIDA 777
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2172-2607 |
1.73e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2172 KLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAvkqrgqveEELLKVKVQMEELLKLKLRIEEEN 2251
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL--------EKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2252 QRLikkdkdntqKFLAKEADNMKKLAEDAARLSVEAQEAarlrqiaeddlnqQRALADKMLKEKMQAIQEASRLRAEAEM 2331
Cdd:COG4717 146 ERL---------EELEERLEELRELEEELEELEAELAEL-------------QEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2332 LQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAES----------------------EKLKLQV 2389
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIaaallallglggsllsliltiaGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2390 SQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDL 2469
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2470 QnkskemadaqQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEE-EVKKAKALKDEQERQKQQMEDEkkkL 2548
Cdd:COG4717 364 Q----------LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEElEEQLEELLGELEELLEALDEEE---L 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222988 2549 QATMDAALNKQKEAEKEMHNKQKEMKELER--KRLEQERILAEENQKLREKLQQLEEAQKD 2607
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAelEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3464-3501 |
1.86e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.49 E-value: 1.86e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1927222988 3464 LEAQMVSGGIIDPVNSHRVPIDVAYQKNIFNQKTAKNL 3501
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1729-2590 |
2.14e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 67.67 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1729 ADF-DNAEQQRSLLEDELyRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERskqlLEVEATKMR- 1806
Cdd:COG3096 271 ADYmRHANERRELSERAL-ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDH----LNLVQTALRq 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1807 ---------DLAEEASKLRA---IAEEAKHQRQVAEEEAARQRAEAERiLKEKLA---------------------AISD 1853
Cdd:COG3096 346 qekieryqeDLEELTERLEEqeeVVEEAAEQLAEAEARLEAAEEEVDS-LKSQLAdyqqaldvqqtraiqyqqavqALEK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1854 ATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQ---ANQHKQQIEEKIVLLKKSSeAEMERQRAivDDTLKQrr 1930
Cdd:COG3096 425 ARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKlsvADAARRQFEKAYELVCKIA-GEVERSQA--WQTARE-- 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1931 vVEEEIRILKLNFEKASSgkldLELELNKLKNIAEETQqsklRAEEEAEKLRKLAleeekrrreaeekvkkiaaaeeeaa 2010
Cdd:COG3096 500 -LLRRYRSQQALAQRLQQ----LRAQLAELEQRLRQQQ----NAERLLEEFCQRI------------------------- 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2011 RQRQAAQDELDRLKkkaEEARKQKDDADKEAEkqilmaqQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLA 2090
Cdd:COG3096 546 GQQLDAAEELEELL---AELEAQLEELEEQAA-------EAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2091 KQAEAAKEKAErEAALLRQQAEEAERQkaaaeqeaanqakaqedAERLRKEAefeAAKRAQAENAALKQKQQADAEMAKH 2170
Cdd:COG3096 616 EQSGEALADSQ-EVTAAMQQLLERERE-----------------ATVERDEL---AARKQALESQIERLSQPGGAEDPRL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2171 KKLAEQ----TLKQKFQ---------------------VEQELTKVKLKLDETDKqksvLDEEL---QRLKDEVDDAVKQ 2222
Cdd:COG3096 675 LALAERlggvLLSEIYDdvtledapyfsalygparhaiVVPDLSAVKEQLAGLED----CPEDLyliEGDPDSFDDSVFD 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2223 rgqVEEELLKVKVQMEELLKLKLRIEEEnQRLIKKDKDNTQKFLAKEADnmkKLAEDAARLSVEAQEAARLRQIAEDDLN 2302
Cdd:COG3096 751 ---AEELEDAVVVKLSDRQWRYSRFPEV-PLFGRAAREKRLEELRAERD---ELAEQYAKASFDVQKLQRLHQAFSQFVG 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2303 QQRALA-----DKMLKEKMQAIQEASRLRAEAE----MLQRQKDLAQEQAQ---------KLLEDKQLmQQRLDEETEEY 2364
Cdd:COG3096 824 GHLAVAfapdpEAELAALRQRRSELERELAQHRaqeqQLRQQLDQLKEQLQllnkllpqaNLLADETL-ADRLEELREEL 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2365 QKSLEAER--KRQLEIIAESEKL-------KLQVSQLSEAQAKAQEEAKKFKKQADSIasrlheTELatqekmtvvekle 2435
Cdd:COG3096 903 DAAQEAQAfiQQHGKALAQLEPLvavlqsdPEQFEQLQADYLQAKEQQRRLKQQIFAL------SEV------------- 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2436 VARLT--SSKEADDLRKAIADL-EKEKSRLKkEAEDLQNKSKEMADAQQKQIEHEKTVLQQ---TFLSEKEMLLKKEKLI 2509
Cdd:COG3096 964 VQRRPhfSYEDAVGLLGENSDLnEKLRARLE-QAEEARREAREQLRQAQAQYSQYNQVLASlksSRDAKQQTLQELEQEL 1042
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2510 EEEKKRLESQFEEevkKAKALKDEQERQKQQMEDEKkklqatmdAALNKQKEA-EKEMHNKQKEMKELERKrLEQERILA 2588
Cdd:COG3096 1043 EELGVQADAEAEE---RARIRRDELHEELSQNRSRR--------SQLEKQLTRcEAEMDSLQKRLRKAERD-YKQEREQV 1110
|
..
gi 1927222988 2589 EE 2590
Cdd:COG3096 1111 VQ 1112
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1236-1580 |
2.63e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 67.07 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1236 KQRQEKIQavtitdsKTLKEQLAQEKK-LLEEVEgNKDKVDECQKYAKAYIDtikdyelQLVAYKAQVEPLASPLKKTkl 1314
Cdd:pfam17380 287 RQQQEKFE-------KMEQERLRQEKEeKAREVE-RRRKLEEAEKARQAEMD-------RQAAIYAEQERMAMERERE-- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1315 dsasdniiQEYVTLRTKYSELMTLTSQYIKFITDSQRRLEdeekaaeKLKAEEQKKMAMMQAELD---KQKQLAEVHAKA 1391
Cdd:pfam17380 350 --------LERIRQEERKRELERIRQEEIAMEISRMRELE-------RLQMERQQKNERVRQELEaarKVKILEEERQRK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1392 IAKAEKEAQELKlRMQEEVNRREDAVVDAEKQKhniQLELHELKNLSEQQIMDKSKQvDDALQSRVKIEEEiRLIRLQLE 1471
Cdd:pfam17380 415 IQQQKVEMEQIR-AEQEEARQREVRRLEEERAR---EMERVRLEEQERQQQVERLRQ-QEEERKRKKLELE-KEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1472 TTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEEtQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLK 1551
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-ERRREAEEERRKQQEMEERRRIQEQMRKATEERSR 567
|
330 340
....*....|....*....|....*....
gi 1927222988 1552 RQAEEAERQVKQAEIEKERQIQVAHVAAQ 1580
Cdd:pfam17380 568 LEAMEREREMMRQIVESEKARAEYEATTP 596
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1236-1986 |
3.02e-10 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 67.12 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1236 KQRQEKIQAVTITDSKTLKEQLAQEKKLLEEVEGNKDKvdecqkyakayidtiKDYELQlvaykaqveplasplkkTKLD 1315
Cdd:pfam01576 203 RQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK---------------KEEELQ-----------------AALA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1316 SASDNIIQEYVTLRtKYSELMTLtsqyikfITDSQRRLEDEEKA---AEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAI 1392
Cdd:pfam01576 251 RLEEETAQKNNALK-KIRELEAQ-------ISELQEDLESERAArnkAEKQRRDLGEELEALKTELEDTLDTTAAQQELR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1393 AKAEKEAQELKLRMQEEVnRREDAVVDAEKQKHNIQLElhELKNLSEQ-----QIMDKSKQvddALQSRVK-IEEEIRLI 1466
Cdd:pfam01576 323 SKREQEVTELKKALEEET-RSHEAQLQEMRQKHTQALE--ELTEQLEQakrnkANLEKAKQ---ALESENAeLQAELRTL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1467 RLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALED 1546
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1547 LENLKRQAEEAERQVKQAEIEKE--RQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEE---SLKQEHGAVLQLQHEAAA 1621
Cdd:pfam01576 477 LQEETRQKLNLSTRLRQLEDERNslQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEdagTLEALEEGKKRLQRELEA 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1622 LKKQQEDAERAREEAEKELEKWRQKANEAL------RLRLQAEEEAHKK---SLAQEDA-------EKQKEEAE-REAKK 1684
Cdd:pfam01576 557 LTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdldhqRQLVSNLEKKQKKfdqMLAEEKAisaryaeERDRAEAEaREKET 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1685 RAKAEDSALKQKEMAENELERQRKvaestaqqKLTAEQEliRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLED 1764
Cdd:pfam01576 637 RALSLARALEEALEAKEELERTNK--------QLRAEME--DLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELED 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1765 EL-----AKVRSEMDvLIQLKSKAEKETMSNSERSKQlleveatKMRDLAEEASKLRAIAEEAKHQRQVAeeEAARQRAE 1839
Cdd:pfam01576 707 ELqatedAKLRLEVN-MQALKAQFERDLQARDEQGEE-------KRRQLVKQVRELEAELEDERKQRAQA--VAAKKKLE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1840 AEriLKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIeekivllkKSSEAEMERQR 1919
Cdd:pfam01576 777 LD--LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKL--------KNLEAELLQLQ 846
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222988 1920 AIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLK----NIAEETQQSKLRAEEEAEKLRKLAL 1986
Cdd:pfam01576 847 EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEariaQLEEELEEEQSNTELLNDRLRKSTL 917
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1766-2242 |
3.26e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.33 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1766 LAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEakhqrqVAEEEAARQRAEAERILK 1845
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE------LEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1846 EKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHkQQIEEKIVLLKKSSEAEMERQraiVDDT 1925
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL-AELQEELEELLEQLSLATEEE---LQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1926 LKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAekLRKLALEEEKRRREAEEKVKKIAAA 2005
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL--LLLIAAALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2006 EEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILmaqqaaqkcsaAEQQVQSVLAQQKEDTIMQTKLKEEYEK 2085
Cdd:COG4717 276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL-----------EEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2086 AKKLAKQAEAAKEKAEREAALLRQQAEEAErqkaaaeqeaANQAKAQEDAERLRkeaefEAAKRAQAENAALKQKQQADA 2165
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEIAA----------LLAEAGVEDEEELR-----AALEQAEEYQELKEELEELEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2166 EMAKHKKLAEQTLKQ--KFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQR--GQVEEELLKVKVQMEELL 2241
Cdd:COG4717 410 QLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELA 489
|
.
gi 1927222988 2242 K 2242
Cdd:COG4717 490 E 490
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1132-1969 |
3.39e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.99 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1132 KEVETYRTKLKKMRAEAEGEQPVFDSLEAELKKATAVSDKMSRVHSE------RDAELDHYRQLLSSLQDRWKAvfsqID 1205
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENEldplknRLKEIEHNLSKIMKLDNEIKA----LK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1206 LRQRELEQLGRQLGYYRES----YDWLIRWINDAKQRQEKIQAVTITDSKTLKEQLAQEKKLLEEvegNKDKVDECQKYA 1281
Cdd:TIGR00606 276 SRKKQMEKDNSELELKMEKvfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ---EKTELLVEQGRL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1282 KAYIDTIKDyelQLVAYKAQVEPLASPLKKTKLDSASDNIIQeyvtlrtkyselmtltsqYIKFITDSQRRLEDEEKAAE 1361
Cdd:TIGR00606 353 QLQADRHQE---HIRARDSLIQSLATRLELDGFERGPFSERQ------------------IKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1362 KLKAEEQKKMAMMQAELDK----QKQLAEVHAKAIAKAEKEAQELKLRMQeEVNRREDAVVDAEKQKHNIQLELHELKNL 1437
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEirdeKKGLGRTIELKKEILEKKQEELKFVIK-ELQQLEGSSDRILELDQELRKAERELSKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1438 SEQQIMDKSKQVDDALQS-RVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEET 1516
Cdd:TIGR00606 491 EKNSLTETLKKEVKSLQNeKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFP 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1517 QKKRMAEeelkrkaeaekeaakqkqkALEDLENLKRQAEEAERQVkQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVE 1596
Cdd:TIGR00606 571 NKKQLED-------------------WLHSKSKEINQTRDRLAKL-NKELASLEQNKNHINNELESKEEQLSSYEDKLFD 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1597 KTSKLEESLKQEhgavlQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRL---RLQAEEEAHKKSLAQED--- 1670
Cdd:TIGR00606 631 VCGSQDEESDLE-----RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVcqrVFQTEAELQEFISDLQSklr 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1671 -AEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLK 1749
Cdd:TIGR00606 706 lAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1750 ---NEVVAAQQQRKQLEDELAKVR--------SEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAI 1818
Cdd:TIGR00606 786 vclTDVTIMERFQMELKDVERKIAqqaaklqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1819 AEEAKHQRQVAEEEAARQRAEAERI------LKEKLAAISDATRLKTEAEIALKEKEAENERL-------RRQAEDEAYQ 1885
Cdd:TIGR00606 866 TNELKSEKLQIGTNLQRRQQFEEQLvelsteVQSLIREIKDAKEQDSPLETFLEKDQQEKEELissketsNKKAQDKVND 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1886 RKALEDQANQHKQQIEEKIV----LLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNF------EKASSGKLDLEL 1955
Cdd:TIGR00606 946 IKEKVKNIHGYMKDIENKIQdgkdDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIdtqkiqERWLQDNLTLRK 1025
|
890
....*....|....
gi 1927222988 1956 ELNKLKNIAEETQQ 1969
Cdd:TIGR00606 1026 RENELKEVEEELKQ 1039
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
523-712 |
3.49e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 62.85 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 523 LRYIQDLLAWVEENQHRIDEAQWGSDLPSVESQLGSHRGLHQTVEDFRSKIERARADETQL---SPVSKGAYRDYLGKLD 599
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 600 LQYGKLLNSSKSRLRNLD---SLHAFVSAATKELMWLNDKEEEEVNFDWSDRNSNMTAKKDNYSGLMRELELREKKVNDI 676
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1927222988 677 QATGDKLVRDGHPGK-KTVESFTAALQTQWSWILQLC 712
Cdd:cd00176 166 NELAEELLEEGHPDAdEEIEEKLEELNERWEELLELA 202
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2158-2606 |
4.03e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.20 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2158 KQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQM 2237
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2238 EELLKLKLRIEEENQRlikkdkdntQKFLAKEADNMKK----LAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKM-- 2311
Cdd:TIGR04523 197 LKLELLLSNLKKKIQK---------NKSLESQISELKKqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIkk 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2312 -LKEKMQAIQEASR-----------LRAEAEMLQRQK----------DLAQEQAQKLLEDKQLMQ-----QRLDEETEEY 2364
Cdd:TIGR04523 268 qLSEKQKELEQNNKkikelekqlnqLKSEISDLNNQKeqdwnkelksELKNQEKKLEEIQNQISQnnkiiSQLNEQISQL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2365 QKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKE 2444
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2445 ADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMadaqQKQIEHEKTVLQQTFLSEKEMLLKKEKlieeekkrLESQFEEEV 2524
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNL----DNTRESLETQLKVLSRSINKIKQNLEQ--------KQKELKSKE 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2525 KKAKALKdeqeRQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQE-----RILAEENQKLREKLQ 2599
Cdd:TIGR04523 496 KELKKLN----EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfelkkENLEKEIDEKNKEIE 571
|
....*..
gi 1927222988 2600 QLEEAQK 2606
Cdd:TIGR04523 572 ELKQTQK 578
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2066-2498 |
4.35e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2066 LAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFE 2145
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2146 AAKRAQAENAALKQKQQADAEMAKhKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQ 2225
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQ-EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2226 VEEELLKVKVQmEELLKLKLRIEEENQRLIKKDKDNTQK---------------FLAKEADNMKKLAEDAARLSVEAQEA 2290
Cdd:COG4717 232 LENELEAAALE-ERLKEARLLLLIAAALLALLGLGGSLLsliltiagvlflvlgLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2291 ARLRQIAEDDLNQQRA-------LADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKlledKQLMQQRLDEETEE 2363
Cdd:COG4717 311 PALEELEEEELEELLAalglppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI----AALLAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2364 YQKSLEAERKRQlEIIAESEKLKLQVSQLSEAQAKAQEEAKKfkkqaDSIASRLHETELATQEKMTVVEKL--EVARLTS 2441
Cdd:COG4717 387 LRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELreELAELEA 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222988 2442 SKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKqIEHEKTVLQQTFLSE 2498
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALEL-LEEAREEYREERLPP 516
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1408-1899 |
4.45e-10 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 66.19 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1408 EEVNRREDAVV----DAEKQKHNIQLELHELKNLSE-QQIMDKSKQVDDAlqSRVKIEEEIRLIRLQLETTVKQKSTAES 1482
Cdd:NF033838 38 EEVRGGNNPTVtssgNESQKEHAKEVESHLEKILSEiQKSLDKRKHTQNV--ALNKKLSDIKTEYLYELNVLKEKSEAEL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1483 ELKQLRDRAAEAEKLRKAAQEEAEK---LRKQVNEETQKKRMAEEELKRKAEAEKeaakqkqkaledLENLKRQAEEAER 1559
Cdd:NF033838 116 TSKTKKELDAAFEQFKKDTLEPGKKvaeATKKVEEAEKKAKDQKEEDRRNYPTNT------------YKTLELEIAESDV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1560 QVKQAEIEkerqiqvahvAAQKSAaaelqskhmsfveKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREeaeke 1639
Cdd:NF033838 184 EVKKAELE----------LVKEEA-------------KEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEE----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1640 lekwrqkanEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREA--------KKR--AKAEDSALKQKEMAENELERQRKV 1709
Cdd:NF033838 236 ---------EAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVlgepatpdKKEndAKSSDSSVGEETLPSPSLKPEKKV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1710 AEstAQQKLTAEQElirlRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAkvrsemdvliqlksKAEKETMS 1789
Cdd:NF033838 307 AE--AEKKVEEAKK----KAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELV--------------KEEAKEPR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1790 NSERSKQL-LEVEATKmrdlaEEASKLraiaEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEK 1868
Cdd:NF033838 367 NEEKIKQAkAKVESKK-----AEATRL----EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEK 437
|
490 500 510
....*....|....*....|....*....|....
gi 1927222988 1869 EAEN---ERLRRQAEDEAYQRKAlEDQANQHKQQ 1899
Cdd:NF033838 438 PAEQpkaEKPADQQAEEDYARRS-EEEYNRLTQQ 470
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2141-2608 |
5.16e-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: 66.40 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2141 EAEFEAAKRAQAENAALKQKQQAD--AEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDD 2218
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDetLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2219 AVKQRGQVEEE-LLKVKVQMEELLKLKLRIEEENQR---LIKKDKDNTQKFLAKEA----DNMKKLAEDAARLSVEAQEA 2290
Cdd:pfam12128 327 LEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERlkaLTGKHQDVTAKYNRRRSkikeQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2291 ARLRQIAEDDLNQQ-RALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQeqaqklLEDKQLMQQRL-DEETEEYQKSL 2368
Cdd:pfam12128 407 DRQLAVAEDDLQALeSELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQAT------ATPELLLQLENfDERIERAREEQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2369 EAERKRQLeiiaeseklklqvsqlseaqaKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADD- 2447
Cdd:pfam12128 481 EAANAEVE---------------------RLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHf 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2448 LRKAIADLEKEKSRLKKEAE----DLQnksKEMADAQQKQiehEKTVLQQTfLSEKEMLLKKEKLIEEEKKRLESQFEEE 2523
Cdd:pfam12128 540 LRKEAPDWEQSIGKVISPELlhrtDLD---PEVWDGSVGG---ELNLYGVK-LDLKRIDVPEWAASEEELRERLDKAEEA 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2524 VKKAKALKDEQERQKQQMEDEKKKLQATMDAA-------------LNKQKEAEKEMHNKQKEmkelERKRLEQERI--LA 2588
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETFArtalknarldlrrLFDEKQSEKDKKNKALA----ERKDSANERLnsLE 688
|
490 500
....*....|....*....|
gi 1927222988 2589 EENQKLREKLQQLEEAQKDQ 2608
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQKEQ 708
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2169-2606 |
5.20e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.81 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2169 KHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVL---DEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKL 2245
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2246 RIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDaarlsVEAQEAARLRQIaeDDLNQQRAladKMLKEKMQAIQEASRL 2325
Cdd:TIGR04523 292 QLKSEISDLNNQKEQDWNKELKSELKNQEKKLEE-----IQNQISQNNKII--SQLNEQIS---QLKKELTNSESENSEK 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2326 RAEAEMLQRQ-KDLAQEQAQKLLEDKQLMQQRLDEETE-EYQKSLEAERKRQLEIIaESEKLKL--QVSQLSEAQAKAQE 2401
Cdd:TIGR04523 362 QRELEEKQNEiEKLKKENQSYKQEIKNLESQINDLESKiQNQEKLNQQKDEQIKKL-QQEKELLekEIERLKETIIKNNS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2402 EAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQ 2481
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2482 KQIEHektvlQQTFLSEKemllkkeklieeekKRLESQFEEevKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKE 2561
Cdd:TIGR04523 521 SLKEK-----IEKLESEK--------------KEKESKISD--LEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKS 579
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1927222988 2562 AEKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQK 2606
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2079-2363 |
5.54e-10 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 65.30 E-value: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2079 LKEEYEKAKKLAKQAEAAKEK-AEREAALLRQQAEEAERQKAAAEQEAANQAKAQE---DAERLRKEAEFEAAKRA--QA 2152
Cdd:pfam07888 92 SREKHEELEEKYKELSASSEElSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLEretELERMKERAKKAGAQRKeeEA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2153 ENAALKQKQQADAEMAKHKKLAEQTLK--------QKFQVEQELTKVKLKLDETDKQKSVLDEELQR------------- 2211
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRnslaqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrslqerlnaser 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2212 ----LKDEVDDAVKQRGQVEEELLKVKVQMEEL------LKLKLRieeENQRLIKKDKDNTQKFLAKEADNMKKLAEDAA 2281
Cdd:pfam07888 252 kvegLGEELSSMAAQRDRTQAELHQARLQAAQLtlqladASLALR---EGRARWAQERETLQQSAEADKDRIEKLSAELQ 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2282 RLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEasrLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEET 2361
Cdd:pfam07888 329 RLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
..
gi 1927222988 2362 EE 2363
Cdd:pfam07888 406 DA 407
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1831-2386 |
5.79e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1831 EEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAE-----------NERLRRQAEDEAYQRKALEDqANQHKQQ 1899
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKEleevlreineiSSELPELREELEKLEKEVKE-LEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1900 IEEKiVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKlDLELELNKLKNIAEETQQSKLRAEEEAE 1979
Cdd:PRK03918 240 IEEL-EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1980 KLRKLALEEEKRRREAEEKVKKIaaaeEEAARQRQAAQDELDRLKKKA---EEARKQKDDADK-EAEKQILMAQQAAQKC 2055
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERL----EELKKKLKELEKRLEELEERHelyEEAKAKKEELERlKKRLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2056 SAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKA---------EREAALLRQQAEEAERQKAAAEQEAA 2126
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2127 NQAKAQEDAERLRKEAEfeaakraqAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLD 2206
Cdd:PRK03918 474 KERKLRKELRELEKVLK--------KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2207 EELQRLKD----------EVDDAVKQRGQVEEELLKVKVQMEELLKLKLR-IEEENQRLI-----KKDKDNTQKFLAKEA 2270
Cdd:PRK03918 546 KELEKLEElkkklaelekKLDELEEELAELLKELEELGFESVEELEERLKeLEPFYNEYLelkdaEKELEREEKELKKLE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2271 DNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRalADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDK 2350
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEE--YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
570 580 590
....*....|....*....|....*....|....*.
gi 1927222988 2351 qlmqqrldEETEEYQKSLEAERKRQLEIIAESEKLK 2386
Cdd:PRK03918 704 --------EEREKAKKELEKLEKALERVEELREKVK 731
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
47-143 |
8.08e-10 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 59.12 E-value: 8.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 47 KKTFTKWVNKHLIKSQ---------RQVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDFL 112
Cdd:cd21217 3 KEAFVEHINSLLADDPdlkhllpidPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1927222988 113 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 143
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1698-2163 |
9.21e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 9.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1698 MAENELERQRKVAES-TAQQKLTAEQELIRLRADFDNAEQQRSL---LEDELYRLKNEVVAAQQQRKQLEDELAKVRSEM 1773
Cdd:COG4717 46 MLLERLEKEADELFKpQGRKPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1774 DV--LIQLKSKAEKETMSNSERSKQLLEveatKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAI 1851
Cdd:COG4717 126 QLlpLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1852 SDATRLKTEAEIALKEKEAENERLRRQAEdeayqRKALEDQANQHKQQIEEKIVLLKksSEAEMERQRAIVDDTLKQRRV 1931
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELE-----QLENELEAAALEERLKEARLLLL--IAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1932 VEE----EIRILKLNFEKASSGKLDLELELNKLKNIAEetqQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEE 2007
Cdd:COG4717 275 IAGvlflVLGLLALLFLLLAREKASLGKEAEELQALPA---LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2008 EAARQRQAAQD-ELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKA 2086
Cdd:COG4717 352 LLREAEELEEElQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222988 2087 KKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQA 2163
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2024-2181 |
1.11e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 63.71 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2024 KKKAEEARKQKDDADKEAE--KQILMAQQAAQKCSAAEQQVQSVLAQQKEdtimQTKLKEEYEKAKKlakQAEAAKEKAE 2101
Cdd:TIGR02794 104 AKQAEQAAKQAEEKQKQAEeaKAKQAAEAKAKAEAEAERKAKEEAAKQAE----EEAKAKAAAEAKK---KAEEAKKKAE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2102 REAallrQQAEEAERQKaaaeqeaaNQAKAQEDAERLRKEAEFEAAKRAQAE----NAALKQKQQADAEMAKHKKLAEQT 2177
Cdd:TIGR02794 177 AEA----KAKAEAEAKA--------KAEEAKAKAEAAKAKAAAEAAAKAEAEaaaaAAAEAERKADEAELGDIFGLASGS 244
|
....
gi 1927222988 2178 LKQK 2181
Cdd:TIGR02794 245 NAEK 248
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1691-1913 |
1.31e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1691 SALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVR 1770
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1771 SEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQR---QVAEEEAARQRAEAERILKEK 1847
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAeelRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 1848 LAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEA 1913
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
48-142 |
1.71e-09 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 58.12 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 48 KTFTKWVNKHLIKS--QRQVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMrfhkLQNVQIALDFLKHRQVKL 119
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1927222988 120 VNIRNDDIADGNPKLTLGLIWTI 142
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2380-2593 |
1.89e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2380 AESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEvarltssKEADDLRKAIADLEKEK 2459
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-------QELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2460 SRLKKEAEDLQNKSKEMADAQQKQIEHEKTVL----------------QQTFLSEKEMLLKKEKLIEEEKKRLESQFEEE 2523
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2524 VKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQK 2593
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2028-2175 |
2.41e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 62.97 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2028 EEARKQKDDADKEAEKQILMA-QQAAQKCSAAEQQVQS--VLAQQKEDTIMQTKLKEEYEKAKKLAKQA-EAAKEKAERE 2103
Cdd:COG2268 199 RDARIAEAEAERETEIAIAQAnREAEEAELEQEREIETarIAEAEAELAKKKAEERREAETARAEAEAAyEIAEANAERE 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 2104 aalLRQQAEEAERQKAAAEqeaanqakAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAE 2175
Cdd:COG2268 279 ---VQRQLEIAEREREIEL--------QEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAE 339
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1673-2443 |
2.41e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.97 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1673 KQKEEAEREAKKRAKAEdSALKQKEmaeNELERQRKV--AESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYR--- 1747
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIE-AELKQKE---NKLQENRKIieAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlc 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1748 --LKNEVVAAQQQRKQLEDELAKVRSemdVLIQLKSKAEKETMSNSErskqlLEVEATKMRdlAEEASKLRAIAEEAKHQ 1825
Cdd:pfam05483 158 nlLKETCARSAEKTKKYEYEREETRQ---VYMDLNNNIEKMILAFEE-----LRVQAENAR--LEMHFKLKEDHEKIQHL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1826 RQVAEEEAARQRAEAERIL---KEKLAAISDATRLKTEAEIALKEKEaenERLRRQAEDEayqrkaleDQANQHKQQIEE 1902
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLiqiTEKENKMKDLTFLLEESRDKANQLE---EKTKLQDENL--------KELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1903 KIVLLKKSSEAEMERQRAIVDDTLKQRRVV-----EEEIRILKLNFEKASSGKLDLELELN--KLKNIAEeTQQSKLRAE 1975
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLQIATKTIcqlteEKEAQMEELNKAKAAHSFVVTEFEATtcSLEELLR-TEQQRLEKN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1976 EEAEKLRKLALEEEKRRREAEEKVKKiaaaeeeaarqrqAAQDELDRLKKKAEEARKQKDDaDKEAEKqilmaqqAAQKC 2055
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTKFKN-------------NKEVELEELKKILAEDEKLLDE-KKQFEK-------IAEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2056 SAAEQQVQSVLaqqkedtimQTKLKEEYEkakkLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDA 2135
Cdd:pfam05483 435 KGKEQELIFLL---------QAREKEIHD----LEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2136 ERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDE 2215
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2216 VDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKklaedaarlsVEAQEAARLRQ 2295
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK----------LELELASAKQK 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2296 IAEDDLNQQRALADKMLKEK--MQAIQEASRLRAEAEMLQRQKDLAQEqaQKLLEDKQLMQQrldeETEEYQKSLEaERK 2373
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKISEEklLEEVEKAKAIADEAVKLQKEIDKRCQ--HKIAEMVALMEK----HKHQYDKIIE-ERD 724
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2374 RQLEIIAESEKlklqvsQLSEAQAKAQEEAKKFKKQADSIASRLhETELATQEKMTVVEKLEVARLTSSK 2443
Cdd:pfam05483 725 SELGLYKNKEQ------EQSSAKAALEIELSNIKAELLSLKKQL-EIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2021-2406 |
2.70e-09 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 63.92 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2021 DRLKKKAEEARKQKDDADKEaekqILMAQQAAQKcSAAEQQVQSVLAQQKEDTI---------MQTKLKEEYEKAKKLAK 2091
Cdd:PRK10929 26 KQITQELEQAKAAKTPAQAE----IVEALQSALN-WLEERKGSLERAKQYQQVIdnfpklsaeLRQQLNNERDEPRSVPP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2092 Q---AEAAKEKAEREAALL---RQQAEEAERQKAAAEQEAANQAKaQEDAERLRKEAEfeaaKRAQAE---NAALKQKQ- 2161
Cdd:PRK10929 101 NmstDALEQEILQVSSQLLeksRQAQQEQDRAREISDSLSQLPQQ-QTEARRQLNEIE----RRLQTLgtpNTPLAQAQl 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2162 -QADAEMAKHK-KLAEQTLKQ-KFQVEQELTKVKLKLDEtdKQKSVLDEELQRLKDEVDDavkQRGQVEEELLkvkvqme 2238
Cdd:PRK10929 176 tALQAESAALKaLVDELELAQlSANNRQELARLRSELAK--KRSQQLDAYLQALRNQLNS---QRQREAERAL------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2239 ellklklrieeENQRLIKKDKDNTQKFLAKEadnMKKLAEDAARLSVEAQE----AARLRQIAEDDLNQQRALAdkMLKE 2314
Cdd:PRK10929 244 -----------ESTELLAEQSGDLPKSIVAQ---FKINRELSQALNQQAQRmdliASQQRQAASQTLQVRQALN--TLRE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2315 KMQ------AIQEAsrLRAEA----EMLQRQK---DLAQEQAQKLLEDKQLMQQRLDEE---------TEEYQKSLEAER 2372
Cdd:PRK10929 308 QSQwlgvsnALGEA--LRAQVarlpEMPKPQQldtEMAQLRVQRLRYEDLLNKQPQLRQirqadgqplTAEQNRILDAQL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1927222988 2373 KRQLEI-----------IAESEKLKLQVSQLSEAQAKAQEEAKKF 2406
Cdd:PRK10929 386 RTQRELlnsllsggdtlILELTKLKVANSQLEDALKEVNEATHRY 430
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1159-1832 |
3.37e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 63.53 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1159 EAELKKATAVSDKMSRVHSERDAELDHYR----QLLSSLQDRWKAVFSQIDLRQRELEQLGRQLGYY---RESYDWLIRW 1231
Cdd:TIGR00606 503 VKSLQNEKADLDRKLRKLDQEMEQLNHHTttrtQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnkKQLEDWLHSK 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1232 INDAKQRQEKIQAVT--ITDSKTLKEQLAQEKKLLEEVEgnkdkvdecQKYAKAYIDTI--KDYELQLVAYKAQVEPLAs 1307
Cdd:TIGR00606 583 SKEINQTRDRLAKLNkeLASLEQNKNHINNELESKEEQL---------SSYEDKLFDVCgsQDEESDLERLKEEIEKSS- 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1308 plKKTKLDSASDNIIQEYVTLRTKYSE----LMTLTSQYIKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQ 1383
Cdd:TIGR00606 653 --KQRAMLAGATAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLG 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1384 LAEVHAKAIAKAEKEAQELKLRMQEeVNRredavvDAEKQKHNIQLELHELknlseQQIMDKSKQVDDaLQSRVKIEEei 1463
Cdd:TIGR00606 731 LAPGRQSIIDLKEKEIPELRNKLQK-VNR------DIQRLKNDIEEQETLL-----GTIMPEEESAKV-CLTDVTIME-- 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1464 rliRLQLETTVKQKSTAESELK-QLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEelkrkaeaekeaakqkqk 1542
Cdd:TIGR00606 796 ---RFQMELKDVERKIAQQAAKlQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQD------------------ 854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1543 aledlenlkRQAEEAERQVKQAEIEKERqIQVAHVAAQKSAAAElqskhmSFVEKTSKLEESLKQEHGAVLQLQHEAAAL 1622
Cdd:TIGR00606 855 ---------QQEQIQHLKSKTNELKSEK-LQIGTNLQRRQQFEE------QLVELSTEVQSLIREIKDAKEQDSPLETFL 918
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1623 KKQQEDAERAREEAEKELEKWRQKANEAlrlrlqaEEEAHKKSLAQEDAEKqkeeaereakkraKAEDSALKQKEMAENE 1702
Cdd:TIGR00606 919 EKDQQEKEELISSKETSNKKAQDKVNDI-------KEKVKNIHGYMKDIEN-------------KIQDGKDDYLKQKETE 978
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1703 LERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEvvaaqQQRKQLEDELAKVRSEMDVLIQLKSK 1782
Cdd:TIGR00606 979 LNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRE-----NELKEVEEELKQHLKEMGQMQVLQMK 1053
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1927222988 1783 AEKETMSNSERSKQLLEVEA-TKMRDLAEEasKLRAIAEEAKHQRQVAEEE 1832
Cdd:TIGR00606 1054 QEHQKLEENIDLIKRNHVLAlGRQKGYEKE--IKHFKKELREPQFRDAEEK 1102
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2805-2842 |
3.85e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 54.64 E-value: 3.85e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1927222988 2805 VLEAQCATGGIIDPINSHRVPNEIAYKQGQYDHEMNKI 2842
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2079-2607 |
3.95e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.21 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2079 LKEEYEKAKKLAKQAEAAKEKAEREAALLRQ-------QAEEAERQKAAAEQEAANQAKAQEDAERLRKEA--EFEAAKR 2149
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidlqtKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTvhELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2150 AQAE-----NAALKQKQQ----------------ADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVL--- 2205
Cdd:pfam15921 160 LKEDmledsNTQIEQLRKmmlshegvlqeirsilVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLkgr 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2206 ----DEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADN-----MKKL 2276
Cdd:pfam15921 240 ifpvEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNqnsmyMRQL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2277 AE---DAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKE----KMQAIQEASRLRAE-----AEMLQRQKDLAQEQAQ 2344
Cdd:pfam15921 320 SDlesTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEarteRDQFSQESGNLDDQlqkllADLHKREKELSLEKEQ 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2345 -------------------KLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKK 2405
Cdd:pfam15921 400 nkrlwdrdtgnsitidhlrRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2406 FKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIE 2485
Cdd:pfam15921 480 VVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAE 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2486 HEKT--VLQQTFLSEKEMLLK---KEKLIEEEKKRLESQFEE---EVKKAKALKDEQERQKQQMED-------EKKKL-- 2548
Cdd:pfam15921 560 KDKVieILRQQIENMTQLVGQhgrTAGAMQVEKAQLEKEINDrrlELQEFKILKDKKDAKIRELEArvsdlelEKVKLvn 639
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 2549 ------------QATMDAALNKQKEAEKEMHNKQKEMKELERKRleqeRILAEENQKLREKLQ-QLEEAQKD 2607
Cdd:pfam15921 640 agserlravkdiKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF----RNKSEEMETTTNKLKmQLKSAQSE 707
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1699-1920 |
4.10e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.15 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1699 AENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQ 1778
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1779 lkskaekeTMSNSERSKQLLEV--EATKMRDLAEEASKLRAIAEEAK---HQRQVAEEEAARQRAEAERILKEKLAAISD 1853
Cdd:COG3883 94 --------ALYRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADAdllEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222988 1854 ATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRA 1920
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4306-4340 |
4.23e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.80 E-value: 4.23e-09
10 20 30
....*....|....*....|....*....|....*
gi 1927222988 4306 QRLLEAQACTGGIIDPTTGERFSVTDATEKGLVDK 4340
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDP 35
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1596-1985 |
5.15e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1596 EKTSKLEEsLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANealRLRLQAEEEAHKKSLAQEDAEKQk 1675
Cdd:COG4717 75 ELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ---LLPLYQELEALEAELAELPERLE- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1676 eeaerEAKKRAKAEDSALKQKEMAENELER-QRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVA 1754
Cdd:COG4717 150 -----ELEERLEELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1755 AQQQRKQLEDE---------------LAKVRSEMDVLIQLKSKAEKET-----------------MSNSERSKQLLEVEA 1802
Cdd:COG4717 225 LEEELEQLENEleaaaleerlkearlLLLIAAALLALLGLGGSLLSLIltiagvlflvlgllallFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1803 TKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDE 1882
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1883 A--YQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQR-RVVEEEIRILKLNFEKASSGKLDLELELNK 1959
Cdd:COG4717 385 EelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420
....*....|....*....|....*.
gi 1927222988 1960 LKNiAEETQQSKLRAEEEAEKLRKLA 1985
Cdd:COG4717 465 LEE-DGELAELLQELEELKAELRELA 489
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1785-2118 |
5.64e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.45 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1785 KETMSNSERSKQLLEVEATKMRDLAEEasklraIAEEAKHQRQVAEEEAARQrAEAERilkeKLAAISDATRLKTEAE-- 1862
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEE------KAREVERRRKLEEAEKARQ-AEMDR----QAAIYAEQERMAMEREre 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1863 ---IALKEKEAENERLRRQAEDEAYQR----KALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEE- 1934
Cdd:pfam17380 350 lerIRQEERKRELERIRQEEIAMEISRmrelERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEq 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1935 ----EIRILKLNFEKASsgkldlELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAa 2010
Cdd:pfam17380 430 eearQREVRRLEEERAR------EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE- 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2011 rqrqaaqdelDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEdtiMQTKLKEEYEKAKKLa 2090
Cdd:pfam17380 503 ----------ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRR---IQEQMRKATEERSRL- 568
|
330 340
....*....|....*....|....*...
gi 1927222988 2091 kqaeaakEKAEREAALLRQQAEEAERQK 2118
Cdd:pfam17380 569 -------EAMEREREMMRQIVESEKARA 589
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2162-2403 |
6.15e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.38 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2162 QADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELlkvkVQMEELL 2241
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----EERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2242 KLKLRIEEENQRLIKK-----DKDNTQKFLAKeADNMKKLAEDAARLsVEAQEAARlrqiaeDDLNQQRALADKMLKEKM 2316
Cdd:COG3883 89 GERARALYRSGGSVSYldvllGSESFSDFLDR-LSALSKIADADADL-LEELKADK------AELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2317 QAIQEASRLRAEaemLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQ 2396
Cdd:COG3883 161 ALKAELEAAKAE---LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
....*..
gi 1927222988 2397 AKAQEEA 2403
Cdd:COG3883 238 AAAAAAA 244
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1227-1903 |
7.31e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 62.43 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1227 WLIRWINDAKQRQEKIQ---AVTITDSKTLKE-QLAQEK---KLLEEVEGNKDKVDEcQKYAKAYIDTIKdyelQLVAYK 1299
Cdd:pfam05483 93 WKVSIEAELKQKENKLQenrKIIEAQRKAIQElQFENEKvslKLEEEIQENKDLIKE-NNATRHLCNLLK----ETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1300 AQveplasplKKTKLDSASDNIIQEYVTLRTKYsELMTLTSQYIKFITDSQR-----RLEDEEKAAEKLKAEEQKKMAmm 1374
Cdd:pfam05483 168 AE--------KTKKYEYEREETRQVYMDLNNNI-EKMILAFEELRVQAENARlemhfKLKEDHEKIQHLEEEYKKEIN-- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1375 qaelDKQKQLAEVHAKAIAKAEK---------EAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELKnLSEQQIMDK 1445
Cdd:pfam05483 237 ----DKEKQVSLLLIQITEKENKmkdltflleESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIK-MSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1446 SKQVDDALQSRVK-IEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQ---VNEETQKKRM 1521
Cdd:pfam05483 312 QKALEEDLQIATKtICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQlkiITMELQKKSS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1522 AEEELKRKAEAEKEAAKQKQKALEDLENL---KRQAEEAERQVKQAEIE-----KERQIQVAHVAAQ------------- 1580
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILAEDEKLldeKKQFEKIAEELKGKEQElifllQAREKEIHDLEIQltaiktseehylk 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1581 --KSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAE 1658
Cdd:pfam05483 472 evEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1659 EEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQR 1738
Cdd:pfam05483 552 SVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1739 SLLEDELYRLKNEVVAAQQQRKQLEDELAKVrsemdvlIQLKSKAEKETMSNSERSKQLLEvEATKMRD-----LAEEAS 1813
Cdd:pfam05483 632 NAYEIKVNKLELELASAKQKFEEIIDNYQKE-------IEDKKISEEKLLEEVEKAKAIAD-EAVKLQKeidkrCQHKIA 703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1814 KLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKlaaisdaTRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQA 1893
Cdd:pfam05483 704 EMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQ-------SSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA 776
|
730
....*....|
gi 1927222988 1894 NQHKQQIEEK 1903
Cdd:pfam05483 777 KENTAILKDK 786
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1294-1846 |
8.79e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 62.15 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1294 QLVAYKAQveplaSPLKKTKLDSASDNIIQ---EYVTLRTKyseLMTLTSQYikfiTDSQRRLEdeeKAAEKLKAEEQKK 1370
Cdd:pfam10174 276 QMEVYKSH-----SKFMKNKIDQLKQELSKkesELLALQTK---LETLTNQN----SDCKQHIE---VLKESLTAKEQRA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1371 mAMMQAELDKQKQLAEVHAKAIAKAEKEAQEL---KLRMQEEVNRREDaVVDAEKQKHNIqleLHE-LKNLSEQqIMDKS 1446
Cdd:pfam10174 341 -AILQTEVDALRLRLEEKESFLNKKTKQLQDLteeKSTLAGEIRDLKD-MLDVKERKINV---LQKkIENLQEQ-LRDKD 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1447 KQVDDaLQSRVKieeeirliRLQLETtvkqkSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQvneetqkkrmaeeel 1526
Cdd:pfam10174 415 KQLAG-LKERVK--------SLQTDS-----SNTDTALTTLEEALSEKERIIERLKEQREREDRE--------------- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1527 krkaeaekeaakqkqkALEDLENLKRQAEEAERQVKQAEIEKerqiqvahvAAQKSAAAELQSKHMSFVEKTSKLEESLK 1606
Cdd:pfam10174 466 ----------------RLEELESLKKENKDLKEKVSALQPEL---------TEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1607 QEHGAVLQLQHEAAALKKQQEDAERAREEAekelekwRQKANEALRLRLQAEEEAHKKslaqEDAEKQKEEAEREAkkra 1686
Cdd:pfam10174 521 SLEIAVEQKKEECSKLENQLKKAHNAEEAV-------RTNPEINDRIRLLEQEVARYK----EESGKAQAEVERLL---- 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1687 kaedSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLED-- 1764
Cdd:pfam10174 586 ----GILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEElm 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1765 -ELAKVRSEMDVLIQ-----LKSKAEKETMSNS---ERSKQLLEVEATKMRDLAEEASKLRA-IA--EEAKHQRQVAEEE 1832
Cdd:pfam10174 662 gALEKTRQELDATKArlsstQQSLAEKDGHLTNlraERRKQLEEILEMKQEALLAAISEKDAnIAllELSSSKKKKTQEE 741
|
570
....*....|....
gi 1927222988 1833 AARQRAEAERILKE 1846
Cdd:pfam10174 742 VMALKREKDRLVHQ 755
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1968-2169 |
9.93e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.98 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1968 QQSKLRAEEEAEKLRKlaleeekRRREAEEKVKKIAAAEEEAARQrqaaqdeldrlKKKAEEARKQKDDADKEAEKQILM 2047
Cdd:PRK09510 79 EQRKKKEQQQAEELQQ-------KQAAEQERLKQLEKERLAAQEQ-----------KKQAEEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2048 AQQAAQKCSAAEQQVQSVLAQQKEDtimQTKLKEEYEKAKklaKQAEAAKEKAEREAAlLRQQAEEAERQKAAAEQEAAN 2127
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAAKKAAA---EAKKKAEAEAAK---KAAAEAKKKAEAEAA-AKAAAEAKKKAEAEAKKKAAA 213
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1927222988 2128 QAKAQEDAERLRKEAEFEAAKRAQAENAAlKQKQQADAEMAK 2169
Cdd:PRK09510 214 EAKKKAAAEAKAAAAKAAAEAKAAAEKAA-AAKAAEKAAAAK 254
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1552-1902 |
1.16e-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: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1552 RQAEEAERQVKQA-EIEKERQIQVAHVAAQKSAAAELQSKhmsfVEKTSKLEESLKQEH-GAVLQLQHEAAALKKQQEda 1629
Cdd:COG3096 275 RHANERRELSERAlELRRELFGARRQLAEEQYRLVEMARE----LEELSARESDLEQDYqAASDHLNLVQTALRQQEK-- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1630 erareeaekeLEKWRQKANEA-LRLRLQAE--EEAHKKslaQEDAEKQKEEAEREAKkRAKaedSALKQKEMAENELERq 1706
Cdd:COG3096 349 ----------IERYQEDLEELtERLEEQEEvvEEAAEQ---LAEAEARLEAAEEEVD-SLK---SQLADYQQALDVQQT- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1707 RKVAESTAQQKLTAEQELIRLRA-DFDNAEQQRSLLEDELYRLkNEVVAAQQQRKQLEDElakVRSEMDVLIQLKSK--A 1783
Cdd:COG3096 411 RAIQYQQAVQALEKARALCGLPDlTPENAEDYLAAFRAKEQQA-TEEVLELEQKLSVADA---ARRQFEKAYELVCKiaG 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1784 EKETMSNSERSKQLLEvEATKMRDLAEEASKLRAiaeeakhqrQVAE-EEAARQRAEAERILKEKLAAISDATRLKTEAE 1862
Cdd:COG3096 487 EVERSQAWQTARELLR-RYRSQQALAQRLQQLRA---------QLAElEQRLRQQQNAERLLEEFCQRIGQQLDAAEELE 556
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1927222988 1863 IALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEE 1902
Cdd:COG3096 557 ELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE 596
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2042-2623 |
1.29e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 61.74 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2042 EKQILMAQQAAQkcsaaeqqvqsvlaQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALL------RQQAEEAE 2115
Cdd:PRK10246 232 EKQLLTAQQQQQ--------------QSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALslaqpaRQLRPHWE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2116 RQKAAAEQEAANQAKAQEDAERLRKEAefeaAKRAQAENAALKQKQQADAEMAKHKK-LAEQ---------------TLK 2179
Cdd:PRK10246 298 RIQEQSAALAHTRQQIEEVNTRLQSTM----ALRARIRHHAAKQSAELQAQQQSLNTwLAEHdrfrqwnnelagwraQFS 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2180 QKFQVEQELTKVKLKLDETDKQKSVL-DEELQRLKDEVDDAVKQRGQ---VEEELLKVKVQMEELLKLKLRIEEENQRLI 2255
Cdd:PRK10246 374 QQTSDREQLRQWQQQLTHAEQKLNALpAITLTLTADEVAAALAQHAEqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVT 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2256 KKDKDNTQKFLAKEAD---------NMKKLAEDAARLSVEAQEAARLR-------------------QIAEDDLNQQRAl 2307
Cdd:PRK10246 454 QEQTQRNAALNEMRQRykektqqlaDVKTICEQEARIKDLEAQRAQLQagqpcplcgstshpaveayQALEPGVNQSRL- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2308 aDKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDkqlmQQRLDEETEEYQKSLEAERKRQLEI---IAESEK 2384
Cdd:PRK10246 533 -DALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQE----EQALTQQWQAVCASLNITLQPQDDIqpwLDAQEE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2385 LKLQVSQLSEAQ------AKAQEEAKKFKKQADsiasrlhetelatQEKMTVVEKLEVARLTSSKEADdlrkaiadleke 2458
Cdd:PRK10246 608 HERQLRLLSQRHelqgqiAAHNQQIIQYQQQIE-------------QRQQQLLTALAGYALTLPQEDE------------ 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2459 ksrlkkEAEDLQNKSKEMADAQQKQIEHekTVLQQTfLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAK----ALKDEQ 2534
Cdd:PRK10246 663 ------EASWLATRQQEAQSWQQRQNEL--TALQNR-IQQLTPLLETLPQSDDLPHSEETVALDNWRQVHeqclSLHSQL 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2535 ERQKQQMEDEKKKL---QATMDAALNKQKEAEKE-----------MHNKQKEMKELERKRLEQERILAEENQKLREKLQQ 2600
Cdd:PRK10246 734 QTLQQQDVLEAQRLqkaQAQFDTALQASVFDDQQaflaalldeetLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQH 813
|
650 660
....*....|....*....|...
gi 1927222988 2601 LEEAQKDQPDKEVIHVTMVETTK 2623
Cdd:PRK10246 814 RPDGLDLTVTVEQIQQELAQLAQ 836
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1469-1717 |
1.39e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1469 QLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAeaekeaakqkqkalEDLE 1548
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE--------------AELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1549 NLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKhmsfvEKTSKLEESLKQEHGAVLQLQHEAAALKKQQED 1628
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSP-----EDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1629 AERAREEAEKELEKWRQ--KANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQ 1706
Cdd:COG4942 162 LAALRAELEAERAELEAllAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
250
....*....|.
gi 1927222988 1707 RKVAESTAQQK 1717
Cdd:COG4942 242 RTPAAGFAALK 252
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
46-145 |
1.40e-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: 55.59 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 46 QKKTFTKWVNKHLIKSQrqVTDLYEDLRDGHNLISLLEVLSGETLPREKG-----RMRFHKLQNVQIALDFLKHRQVKLV 120
Cdd:cd21299 5 EERCFRLWINSLGIDTY--VNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 1927222988 121 NIRNDDIADGNPKLTLGLIWTIILH 145
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1352-2111 |
1.62e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1352 RLEDEEKAAEKLKaEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKlrmqEEVNRREDAVVDAEKQKHNIQLEL 1431
Cdd:PRK03918 156 GLDDYENAYKNLG-EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVL----REINEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1432 HELKNLSEQqIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKqkstaesELKQLRDRAAEAEKLRKAAqEEAEKLRKQ 1511
Cdd:PRK03918 231 KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKK-------EIEELEEKVKELKELKEKA-EEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1512 VNEETQKKRMAEEELkrkaeaekeaakqkqkaledlENLKRQAEEAERQVKQAEIEKERqiqvahvaaqksaaaelqskh 1591
Cdd:PRK03918 302 YEEYLDELREIEKRL---------------------SRLEEEINGIEERIKELEEKEER--------------------- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1592 msfVEKTSKLEESLKQEHGAvlqlqheaaalkkqqedaerareeaekeLEKWRQKANEALRLrlQAEEEAHKKSLAQEDA 1671
Cdd:PRK03918 340 ---LEELKKKLKELEKRLEE----------------------------LEERHELYEEAKAK--KEELERLKKRLTGLTP 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1672 EKQKEEAEREAKKRAKAEDsalkqkemAENELERQRKVAESTAQQKLTAEQELirLRADFDNAEQQRSLLEDELYRLKNE 1751
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEE--------EISKITARIGELKKEIKELKKAIEEL--KKAKGKCPVCGRELTEEHRKELLEE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1752 VVAaqqqrkqledELAKVRSEMDVLIQLKSKAEKEtmsnserskqllEVEATKMRDLAEEASKLRAIAEEAKHqrqvaee 1831
Cdd:PRK03918 457 YTA----------ELKRIEKELKEIEEKERKLRKE------------LRELEKVLKKESELIKLKELAEQLKE------- 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1832 eaarqraeaeriLKEKLAAISDATrlkteaeiaLKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSS 1911
Cdd:PRK03918 508 ------------LEEKLKKYNLEE---------LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1912 EAEMERQ---RAIVDDTLKQRRVVEEEIRILKLNFEK---ASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLa 1985
Cdd:PRK03918 567 ELEEELAellKELEELGFESVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL- 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1986 leeekRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKqilmaqqaaqkcsaaeqqvqsv 2065
Cdd:PRK03918 646 -----RKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK---------------------- 698
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1927222988 2066 LAQQKEDtimQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQA 2111
Cdd:PRK03918 699 LKEELEE---REKAKKELEKLEKALERVEELREKVKKYKALLKERA 741
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
156-258 |
1.66e-08 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 55.56 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 156 QSEDMTAKEKLLLWSQ-RMTDgyqgIRCDNFTTSWRDGKLFNAVIHKHYPRLV-DMGRVYRQTNLENLEQAFGVAERDLG 233
Cdd:cd21315 11 DGKGPTPKQRLLGWIQsKVPD----LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLD 86
|
90 100
....*....|....*....|....*
gi 1927222988 234 VTRLLDPEDVDVPHPDEKSIITYVS 258
Cdd:cd21315 87 VPQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1641-2392 |
1.91e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.01 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1641 EKWRQKAN--EALRLRLQAEEEAHKKSLAQEdAEKQKEEAEREAKKRakaedsalkqKEMAENELERQRKVAESTaqqkl 1718
Cdd:pfam12128 244 TKLQQEFNtlESAELRLSHLHFGYKSDETLI-ASRQEERQETSAELN----------QLLRTLDDQWKEKRDELN----- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1719 taeQELIRLRADFDNAEQQRSLLEDELYRLKNEVVaaqQQRKQLEDELAKVRSEMdvliqlkskaeketmSNSERSKQLL 1798
Cdd:pfam12128 308 ---GELSAADAAVAKDRSELEALEDQHGAFLDADI---ETAAADQEQLPSWQSEL---------------ENLEERLKAL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1799 EveaTKMRDLAEEASKLRA-IAEEAKHQRQVAEEEAARQRAEAERilkeKLAAISDA-----TRLKTEAEIALKEKEAEN 1872
Cdd:pfam12128 367 T---GKHQDVTAKYNRRRSkIKEQNNRDIAGIKDKLAKIREARDR----QLAVAEDDlqaleSELREQLEAGKLEFNEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1873 ERLRRQAEDEayqrKALEDQAnqhkqQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLD 1952
Cdd:pfam12128 440 YRLKSRLGEL----KLRLNQA-----TATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1953 LELELNKLKNIAEETQQ----------SKLRAEEE--AEKLRKLALEEEKRRREAEEKVKKIAAAEEE------------ 2008
Cdd:pfam12128 511 ASRRLEERQSALDELELqlfpqagtllHFLRKEAPdwEQSIGKVISPELLHRTDLDPEVWDGSVGGELnlygvkldlkri 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2009 AARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTI--------MQTKLK 2080
Cdd:pfam12128 591 DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRrlfdekqsEKDKKN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2081 EEYEKAKK--------LAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQA 2152
Cdd:pfam12128 671 KALAERKDsanerlnsLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELK 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2153 --------ENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQksvldeELQRLKDEVDDavkqrg 2224
Cdd:pfam12128 751 aletwykrDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQ------RRPRLATQLSN------ 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2225 qVEEELLKVKVQMEellklklRIEEENQRLIKKdkdntqkfLAKEADNMKKLA----EDAARLSVEAQEAARLRQIAEDD 2300
Cdd:pfam12128 819 -IERAISELQQQLA-------RLIADTKLRRAK--------LEMERKASEKQQvrlsENLRGLRCEMSKLATLKEDANSE 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2301 lnqqraladkmlkekmQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLED-----KQLMQQRLDEETEEYQKSLEAERKRQ 2375
Cdd:pfam12128 883 ----------------QAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREEDHYQNDKG 946
|
810
....*....|....*..
gi 1927222988 2376 LEIIAESEKLKlQVSQL 2392
Cdd:pfam12128 947 IRLLDYRKLVP-YLEQW 962
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2246-2482 |
1.94e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2246 RIEEENQRL--IKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEAS 2323
Cdd:COG4942 21 AAAEAEAELeqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2324 RLRAE-AEMLQRQKDLAQEQAQKLL---EDKQLMQQRLdeeteEYQKSLEAERKRQLEiiaeseKLKLQVSQLSEAQAKA 2399
Cdd:COG4942 101 AQKEElAELLRALYRLGRQPPLALLlspEDFLDAVRRL-----QYLKYLAPARREQAE------ELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2400 QEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADA 2479
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 1927222988 2480 QQK 2482
Cdd:COG4942 250 ALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2206-2415 |
2.00e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2206 DEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLiKKDKDNTQKFLAKEADNMKKLAEDAARLSV 2285
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2286 EAQEAARLRQIAE--------DDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRL 2357
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 2358 DEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIAS 2415
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1546-1961 |
2.24e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 60.84 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1546 DLENLKRQAEEAE--RQVKQAEIEKERQIQVAHVAAQKSAAAELQsKHMSFVEKTSKLEESLKQEhgaVLQLQHEAAALK 1623
Cdd:PRK10929 24 DEKQITQELEQAKaaKTPAQAEIVEALQSALNWLEERKGSLERAK-QYQQVIDNFPKLSAELRQQ---LNNERDEPRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1624 KQQEDAERARE---EAEKELEKWRQKANEALRLRLQAEeeahkkSLAQedAEKQKEEAER---EAKKRAKAEDSALKQKE 1697
Cdd:PRK10929 100 PNMSTDALEQEilqVSSQLLEKSRQAQQEQDRAREISD------SLSQ--LPQQQTEARRqlnEIERRLQTLGTPNTPLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1698 MAENELeRQrkvAESTAQQKLTAEQELIRLRAdfdNAEQqrslledELYRLKNEVvaAQQQRKQLEDELAKVRSemdvli 1777
Cdd:PRK10929 172 QAQLTA-LQ---AESAALKALVDELELAQLSA---NNRQ-------ELARLRSEL--AKKRSQQLDAYLQALRN------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1778 QLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAaisdatrL 1857
Cdd:PRK10929 230 QLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQA-------L 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1858 KTEAEIA--LKEKEAENERLRRQA----EDEAYQRkaLEDQANQ---HKQQIEEkivLLKKSSEAEMERQRAIVDDTLKQ 1928
Cdd:PRK10929 303 NTLREQSqwLGVSNALGEALRAQVarlpEMPKPQQ--LDTEMAQlrvQRLRYED---LLNKQPQLRQIRQADGQPLTAEQ 377
|
410 420 430
....*....|....*....|....*....|...
gi 1927222988 1929 RRVVEEEIRILKLNFEKASSGKLDLELELNKLK 1961
Cdd:PRK10929 378 NRILDAQLRTQRELLNSLLSGGDTLILELTKLK 410
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4384-4422 |
2.49e-08 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 52.33 E-value: 2.49e-08
10 20 30
....*....|....*....|....*....|....*....
gi 1927222988 4384 FLEIQYLTGGLIEPDVEGRVSLDESIRKGTIDARTAQKL 4422
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2020-2415 |
2.51e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2020 LDRLKKKAEEARKQK-------DDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQ 2092
Cdd:COG4717 48 LERLEKEADELFKPQgrkpelnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2093 AEAAKE--KAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKH 2170
Cdd:COG4717 128 LPLYQEleALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2171 KKLAEQTLKQKfQVEQELTKVKLKLDETDKQKSVLDEELQRLK----------------DEVDDAVKQRGQV-------- 2226
Cdd:COG4717 208 LAELEEELEEA-QEELEELEEELEQLENELEAAALEERLKEARlllliaaallallglgGSLLSLILTIAGVlflvlgll 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2227 ---------EEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIA 2297
Cdd:COG4717 287 allflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2298 EDDLNQQRALA------DKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLmqQRLDEETEEYQKSLEAE 2371
Cdd:COG4717 367 ELEQEIAALLAeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEEL 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2372 RKRQLEIIAESEKLKLQVSQL------SEAQAKAQEEAKKFKKQADSIAS 2415
Cdd:COG4717 445 EEELEELREELAELEAELEQLeedgelAELLQELEELKAELRELAEEWAA 494
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2010-2218 |
2.60e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.43 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2010 ARQRQAAQDELDRLKKKAEEARKQKDD-ADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEdtimqtkLKEEYEKAKK 2088
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQRKKKEQQQAEElQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA-------ALKQKQAEEA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2089 LAKQAEAAKEKAEREAALLRQQAEEAERQKaAAEQEAANQAKAQEDAerlRKEAEFEAAKRAQAE---NAALKQKQQADA 2165
Cdd:PRK09510 138 AAKAAAAAKAKAEAEAKRAAAAAKKAAAEA-KKKAEAEAAKKAAAEA---KKKAEAEAAAKAAAEakkKAEAEAKKKAAA 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1927222988 2166 EmAKHKKLAEqtlkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDD 2218
Cdd:PRK09510 214 E-AKKKAAAE----AKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1973-2417 |
2.68e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1973 RAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEK--QILMAQQ 2050
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2051 AAQKCSAAEQQVQSVlaqqkedtimQTKLKEEYEKAKKLaKQAEAAKEKAEREAALLRQQAEEAERQkaAAEQEAANQAK 2130
Cdd:COG4717 130 LYQELEALEAELAEL----------PERLEELEERLEEL-RELEEELEELEAELAELQEELEELLEQ--LSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2131 AQEDAERLRKEAEF--EAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKF-------------------------- 2182
Cdd:COG4717 197 LAEELEELQQRLAEleEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallallglggsllsliltia 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2183 ------------------QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRgqvEEELLKVKVQMEELLKLK 2244
Cdd:COG4717 277 gvlflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS---PEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2245 LRIEEENQRLIKKDKDNTQKFLAKEADnmkklAEDAARLSVEAQEAARLRQIAE--DDLNQQRALADKMLKEKMQAIQEA 2322
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALLAEAG-----VEDEEELRAALEQAEEYQELKEelEELEEQLEELLGELEELLEALDEE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2323 sRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLD--EETEEYQKsLEAERKRQLEIIAESEK----LKLQVSQLSEAQ 2396
Cdd:COG4717 429 -ELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAE-LLQELEELKAELRELAEewaaLKLALELLEEAR 506
|
490 500
....*....|....*....|..
gi 1927222988 2397 AKAQEE-AKKFKKQADSIASRL 2417
Cdd:COG4717 507 EEYREErLPPVLERASEYFSRL 528
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1258-1573 |
2.94e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1258 AQEKKLLEEV----EGNKDKVDECQKYAKAyidTIKDYELQLVAYKAQVEPLASPLKKTKLDSASDNIIQEYVTLRTKYS 1333
Cdd:PTZ00121 1479 AEEAKKADEAkkkaEEAKKKADEAKKAAEA---KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1334 ELmtltsqyikfitdsqRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQ---KQLAEVHAKAIAKAEKEAQELK------- 1403
Cdd:PTZ00121 1556 EL---------------KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeeARIEEVMKLYEEEKKMKAEEAKkaeeaki 1620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1404 ----LRMQEEVNRREDAVV--DAEKQKHNIQLELHELKN-LSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQ 1476
Cdd:PTZ00121 1621 kaeeLKKAEEEKKKVEQLKkkEAEEKKKAEELKKAEEENkIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1477 KSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEE 1556
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
330
....*....|....*..
gi 1927222988 1557 AERQVKQAEIEKERQIQ 1573
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVD 1797
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1552-1985 |
4.22e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1552 RQAEEAERQVKQA-EIEKERQIQVAHVAAQKSAAAELQSKhmsfVEKTSKLEESLKQEHGAV---LQLQHEAAALKKQqe 1627
Cdd:PRK04863 276 RHANERRVHLEEAlELRRELYTSRRQLAAEQYRLVEMARE----LAELNEAESDLEQDYQAAsdhLNLVQTALRQQEK-- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1628 daerareeaekeLEKWRQ---KANEALRLRLQAEEEAHKKslaQEDAEKQKEEAEREAKkRAKAEDSALKQkemAENELE 1704
Cdd:PRK04863 350 ------------IERYQAdleELEERLEEQNEVVEEADEQ---QEENEARAEAAEEEVD-ELKSQLADYQQ---ALDVQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1705 RqRKVAESTAQQKLTAEQELIRLRA-DFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKA 1783
Cdd:PRK04863 411 T-RAIQYQQAVQALERAKQLCGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEV 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1784 EKETMSNSERSkqlLEVEATKMRDLAEEASKLRAIAEEAKhQRQVAEEEAARQRAEAERILKEKLAAISDATRLkteaei 1863
Cdd:PRK04863 490 SRSEAWDVARE---LLRRLREQRHLAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL------ 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1864 aLKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEkivLLKKSSE-----AEMERQRAIVDDTLKQRRVVEEEIRI 1938
Cdd:PRK04863 560 -QEELEARLESLSESVSEARERRMALRQQLEQLQARIQR---LAARAPAwlaaqDALARLREQSGEEFEDSQDVTEYMQQ 635
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1927222988 1939 LKLNFEKASSGKLDLELELNKLKNIAEETQQsklRAEEEAEKLRKLA 1985
Cdd:PRK04863 636 LLERERELTVERDELAARKQALDEEIERLSQ---PGGSEDPRLNALA 679
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1691-1903 |
4.24e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1691 SALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAK-- 1768
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1769 --------VRSEMDVLiqLKSKAEKETMSNSERSKQLLEveatKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEA 1840
Cdd:COG3883 93 ralyrsggSVSYLDVL--LGSESFSDFLDRLSALSKIAD----ADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222988 1841 ERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEK 1903
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1545-1778 |
4.44e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.70 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1545 EDLENLKRQAEEAERQvKQAEIEKERQIQVAHVAAQKSAAAELQSKHmsfVEKTSKLEESLKQEHGAVLQLQHEAAALKK 1624
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQ-RAAEQARQKELEQRAAAEKAAKQAEQAAKQ---AEEKQKQAEEAKAKQAAEAKAKAEAEAERK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1625 QQEdaerareeaekelekwrqkanealRLRLQAEEEAHKKslAQEDAEKQKEEAEREAKKRAKAEDSALKQK--EMAENE 1702
Cdd:TIGR02794 144 AKE------------------------EAAKQAEEEAKAK--AAAEAKKKAEEAKKKAEAEAKAKAEAEAKAkaEEAKAK 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 1703 LERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQ 1778
Cdd:TIGR02794 198 AEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQ 273
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2381-2609 |
5.38e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2381 ESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETElatqekmtvveklevarltssKEADDLRKAIADLEKEKS 2460
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ---------------------AELEALQAEIDKLQAEIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2461 RLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQ-------QTFLSEKEMLLkkeklieeekkRLESQFEEEVKKAKALKDE 2533
Cdd:COG3883 76 EAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfSDFLDRLSALS-----------KIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 2534 QERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQP 2609
Cdd:COG3883 145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1404-2312 |
5.44e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1404 LRMQEEVNRREDAVVDAEKQKHNIQLELHElknlSEQQIMDKSKQVDDALQSRVKIEEEIRLI--RLQLETTV----KQK 1477
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAA----EQYRLVEMARELAELNEAESDLEQDYQAAsdHLNLVQTAlrqqEKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1478 STAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQvneetqkKRMAEEELKRKAEAekeaakqkqkaLED----LENLKRQ 1553
Cdd:PRK04863 351 ERYQADLEELEERLEEQNEVVEEADEQQEENEAR-------AEAAEEEVDELKSQ-----------LADyqqaLDVQQTR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1554 AEeAERQVKQAEIEKERQIQVAHVAAQKSAA--AELQSKhmsfvektsklEESLKQEhgaVLQLQHE---AAALKKQQEd 1628
Cdd:PRK04863 413 AI-QYQQAVQALERAKQLCGLPDLTADNAEDwlEEFQAK-----------EQEATEE---LLSLEQKlsvAQAAHSQFE- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1629 aerareeaekelekwrqKANEALRlRLQAE---EEAHKKslAQE---DAEKQKEEAEREAKKRAKAedSALKQKEMAENE 1702
Cdd:PRK04863 477 -----------------QAYQLVR-KIAGEvsrSEAWDV--AREllrRLREQRHLAEQLQQLRMRL--SELEQRLRQQQR 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1703 LERQRKVAESTAQQKLTAEQELIRLRADfdnAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSK 1782
Cdd:PRK04863 535 AERLLAEFCKRLGKNLDDEDELEQLQEE---LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1783 AEK------ETMSNSERSKQLLEVEATKMRDLAEE----ASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAIS 1852
Cdd:PRK04863 612 LARlreqsgEEFEDSQDVTEYMQQLLERERELTVErdelAARKQALDEEIERLSQPGGSEDPRLNALAERFGGVLLSEIY 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1853 DATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDqanqhkqqIEEKIVLLK--------KSSEAEmERQRAIVDd 1924
Cdd:PRK04863 692 DDVSLEDAPYFSALYGPARHAIVVPDLSDAAEQLAGLED--------CPEDLYLIEgdpdsfddSVFSVE-ELEKAVVV- 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1925 tlkqrRVVEEEIRILKLNfekassgkldlelELNKLKNIAEETQQSKLRAE--EEAEKLRKLAleeekrrreaeEKVKKI 2002
Cdd:PRK04863 762 -----KIADRQWRYSRFP-------------EVPLFGRAAREKRIEQLRAEreELAERYATLS-----------FDVQKL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2003 AAAEEEAARQRQAA-----QDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQK--EDTIM 2075
Cdd:PRK04863 813 QRLHQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNllADETL 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2076 QTKLKE------EYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAE--RQKAAAEQEAANQAKAQEDA--ERLRKEAEF- 2144
Cdd:PRK04863 893 ADRVEEireqldEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEqlKQDYQQAQQTQRDAKQQAFAltEVVQRRAHFs 972
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2145 -EAAKRAQAENAALKQKQQADAEMAKHKKL-AEQTLKQKFQVEQELTKVKLKLDETdkqKSVLDEELQRLKDEVDD---- 2218
Cdd:PRK04863 973 yEDAAEMLAKNSDLNEKLRQRLEQAEQERTrAREQLRQAQAQLAQYNQVLASLKSS---YDAKRQMLQELKQELQDlgvp 1049
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2219 --------AVKQRGQVEEELLKVKVQMEELLKLKLRIEEE----NQRLIKKDKDNTQkfLAKEADNMKKLAEDAARLSVE 2286
Cdd:PRK04863 1050 adsgaeerARARRDELHARLSANRSRRNQLEKQLTFCEAEmdnlTKKLRKLERDYHE--MREQVVNAKAGWCAVLRLVKD 1127
|
970 980
....*....|....*....|....*...
gi 1927222988 2287 AQEAARL--RQIAEDDLNQQRALADKML 2312
Cdd:PRK04863 1128 NGVERRLhrRELAYLSADELRSMSDKAL 1155
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1747-2493 |
6.10e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.26 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1747 RLKNEVVAAQQQRKQLEDELAKVRSEM--------DVLIQLKSKAEKETMSNSE------RSKQL---LEVEATKMRDLA 1809
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELknkekelkNLDKNLNKDEEKINNSNNKikileqQIKDLndkLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1810 EEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEaeiaLKEKEAENERLRRQAEDeayqrkaL 1889
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKKQKEE-------L 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1890 EDQANQHKQQIEEKivllkksseaemerqRAIVDDTLKQRRVVEEEIRILKLNFEK---ASSGKLDLELELNKLKNIAEE 1966
Cdd:TIGR04523 172 ENELNLLEKEKLNI---------------QKNIDKIKNKLLKLELLLSNLKKKIQKnksLESQISELKKQNNQLKDNIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1967 TQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKD-DADKEAEKQI 2045
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqDWNKELKSEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2046 lmAQQAAQKcsaaeQQVQSVLAQQKEDTimqTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEA 2125
Cdd:TIGR04523 317 --KNQEKKL-----EEIQNQISQNNKII---SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2126 ANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEmakHKKLAEQTLKQKFQV---EQELTKVKLKLDETDKQK 2202
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE---IERLKETIIKNNSEIkdlTNQDSVKELIIKNLDNTR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2203 SVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKlaedaar 2282
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK------- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2283 lsvEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEasrLRAEAEMLQRqkdlAQEQAQKLLEDKQLMQQRLDEETE 2362
Cdd:TIGR04523 537 ---ESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEE---LKQTQKSLKK----KQEEKQELIDQKEKEKKDLIKEIE 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2363 EYQKSLEaERKRQLEII-AESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVeklevarlts 2441
Cdd:TIGR04523 607 EKEKKIS-SLEKELEKAkKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI---------- 675
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1927222988 2442 skeaDDLRKAIADLEKEKSRLKKEA--EDLQNKSKEMADAQQKQIEHEKTVLQQ 2493
Cdd:TIGR04523 676 ----DDIIELMKDWLKELSLHYKKYitRMIRIKDLPKLEEKYKEIEKELKKLDE 725
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1497-1975 |
7.20e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1497 LRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERqiqvah 1576
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK------ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1577 vaaqksaaAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAErareEAEKELEKWRQKANEALRLRLQ 1656
Cdd:COG4717 121 --------LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE----ELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1657 AEEEAHKKSLAQ-EDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELER---QRKVAESTAQQKLTAEQELIRLRADFD 1732
Cdd:COG4717 189 ATEEELQDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLENELEAaalEERLKEARLLLLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1733 NAEQQRS----------LLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEA 1802
Cdd:COG4717 269 LSLILTIagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1803 TK--MRDLAEEASKLRAIAEEAK-----HQRQVAEEEAARQRAEAERI---LKEKLAAISDATRLKTEAEIALKEKEAEn 1872
Cdd:COG4717 349 LQelLREAEELEEELQLEELEQEiaallAEAGVEDEEELRAALEQAEEyqeLKEELEELEEQLEELLGELEELLEALDE- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1873 ERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKksseaEMERQRAIvDDTLKQRRVVEEEIRILklnFEKASSGKLD 1952
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELE-----QLEEDGEL-AELLQELEELKAELREL---AEEWAALKLA 498
|
490 500
....*....|....*....|...
gi 1927222988 1953 LELeLNKLKNIAEETQQSKLRAE 1975
Cdd:COG4717 499 LEL-LEEAREEYREERLPPVLER 520
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2087-2608 |
9.00e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 58.60 E-value: 9.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2087 KKLAKQAEAAKEKAEREA-ALLRQQAEEAERQKAAaeqeaanqakaQEDAERLRK-EAEFEAAKRAQAENAalKQKQQAD 2164
Cdd:pfam05557 19 KQMELEHKRARIELEKKAsALKRQLDRESDRNQEL-----------QKRIRLLEKrEAEAEEALREQAELN--RLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2165 AEMAKHKKLAEQTLKQKFQV----EQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEEL 2240
Cdd:pfam05557 86 EALNKKLNEKESQLADAREVisclKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2241 LKLKLRIEEENQRLIKKDKDntqkflAKEADNMKKLAEDAARLSVEAQ----EAARLRQIAEDDLNQQRALADkmLKEKM 2316
Cdd:pfam05557 166 AEAEQRIKELEFEIQSQEQD------SEIVKNSKSELARIPELEKELErlreHNKHLNENIENKLLLKEEVED--LKRKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2317 QAIQEAsrlRAEAEMLQRQKDLAQeqaQKLLEDKQLMQQRLDE--ETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSE 2394
Cdd:pfam05557 238 EREEKY---REEAATLELEKEKLE---QELQSWVKLAQDTGLNlrSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2395 AQAKAQEEAKKFKKQADSIASRLHETElatqekmTVVEKLEVARLTSSKEADDLRKAIADLEKE---------KSRLKKE 2465
Cdd:pfam05557 312 ARRELEQELAQYLKKIEDLNKKLKRHK-------ALVRRLQRRVLLLTKERDGYRAILESYDKEltmsnyspqLLERIEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2466 AEDLQNKSKemadAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLE----SQFEEEVKKAKALKDEQERQKQQM 2541
Cdd:pfam05557 385 AEDMTQKMQ----AHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESladpSYSKEEVDSLRRKLETLELERQRL 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222988 2542 EDEKKKLQATMdAALNKQKEAE----KEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQ 2608
Cdd:pfam05557 461 REQKNELEMEL-ERRCLQGDYDpkktKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQV 530
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1836-2192 |
9.42e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.60 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1836 QRAEAERILKEKLAAIsDATRLKTEAEialkEKEAENERLRRQAEDEAYQRKALEDQANQHKQQieekivllkksSEAEM 1915
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAEQ-----------ERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1916 ERQRAIVDDTLKQRRVVEEEIRILKLNFEKAssgkldlelELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREA 1995
Cdd:pfam17380 345 ERERELERIRQEERKRELERIRQEEIAMEIS---------RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1996 EEKVKKIAAAEEEAARQRQaaqDELDRLKKkaEEARKQKDDADKEAEKQilmaqqaaqkcsaaeQQVQsVLAQQKEDtim 2075
Cdd:pfam17380 416 QQQKVEMEQIRAEQEEARQ---REVRRLEE--ERAREMERVRLEEQERQ---------------QQVE-RLRQQEEE--- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2076 QTKLKEEYEKAKKLAKQAEAAKEKA-EREAALLRQQAEEAERQKAAAEQEAANQAKA-------QEDAERLRKEAEFEAA 2147
Cdd:pfam17380 472 RKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEERQKAiyeeerrREAEEERRKQQEMEER 551
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2148 KRAQAENAALKQKQQADAEMAKHKKLAEQTL-----KQKFQVEQELTKVK 2192
Cdd:pfam17380 552 RRIQEQMRKATEERSRLEAMEREREMMRQIVesekaRAEYEATTPITTIK 601
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1825-2604 |
9.79e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1825 QRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEiALKEKEAENERLRRQAEDeayqRKALEDQANQHKQQIEEKI 1904
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELA-ELNEAESDLEQDYQAASD----HLNLVQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1905 VLLKKSSEAeMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKlRAEEEAEKLRKL 1984
Cdd:PRK04863 355 ADLEELEER-LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAV-QALERAKQLCGL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1985 AleeekrrreaeekvkkiaaaeeeaarqrqaaQDELDRLKKKAEEARKQKDDADKE---AEKQILMAQQAAQKCSAAEQQ 2061
Cdd:PRK04863 433 P-------------------------------DLTADNAEDWLEEFQAKEQEATEEllsLEQKLSVAQAAHSQFEQAYQL 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2062 VQSVLAQqkedtimqTKLKEEYEKAKKLAKQAEAAKEKAEREAALlRQQAEEAERQkaaaeqeaanqAKAQEDAERLRKE 2141
Cdd:PRK04863 482 VRKIAGE--------VSRSEAWDVARELLRRLREQRHLAEQLQQL-RMRLSELEQR-----------LRQQQRAERLLAE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2142 AEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSV---LDEELQRLKDEVDD 2218
Cdd:PRK04863 542 FCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2219 AVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLiKKDKDNTQKFLAKEADNMKKLAED--AARLS-----VEAQEAA 2291
Cdd:PRK04863 622 EFEDSQDVTEYMQQLLERERELTVERDELAARKQAL-DEEIERLSQPGGSEDPRLNALAERfgGVLLSeiyddVSLEDAP 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2292 -------RLRQ-IAEDDLNQ-QRALA------------------------DKMLKEKMQAIQEA------SRLRAE---- 2328
Cdd:PRK04863 701 yfsalygPARHaIVVPDLSDaAEQLAgledcpedlyliegdpdsfddsvfSVEELEKAVVVKIAdrqwrySRFPEVplfg 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2329 -------AEMLQRQKDLAQEQAQKLLEDKQLMQqRLDEETEEY-------------QKSLEAERKRQLEIIAESEKLKLQ 2388
Cdd:PRK04863 781 raarekrIEQLRAEREELAERYATLSFDVQKLQ-RLHQAFSRFigshlavafeadpEAELRQLNRRRVELERALADHESQ 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2389 VSQLSEAQAKAQEEAKKFKKQADSIAsrLHETELATQEKMTVVEKLEVArltsSKEADDLR---KAIADLEKEKSRLKKE 2465
Cdd:PRK04863 860 EQQQRSQLEQAKEGLSALNRLLPRLN--LLADETLADRVEEIREQLDEA----EEAKRFVQqhgNALAQLEPIVSVLQSD 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2466 AEDLQNKSKEMADAQQKQieheKTVLQQTF-LSE-------------KEMLLKKEKLIEEEKKRLEsQFEEEVKKAKalk 2531
Cdd:PRK04863 934 PEQFEQLKQDYQQAQQTQ----RDAKQQAFaLTEvvqrrahfsyedaAEMLAKNSDLNEKLRQRLE-QAEQERTRAR--- 1005
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2532 dEQERQKQQMEDEKKKLQATMDAALN-KQ---KEAEKEMHN---------------KQKEMKE-----------LERKRL 2581
Cdd:PRK04863 1006 -EQLRQAQAQLAQYNQVLASLKSSYDaKRqmlQELKQELQDlgvpadsgaeeraraRRDELHArlsanrsrrnqLEKQLT 1084
|
890 900
....*....|....*....|....*.
gi 1927222988 2582 EQERILAEENQKLR---EKLQQLEEA 2604
Cdd:PRK04863 1085 FCEAEMDNLTKKLRkleRDYHEMREQ 1110
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
161-263 |
1.01e-07 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 53.15 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 161 TAKEKLLLWSQRMTdgyQGIRCDNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTN-LENLEQAFGVAERDLGVTRLLD 239
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQpVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1927222988 240 PEDVDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1373-1528 |
1.52e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.70 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1373 MMQAELDKQKQLAEVHAKaIAKAEKEAQELKLR---MQEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQqiMDKSKQV 1449
Cdd:COG1579 1 AMPEDLRALLDLQELDSE-LDRLEHRLKELPAElaeLEDELAALEARLEAAKTELEDLEKEIKRLELEIEE--VEARIKK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222988 1450 DDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKR 1528
Cdd:COG1579 78 YEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2141-2455 |
1.72e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 58.00 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2141 EAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTL---KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVD 2217
Cdd:PRK11281 32 NGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2218 DAVKQR------GQVEEELLKVKVQMEELLKlklRIEEENQRLI--KKDKDNTQKFLakeADNMKKLAEDAARLSVEAQE 2289
Cdd:PRK11281 112 EETRETlstlslRQLESRLAQTLDQLQNAQN---DLAEYNSQLVslQTQPERAQAAL---YANSQRLQQIRNLLKGGKVG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2290 AARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRaeaEMLQRQKDLAQEQAQKLLEDKQLMQ-----QRLD--EET- 2361
Cdd:PRK11281 186 GKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQ---DLLQKQRDYLTARIQRLEHQLQLLQeainsKRLTlsEKTv 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2362 EEYQKSLEAERKRQLEIIAESEKLKLQVSQ-LSEAQAKAQE---EAKKFKKQADsiasRLHETELATQEKMTVVE-KLEV 2436
Cdd:PRK11281 263 QEAQSQDEAARIQANPLVAQELEINLQLSQrLLKATEKLNTltqQNLRVKNWLD----RLTQSERNIKEQISVLKgSLLL 338
|
330 340
....*....|....*....|....*..
gi 1927222988 2437 AR--------LTSSKEADDLRKAIADL 2455
Cdd:PRK11281 339 SRilyqqqqaLPSADLIEGLADRIADL 365
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1498-2117 |
1.82e-07 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 57.35 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1498 RKAAQEEAEKLRKQVNEETQKKRMAEEElkrkaeaekeaakqKQKALEDLENLKRQAEEAERQVKQAEIEkERQiqvahv 1577
Cdd:pfam05701 37 RKLVELELEKVQEEIPEYKKQSEAAEAA--------------KAQVLEELESTKRLIEELKLNLERAQTE-EAQ------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1578 AAQKSAAAELQSKHMsfvektsklEESLKQEHGAVLQLQHEAAalKKQQEDAERAREEAEKELEKWRQKANEALRLRLQA 1657
Cdd:pfam05701 96 AKQDSELAKLRVEEM---------EQGIADEASVAAKAQLEVA--KARHAAAVAELKSVKEELESLRKEYASLVSERDIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1658 EEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAEnelERQRKVAESTAQQKLTAEQELirlradfdnaEQq 1737
Cdd:pfam05701 165 IKRAEEAVSASKEIEKTVEELTIELIATKESLESAHAAHLEAE---EHRIGAALAREQDKLNWEKEL----------KQ- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1738 rslLEDELYRLKNEVVAAQQQRKQLE---DELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEask 1814
Cdd:pfam05701 231 ---AEEELQRLNQQLLSAKDLKSKLEtasALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAALASAKKELEE--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1815 LRAIAEEAKHQRQVAEEEAARQRAEAERiLKEKLAAISdatRLKTEAEIALKEKEAENERLRrqAEDEAYQRKALEDQan 1894
Cdd:pfam05701 305 VKANIEKAKDEVNCLRVAAASLRSELEK-EKAELASLR---QREGMASIAVSSLEAELNRTK--SEIALVQAKEKEAR-- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1895 qhkqqiEEKIVLLKKSSEAEMErqraiVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELnklkniaeetqQSKLRA 1974
Cdd:pfam05701 377 ------EKMVELPKQLQQAAQE-----AEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRL-----------EAVLKE 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1975 EEEAEKLRKLALEEEKRRREAEEKVKKiaAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQK 2054
Cdd:pfam05701 435 IEAAKASEKLALAAIKALQESESSAES--TNQEDSPRGVTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELR 512
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222988 2055 CSAAEQQVQSVLAQQKEDtimqtkLKEEYEKAKKlakqAEAAKEKAEREaalLRQQAEEAERQ 2117
Cdd:pfam05701 513 SLEKLEEVNREMEERKEA------LKIALEKAEK----AKEGKLAAEQE---LRKWRAEHEQR 562
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4032-4068 |
1.87e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 49.79 E-value: 1.87e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1927222988 4032 IRLLEAQIATGGIIDPEESHRVPVEVAYKRGFFDEEM 4068
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1252-1736 |
2.26e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1252 TLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLASplKKTKLDSASDNIIQEYVTLRTK 1331
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRE--TIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1332 YSELmtltSQYIKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVN 1411
Cdd:PRK02224 288 LEEL----EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1412 RREDAVVDAEKQKHNIQLELHELKNLsEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRA 1491
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEEL-EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1492 AEAEKLRKAAQ--------EEAEKLrkqvnEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQ 1563
Cdd:PRK02224 443 EEAEALLEAGKcpecgqpvEGSPHV-----ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1564 AE-IEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQ-------------EDA 1629
Cdd:PRK02224 518 REdLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaelkeriesleriRTL 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1630 ERAREEAEKELEKWRQK------ANEALRLRLQAEEEaHKKSLAQ-------EDAEKQKEEAER-----EAKKRAKAE-- 1689
Cdd:PRK02224 598 LAAIADAEDEIERLREKrealaeLNDERRERLAEKRE-RKRELEAefdeariEEAREDKERAEEyleqvEEKLDELREer 676
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1927222988 1690 DSALKQKEMAENELERQRKVAEstaqqKLTA-EQELIRLRADFDNAEQ 1736
Cdd:PRK02224 677 DDLQAEIGAVENELEELEELRE-----RREAlENRVEALEALYDEAEE 719
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
156-263 |
2.44e-07 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 52.02 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 156 QSEDMTAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLV-DMGRVYRQTNLENLEQAFGVAERDLGV 234
Cdd:cd21313 3 DAKKQTPKQRLLGWIQ---NKIPYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1927222988 235 TRLLDPEDVDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1400-1969 |
2.47e-07 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 56.96 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1400 QELKlRMQEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQQIMDKSKQVDDALQSRVKIE-EEIRLIRLQLETTVKQKS 1478
Cdd:pfam05701 42 LELE-KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSElAKLRVEEMEQGIADEASV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1479 TAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAekeaakqkqkaledlenlkrqAEEAE 1558
Cdd:pfam05701 121 AAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSA---------------------SKEIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1559 RQVKQAEIE----KE--RQIQVAHVAA--QKSAAAelqskhMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAe 1630
Cdd:pfam05701 180 KTVEELTIEliatKEslESAHAAHLEAeeHRIGAA------LAREQDKLNWEKELKQAEEELQRLNQQLLSAKDLKSKL- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1631 rareeaekelekwrqKANEALRLRLQAEEEAHKKSlaqedaeKQKEEAEREAKKRaKAEDSALKQKEMAENELERQRKVA 1710
Cdd:pfam05701 253 ---------------ETASALLLDLKAELAAYMES-------KLKEEADGEGNEK-KTSTSIQAALASAKKELEEVKANI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1711 EstaqqKLTAEQELIRLRAdfdnaeqqrSLLEDELYRLKNEVVAAQQQR-------KQLEDELAKVRSEMdVLIQLKSKA 1783
Cdd:pfam05701 310 E-----KAKDEVNCLRVAA---------ASLRSELEKEKAELASLRQREgmasiavSSLEAELNRTKSEI-ALVQAKEKE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1784 EKETMsnSERSKQLLEV--EATKMRDLA----EEASKLRAIAEEAKHQRQVAEE--EAARQRAEAERIlKEKLAAISDAT 1855
Cdd:pfam05701 375 AREKM--VELPKQLQQAaqEAEEAKSLAqaarEELRKAKEEAEQAKAAASTVESrlEAVLKEIEAAKA-SEKLALAAIKA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1856 RLKTEAEIALKEKEA----------ENERLRRQAEDEayqrkalEDQANqhkQQIEEKIVLLKKSSEAEMeRQRAIVDDT 1925
Cdd:pfam05701 452 LQESESSAESTNQEDsprgvtlsleEYYELSKRAHEA-------EELAN---KRVAEAVSQIEEAKESEL-RSLEKLEEV 520
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1927222988 1926 LKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKniAEETQQ 1969
Cdd:pfam05701 521 NREMEERKEALKIALEKAEKAKEGKLAAEQELRKWR--AEHEQR 562
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1491-1704 |
2.60e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1491 AAEAEKLRK--AAQEEAEKLRKQVNEETQKKRMAEEELKRKAEaekeaakqkqkaledlenlKRQAEEAER----QVKQA 1564
Cdd:PRK09510 74 AKRAEEQRKkkEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ-------------------KKQAEEAAKqaalKQKQA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1565 EIEKERQIQVAHVAA--QKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEdaerareeaekelek 1642
Cdd:PRK09510 135 EEAAAKAAAAAKAKAeaEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA--------------- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 1643 wRQKANEALRLRlqAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELE 1704
Cdd:PRK09510 200 -KKKAEAEAKKK--AAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1153-1938 |
2.60e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1153 PVFDSLEAELKKATAVSDKMSRVHSERdaELDHYRQLLSSLQDRWKavfsqidlRQRELEQlgRQLGYYRESYDWLIRWI 1232
Cdd:pfam15921 52 PIFPKYEVELDSPRKIIAYPGKEHIER--VLEEYSHQVKDLQRRLN--------ESNELHE--KQKFYLRQSVIDLQTKL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1233 NDAKQRQEKIQAVTITDSKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDyelQLVAYKAQVEPLASPLkkT 1312
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRK---MMLSHEGVLQEIRSIL--V 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1313 KLDSASDNIIQEYVTLRT-KYSELMTLTSQYIKF----ITDSQRRLEDEEKAAEKLKAEEQKKMAMM-QAELDKQKQLAE 1386
Cdd:pfam15921 195 DFEEASGKKIYEHDSMSTmHFRSLGSAISKILREldteISYLKGRIFPVEDQLEALKSESQNKIELLlQQHQDRIEQLIS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1387 VHakaiakaekeaqelklrmqeEVnrredavvdaekqkhniqlelhELKNLSEQQIMDKSKQvdDALQSRVKIEEEirLI 1466
Cdd:pfam15921 275 EH--------------------EV----------------------EITGLTEKASSARSQA--NSIQSQLEIIQE--QA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1467 RLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKL--------------RKQVNEET-----QKKRMAEEELK 1527
Cdd:pfam15921 309 RNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlanseltearteRDQFSQESgnlddQLQKLLADLHK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1528 RKAEAEKEAAKQKQKALEDLEN------LKRQAEEAERQVKQAEI-----------EKERQI-----------QVAHVAA 1579
Cdd:pfam15921 389 REKELSLEKEQNKRLWDRDTGNsitidhLRRELDDRNMEVQRLEAllkamksecqgQMERQMaaiqgknesleKVSSLTA 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1580 QKSAAAELQSKHM-SFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLR-LQA 1657
Cdd:pfam15921 469 QLESTKEMLRKVVeELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnVQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1658 EEEAHKKSLAQEDA-----EKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFD 1732
Cdd:pfam15921 549 ECEALKLQMAEKDKvieilRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVS 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1733 NAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQ--------LKSKAEKETMSNSERSKQL----LEV 1800
Cdd:pfam15921 629 DLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEdyevlkrnFRNKSEEMETTTNKLKMQLksaqSEL 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1801 EATKMRDLAEEASKLRAIAEEAKHQRQVAeeeAARQRAEAeriLKEKLAAISDA-TRLKTEAEIALKEKEAENERLRRQA 1879
Cdd:pfam15921 709 EQTRNTLKSMEGSDGHAMKVAMGMQKQIT---AKRGQIDA---LQSKIQFLEEAmTNANKEKHFLKEEKNKLSQELSTVA 782
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 1880 EDE---AYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIvddtlkqRRVVEEEIRI 1938
Cdd:pfam15921 783 TEKnkmAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDII-------QRQEQESVRL 837
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2204-2454 |
2.75e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2204 VLDEelQRLKDEVDDAVKQRGQ---VEEELLKVKVQMEELLklklRIEEENQRLIKKDKDNTQKflakeadnmkklaeDA 2280
Cdd:COG4913 217 MLEE--PDTFEAADALVEHFDDlerAHEALEDAREQIELLE----PIRELAERYAAARERLAEL--------------EY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2281 ARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQ----EQAQKLLEDKQLMQQR 2356
Cdd:COG4913 277 LRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2357 LDEETEEYQKSLeaeRKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEV 2436
Cdd:COG4913 357 RERRRARLEALL---AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
250
....*....|....*...
gi 1927222988 2437 ARLTSSKEADDLRKAIAD 2454
Cdd:COG4913 434 RKSNIPARLLALRDALAE 451
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2243-2564 |
2.77e-07 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 57.54 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2243 LKLRIEEENQRLIKKDKDNTQKfLAKEADNMKKLAEdaarlsvEAQEAARLRQIAEDDLNQQRALADKmlkekmqAIQEA 2322
Cdd:NF012221 1505 LKLTAKAGSNRLEFKGTGHNDG-LGYILDNVVATSE-------SSQQADAVSKHAKQDDAAQNALADK-------ERAEA 1569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2323 SRLRAEAEMLQRQKDLAQEQAQklLEDKQlmQQRLDEETEEYQKSLEAERKrqlEIIAESEKLKLQVSQLSEAQAKAQEE 2402
Cdd:NF012221 1570 DRQRLEQEKQQQLAAISGSQSQ--LESTD--QNALETNGQAQRDAILEESR---AVTKELTTLAQGLDALDSQATYAGES 1642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2403 AKKFKKQ-ADSIASRLHETELATqeKMTVVEKLEVARLTSSKEADDLRKAIAdleKEKSRLKKEAEDLQNKSKEMADAQQ 2481
Cdd:NF012221 1643 GDQWRNPfAGGLLDRVQEQLDDA--KKISGKQLADAKQRHVDNQQKVKDAVA---KSEAGVAQGEQNQANAEQDIDDAKA 1717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2482 KQIEHEKTVLQQtflsekemllkkeklieeekkRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKE 2561
Cdd:NF012221 1718 DAEKRKDDALAK---------------------QNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDE 1776
|
...
gi 1927222988 2562 AEK 2564
Cdd:NF012221 1777 SDK 1779
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2031-2468 |
3.14e-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: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2031 RKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQK--EDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLR 2108
Cdd:pfam09731 77 GESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKaqLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2109 QQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRaQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQEL 2188
Cdd:pfam09731 157 QAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKE-VINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2189 TKVKLKLDETDKQKS-------VLDEELQRLKDEVDDAVKQRGQVEEELLKVKVqmeelLKLKLRIEEENQRLIKKDKDn 2261
Cdd:pfam09731 236 EKAQSLAKLVDQYKElvaseriVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLI-----AHAHREIDQLSKKLAELKKR- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2262 tqkflakeadnmkklAEDAARLSVEAQEAarlrqiaeddlnQQRALADKMLKekmqaiqeasrlRAEAEMLQRQKDLAQE 2341
Cdd:pfam09731 310 ---------------EEKHIERALEKQKE------------ELDKLAEELSA------------RLEEVRAADEAQLRLE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2342 QAQKLLEdkqlmqqrldeETEEYQKSLEAERKRQLEIIAE-------SEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIA 2414
Cdd:pfam09731 351 FEREREE-----------IRESYEEKLRTELERQAEAHEEhlkdvlvEQEIELQREFLQDIKEKVEEERAGRLLKLNELL 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 2415 SRLHETELATQEKMTVV-EKLEVARLTSSKEA--DDLRKAIAD-----LEKEKSRLKKEAED 2468
Cdd:pfam09731 420 ANLKGLEKATSSHSEVEdENRKAQQLWLAVEAlrSTLEDGSADsrprpLVRELKALKELASD 481
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
41-148 |
3.17e-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: 52.31 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 41 ERDRVQKKTFTKWVNKHLIKSQrqVTDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 111
Cdd:cd21331 18 EGETREERTFRNWMNSLGVNPH--VNHLYGDLQDALVILQLYEKIkvpvdwnkvNKPPYPKLGANMK--KLENCNYAVEL 93
|
90 100 110
....*....|....*....|....*....|....*...
gi 1927222988 112 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21331 94 GKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2020-2602 |
3.34e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.98 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2020 LDRLKKKAEEARKQKddadKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEK 2099
Cdd:TIGR00606 188 LETLRQVRQTQGQKV----QEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2100 -AEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAK-RAQAENAALKQKqqadaEMAKHKKLAEQT 2177
Cdd:TIGR00606 264 iMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTvREKERELVDCQR-----ELEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2178 LKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEellkvkVQMEELLKLKLRIEEENQRLIKK 2257
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSE------RQIKNFHTLVIERQEDEAKTAAQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2258 DkdntqkfLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASR-LRAEAEMLQRQK 2336
Cdd:TIGR00606 413 L-------CADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRiLELDQELRKAER 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2337 DLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKlQVSQLSEAQAKAQEEAKKFKKQ-ADSIAS 2415
Cdd:TIGR00606 486 ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT-QMEMLTKDKMDKDEQIRKIKSRhSDELTS 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2416 RLHETELATQEKMTVVEKLEVARLTSSKEADdLRKAIADLEKEKSRLKKEAE------------------------DLQN 2471
Cdd:TIGR00606 565 LLGYFPNKKQLEDWLHSKSKEINQTRDRLAK-LNKELASLEQNKNHINNELEskeeqlssyedklfdvcgsqdeesDLER 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2472 KSKEMADA-QQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQA 2550
Cdd:TIGR00606 644 LKEEIEKSsKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK 723
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 2551 TMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLE 2602
Cdd:TIGR00606 724 RRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG 775
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1930-2174 |
3.94e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.49 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1930 RVVEEEIRILKLNFEKASSGKLDLELelnKLKNIAEETQQSKLRAEEEAEKLRKL------ALEEEKRRREAEEKVKKIA 2003
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARFEA---RQARLEREKAAREARHKKAAEARAAKdkdavaAALARVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2004 AAEEEAARQRQAAQDELDRLKKKAEEARKQKDDA--DKEAEKQILMAQQAAQKcsAAEQQVQSVLAQQKEDTIMQTKLKE 2081
Cdd:PRK05035 509 KAGARPDNSAVIAAREARKAQARARQAEKQAAAAadPKKAAVAAAIARAKAKK--AAQQAANAEAEEEVDPKKAAVAAAI 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2082 EYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQ 2161
Cdd:PRK05035 587 ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQAN 666
|
250
....*....|...
gi 1927222988 2162 QADAEMAKHKKLA 2174
Cdd:PRK05035 667 AEPEEAEDPKKAA 679
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1483-1722 |
4.00e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.49 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1483 ELKQLR---DRAAEAEKLRKAAQEEAEKLRKQVNE--ETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEA 1557
Cdd:PRK05035 456 EARQARlerEKAAREARHKKAAEARAAKDKDAVAAalARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQA 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1558 ERQVKQAEIEKERQIQ--VAHVAAQKSAAAElqskhmsfveKTSKLEESLKQEHGAVLQLQHEAAAlKKQQEDAERAREE 1635
Cdd:PRK05035 536 EKQAAAAADPKKAAVAaaIARAKAKKAAQQA----------ANAEAEEEVDPKKAAVAAAIARAKA-KKAAQQAASAEPE 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1636 AEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRK----VAE 1711
Cdd:PRK05035 605 EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKaavaAAI 684
|
250
....*....|.
gi 1927222988 1712 STAQQKLTAEQ 1722
Cdd:PRK05035 685 ARAKAKKAAQQ 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1384-1625 |
4.35e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1384 LAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELknlsEQQIMDKSKQVDdalqsrvKIEEEI 1463
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIR-------ALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1464 RLIRLQLETTVKQKSTAESELKQLRDRAAE-AEKLRKAAQEEAEKLRKQVNEETQKKRMAeEELKRKAEAEKEAAKQKQK 1542
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1543 ALEDLENLKRQAEEAERQVKQ--AEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAA 1620
Cdd:COG4942 158 DLAELAALRAELEAERAELEAllAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*
gi 1927222988 1621 ALKKQ 1625
Cdd:COG4942 238 AAAER 242
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3919-3955 |
4.65e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 49.02 E-value: 4.65e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1927222988 3919 RYLEGTSCIAGVFLETSKERLSIYQAMKKNMIRPGTA 3955
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2443-2615 |
5.78e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2443 KEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEE 2522
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2523 EVKKAKALKdEQERQKQQMEDEKKKLQATMDAALNK-QKEAEKEMHNKQKEMKELERKRLEQERILA---EENQKLREKL 2598
Cdd:COG4717 151 LEERLEELR-ELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEeaqEELEELEEEL 229
|
170
....*....|....*..
gi 1927222988 2599 QQLEEAQKDQPDKEVIH 2615
Cdd:COG4717 230 EQLENELEAAALEERLK 246
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3720-3754 |
5.88e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.63 E-value: 5.88e-07
10 20 30
....*....|....*....|....*....|....*
gi 1927222988 3720 LLEAQAATGFIVDPVKNETLTVDEAVRKGIVGPEI 3754
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4135-4163 |
6.37e-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: 6.37e-07
10 20
....*....|....*....|....*....
gi 1927222988 4135 IVDPETGKEMTVYEAYRKGLIDHQTYLEL 4163
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1915-2267 |
8.39e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.51 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1915 MERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEE---AEKLRKLALEEEKR 1991
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQErmaMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1992 RREAEEKVKKiaaaeeEAARQRQAAQDELDRLKKKaeeaRKQKDdadkEAEKQILmaqQAAQKCSAAEQQVQSVLAQQKE 2071
Cdd:pfam17380 358 RKRELERIRQ------EEIAMEISRMRELERLQME----RQQKN----ERVRQEL---EAARKVKILEEERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2072 DTIMQTKLKEEyekakklAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEaanqakaQEDAERLRKEAEFEAAKRAQ 2151
Cdd:pfam17380 421 EMEQIRAEQEE-------ARQREVRRLEEERAREMERVRLEEQERQQQVERLR-------QQEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2152 AENAALKQKQQADAEMAKHKKLAEQTLKQKFqVEQELtkvklkldeTDKQKSVLDEELQRLKDE---VDDAVKQRGQVEE 2228
Cdd:pfam17380 487 KRAEEQRRKILEKELEERKQAMIEEERKRKL-LEKEM---------EERQKAIYEEERRREAEEerrKQQEMEERRRIQE 556
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1927222988 2229 ELLKVKvqmEELLKLK-LRIEEENQRLIKKDKDNTQKFLA 2267
Cdd:pfam17380 557 QMRKAT---EERSRLEaMEREREMMRQIVESEKARAEYEA 593
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2131-2376 |
8.45e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2131 AQEDAERLRKEAEfEAAKRAQAENAALKQKQQAdaemakhkklAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQ 2210
Cdd:COG4942 18 QADAAAEAEAELE-QLQQEIAELEKELAALKKE----------EKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2211 RLKDEVDDAVKQRGQVEEEL---LKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEA 2287
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELaelLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2288 QEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKS 2367
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
....*....
gi 1927222988 2368 LEAERKRQL 2376
Cdd:COG4942 247 GFAALKGKL 255
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1640-1924 |
8.53e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 55.42 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1640 LEKWRQKANEALRLRLQAEEEAHKKSL--AQEDAEKQKEEAEREAKKRAKAEDSAL--KQKEMAENELERQRKVAESTAQ 1715
Cdd:pfam05667 245 RTKLLKRIAEQLRSAALAGTEATSGASrsAQDLAELLSSFSGSSTTDTGLTKGSRFthTEKLQFTNEAPAATSSPPTKVE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1716 Q----KLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVvaaqqqrKQLEDELAKVRSEMDVLIQLKSKAEK------ 1785
Cdd:pfam05667 325 TeeelQQQREEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNEELEKQYKVKKKtldllp 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1786 ETMSNSERSKQLLEVEATKMRDLAEEASKLRA--IAEEAKHQRQVAEEEAARQRAEAE-RILKEKLAAISDATRLKTEAe 1862
Cdd:pfam05667 398 DAEENIAKLQALVDASAQRLVELAGQWEKHRVplIEEYRALKEAKSNKEDESQRKLEEiKELREKIKEVAEEAKQKEEL- 476
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1863 iaLKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIE-EKIVLLKKSSEAEM-------ERQRAIVDD 1924
Cdd:pfam05667 477 --YKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEiTKILSDTKSLQKEInsltgklDRTFTVTDE 544
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1648-1924 |
8.74e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 54.69 E-value: 8.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1648 NEALRLRLQA------EEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAEN--------ELERQRKVAE-- 1711
Cdd:pfam19220 5 NELLRVRLGEmadrleDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYgklrrelaGLTRRLSAAEge 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1712 -STAQQKLTAEQELIRlRADFDNAEQQRSLLEDE--LYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETM 1788
Cdd:pfam19220 85 lEELVARLAKLEAALR-EAEAAKEELRIELRDKTaqAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1789 SNSERSkQLLEVEATKMRDLAEEAS----------------------KLRAI-----AEEAKHQRQVAEEEAARQRAEAE 1841
Cdd:pfam19220 164 TARERL-ALLEQENRRLQALSEEQAaelaeltrrlaeletqldatraRLRALegqlaAEQAERERAEAQLEEAVEAHRAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1842 RI-LKEKLAAISD----ATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKksseaEME 1916
Cdd:pfam19220 243 RAsLRMKLEALTAraaaTEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQ-----EMQ 317
|
....*...
gi 1927222988 1917 RQRAIVDD 1924
Cdd:pfam19220 318 RARAELEE 325
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
38-142 |
8.77e-07 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 50.73 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 38 RKDERDRVQKKTFTKWVNKHLIKS--QRQVTDLYEDLRDGHNLISLLEVLSGETLPREKG--RMRFHKLQNVQIALDFLK 113
Cdd:cd21285 3 SWEAENGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLA 82
|
90 100
....*....|....*....|....*....
gi 1927222988 114 HRQVKLVNIRNDDIADGNPKLTLGLIWTI 142
Cdd:cd21285 83 AKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1479-1715 |
1.09e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1479 TAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAeaekeaakqkqkalEDLENLKRQAEEAE 1558
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ--------------AEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1559 RQVKQAEIEKERQIQVAHVAAQKSAAAE--LQSKHMS-FVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREE 1635
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYLDvlLGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1636 AEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQ 1715
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2328-2608 |
1.12e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.15 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2328 EAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEyqksLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFK 2407
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEE----EEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2408 KQADSIASRLHETELA-TQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEH 2486
Cdd:pfam13868 101 EQMDEIVERIQEEDQAeAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2487 EKTVLQQTFLSEKEMLLKKEKLIEEEKKRLEsqfeEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEM 2566
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAKLY----QEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEA 256
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1927222988 2567 HNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQ 2608
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2226-2585 |
1.24e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.15 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2226 VEEELLKVKVQMEELLKLKLRIEEENQRLIKKDkdntQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQR 2305
Cdd:pfam13868 1 LRENSDELRELNSKLLAAKCNKERDAQIAEKKR----IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2306 ALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQK-SLEAERKRQLEIIAESEK 2384
Cdd:pfam13868 77 ELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEeQAEWKELEKEEEREEDER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2385 LKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEksrlkk 2464
Cdd:pfam13868 157 ILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKK------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2465 eaedlQNKSKEMADAQQKQIEHEKTVLQQtflsEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDE 2544
Cdd:pfam13868 231 -----ARQRQELQQAREEQIELKERRLAE----EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1927222988 2545 KKKLQAtmdaalnKQKEAEKEMHNKQKEMKELERKRLEQER 2585
Cdd:pfam13868 302 REEQRA-------AEREEELEEGERLREEEAERRERIEEER 335
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1354-1700 |
1.24e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.49 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1354 EDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEvhakAIAKAEKEAQelkLRMQEEVNRREDAVVDAEKQKHNIQLElHE 1433
Cdd:pfam02029 34 ESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLD----RTAKREERRQ---KRLQEALERQKEFDPTIADEKESVAER-KE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1434 LKNLSEQQIMDKSKQVDDaLQSRVKIEEeirlirlqleTTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQV- 1512
Cdd:pfam02029 106 NNEEEENSSWEKEEKRDS-RLGRYKEEE----------TEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENf 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1513 NEETQKKRMAEEELKRKAeaekeaakqkqkalEDLENLKRQAEEAERQVKQAEIE-KERQIQVAHVAAQKSAAAELQSKH 1591
Cdd:pfam02029 175 AKEEVKDEKIKKEKKVKY--------------ESKVFLDQKRGHPEVKSQNGEEEvTKLKVTTKRRQGGLSQSQEREEEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1592 MSFVEKTSKLEEsLKQEHGAvlqLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLaQEDA 1671
Cdd:pfam02029 241 EVFLEAEQKLEE-LRRRRQE---KESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAERKLRE-EEEK 315
|
330 340
....*....|....*....|....*....
gi 1927222988 1672 EKQKEEAEReakKRAKAedsALKQKEMAE 1700
Cdd:pfam02029 316 RRMKEEIER---RRAEA---AEKRQKLPE 338
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1560-1940 |
1.30e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 54.76 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1560 QVKQAEIEKERQIQVAHVAAQKSAAAELQSKHmsfveKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKE 1639
Cdd:pfam09731 98 SSEVAEEEKEATKDAAEAKAQLPKSEQEKEKA-----LEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1640 LEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQR------KVAEST 1713
Cdd:pfam09731 173 AEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSlaklvdQYKELV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1714 AQQKLTAEQELIRLRAD-FDNAEQQRSLLEDELYRLkneVVAAQQQRKQLEDELA--KVRSEMDVLIQLKSKAEKETMSN 1790
Cdd:pfam09731 253 ASERIVFQQELVSIFPDiIPVLKEDNLLSNDDLNSL---IAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1791 SERSKQLLEVEATKMRDLAEEASklRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLaaISDATRLKTEAEIALKEKEA 1870
Cdd:pfam09731 330 EELSARLEEVRAADEAQLRLEFE--REREEIRESYEEKLRTELERQAEAHEEHLKDVL--VEQEIELQREFLQDIKEKVE 405
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222988 1871 ENERLRRQAEDEAYQR-KALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILK 1940
Cdd:pfam09731 406 EERAGRLLKLNELLANlKGLEKATSSHSEVEDENRKAQQLWLAVEALRSTLEDGSADSRPRPLVRELKALK 476
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2516-2674 |
1.30e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.83 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2516 LESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQ--------KEAEKEMHNKQKEMKELERKRLEQ--ER 2585
Cdd:PRK00409 528 LERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqqaiKEAKKEADEIIKELRQLQKGGYASvkAH 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2586 ILAEENQKLREKLQQLEEAQKDQPdkevihvtmvETTKNVYNGQNV--------GDVVDSAEKKPDPLAFNGIREKVPAS 2657
Cdd:PRK00409 608 ELIEARKRLNKANEKKEKKKKKQK----------EKQEELKVGDEVkylslgqkGEVLSIPDDKEAIVQAGIMKMKVPLS 677
|
170
....*....|....*..
gi 1927222988 2658 RLHDLGLLPKKDFDKLK 2674
Cdd:PRK00409 678 DLEKIQKPKKKKKKKPK 694
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2209-2607 |
1.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2209 LQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKdKDNTQKFLAKEADNMKKLAEDAARLSVEAQ 2288
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2289 EAARLRQIAEddLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLmqqrldeeteeyqksl 2368
Cdd:COG4717 127 LLPLYQELEA--LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL---------------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2369 eAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQ-EKMTVVEKLEVARLTSSKEADD 2447
Cdd:COG4717 189 -ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2448 LRKAIADLEK-----------EKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVlqQTFLSEKEMLLKKEKLIEEEKKRL 2516
Cdd:COG4717 268 LLSLILTIAGvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEEL--EELLAALGLPPDLSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2517 ESQFEEEVKKAKALkdEQERQKQQMEDEKKKL----QATMDAALNKQKEAEKEMHNKQKEMKELER-----KRLEQERIL 2587
Cdd:COG4717 346 IEELQELLREAEEL--EEELQLEELEQEIAALlaeaGVEDEEELRAALEQAEEYQELKEELEELEEqleelLGELEELLE 423
|
410 420
....*....|....*....|
gi 1927222988 2588 AEENQKLREKLQQLEEAQKD 2607
Cdd:COG4717 424 ALDEEELEEELEELEEELEE 443
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1545-1884 |
1.57e-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: 54.96 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1545 EDLENLKRQAEEAERQVKQAE-IEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTskLEESLKQEHGAVLQLQhEAAALK 1623
Cdd:COG3096 836 AELAALRQRRSELERELAQHRaQEQQLRQQLDQLKEQLQLLNKLLPQANLLADET--LADRLEELREELDAAQ-EAQAFI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1624 KQQEDAERAREEAEKELEKWRQKaNEALRLRLQAEEEAHKKSLAQEDAEKQ----------KEEAEREAKKRAKAEdsAL 1693
Cdd:COG3096 913 QQHGKALAQLEPLVAVLQSDPEQ-FEQLQADYLQAKEQQRRLKQQIFALSEvvqrrphfsyEDAVGLLGENSDLNE--KL 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1694 KQK-EMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELY-------------------RLKNEVV 1753
Cdd:COG3096 990 RARlEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEelgvqadaeaeerarirrdELHEELS 1069
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1754 AAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETmsnserskqlleveaTKMRDLAEEASK----LRAIAEEAKHQRQVA 1829
Cdd:COG3096 1070 QNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDY---------------KQEREQVVQAKAgwcaVLRLARDNDVERRLH 1134
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 1830 EEEAARQRAeaerilkEKLAAISDatrlktEAEIALKEKEAENERLR---RQAEDEAY 1884
Cdd:COG3096 1135 RRELAYLSA-------DELRSMSD------KALGALRLAVADNEHLRdalRLSEDPRR 1179
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1729-2180 |
1.85e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 54.14 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1729 ADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKE---TMSNSERSKQLLEveatKM 1805
Cdd:COG5278 79 EPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEaalALVRSGEGKALMD----EI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1806 RDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQ 1885
Cdd:COG5278 155 RARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1886 RKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAE 1965
Cdd:COG5278 235 LAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1966 ETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQI 2045
Cdd:COG5278 315 AAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2046 LMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEA 2125
Cdd:COG5278 395 IAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAAL 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 2126 ANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQ 2180
Cdd:COG5278 475 AALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAE 529
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2266-2629 |
1.85e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 54.34 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2266 LAKEADNMKKLaedaaRLSVEAQeaarLRQiAEDDLNQQRALADKMLK--EKMQAIQEASRLRAEaEMLQRQKDLAQEQ- 2342
Cdd:pfam05483 83 LYKEAEKIKKW-----KVSIEAE----LKQ-KENKLQENRKIIEAQRKaiQELQFENEKVSLKLE-EEIQENKDLIKENn 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2343 -AQKLLEDKQLMQQRLDEETEEYQKSLEAERK----------------RQLEIIAESEKLKLQVsQLSEAQAKAQEEAKK 2405
Cdd:pfam05483 152 aTRHLCNLLKETCARSAEKTKKYEYEREETRQvymdlnnniekmilafEELRVQAENARLEMHF-KLKEDHEKIQHLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2406 FKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKA-------IADLEKEKSRLKKEAEDLQnKSKEMAD 2478
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKtklqdenLKELIEKKDHLTKELEDIK-MSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2479 AQQKQIEHE-----KTVLQQTflSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMD 2553
Cdd:pfam05483 310 STQKALEEDlqiatKTICQLT--EEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQ 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2554 AALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQ--KLREKLQQLEEA--------QKDQPDKEvIHVTMVETTK 2623
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQElifllqarEKEIHDLE-IQLTAIKTSE 466
|
....*.
gi 1927222988 2624 NVYNGQ 2629
Cdd:pfam05483 467 EHYLKE 472
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1347-1570 |
2.86e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1347 TDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELklrmQEEVNRREDAVVDAEKQKHN 1426
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1427 IQLELHELKNLSEQQI--------------MDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAA 1492
Cdd:COG4942 95 LRAELEAQKEELAELLralyrlgrqpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 1493 EAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKER 1570
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2320-2612 |
3.02e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2320 QEASRLRAEAEMLQRQKDLAQEQ---AQKLLEDKQLMQQRLDEETEEYQKS----LEAERKRQlEIIAESEKLKLQVSQL 2392
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETrdeADEVLEEHEERREELETLEAEIEDLretiAETERERE-ELAEEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2393 SEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNK 2472
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2473 SKEMADA------QQKQIEHEKTVLQQTF----------LSEKEMLLKKEKLIEEEKKRLESQFEEE---VKKAKALK-- 2531
Cdd:PRK02224 372 LEEAREAvedrreEIEELEEEIEELRERFgdapvdlgnaEDFLEELREERDELREREAELEATLRTArerVEEAEALLea 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2532 -------------------DEQERQKQQMEDEKKKLQATMDaALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQ 2592
Cdd:PRK02224 452 gkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVE-EVEERLERAEDLVEAEDRIERLEERREDLEELIAERRE 530
|
330 340
....*....|....*....|
gi 1927222988 2593 KLREKLQQLEEAQKDQPDKE 2612
Cdd:PRK02224 531 TIEEKRERAEELRERAAELE 550
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1599-1923 |
3.23e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 53.36 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1599 SKLEESLkQEHGAVLQLQHeaaALKKQQEDAERAREEAEKELEKWRQkaneALRLRLQAEEEAHKKSLA-QEDAEKQKEE 1677
Cdd:pfam07888 34 NRLEECL-QERAELLQAQE---AANRQREKEKERYKRDREQWERQRR----ELESRVAELKEELRQSREkHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1678 AEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQ 1757
Cdd:pfam07888 106 LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1758 QRKQLEDELAKVRSEMD----VLIQLKSKAEKETMSNSERSKQLLEVEATK--MRDLAEEASKLRAIAEEAKhqRQVAEE 1831
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLeeLRSLQERLNASERKVEGLG--EELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1832 EAARQRAEAErILKEKLAAISDATRLkTEAEIALKEKEA----ENERLRRQAEDEAYQRKALedqaNQHKQQIEEKIvll 1907
Cdd:pfam07888 264 AAQRDRTQAE-LHQARLQAAQLTLQL-ADASLALREGRArwaqERETLQQSAEADKDRIEKL----SAELQRLEERL--- 334
|
330
....*....|....*.
gi 1927222988 1908 kksSEAEMERQRAIVD 1923
Cdd:pfam07888 335 ---QEERMEREKLEVE 347
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1438-1787 |
3.49e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1438 SEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVK----QKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVN 1513
Cdd:pfam07888 39 CLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRelesRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1514 EETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKErQIQVAHVAAQ---KSAAAELQSK 1590
Cdd:pfam07888 119 ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK-QLQAKLQQTEeelRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1591 HMSFVEKTSKLEE------SLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKK 1664
Cdd:pfam07888 198 RNSLAQRDTQVLQlqdtitTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1665 SLAQEDAEKQ--------KEEAEREAKKRAKAEDSALKQKEMAEN---ELERQRKVAESTAQQKLTAEQELIRLRadfDN 1733
Cdd:pfam07888 278 RLQAAQLTLQladaslalREGRARWAQERETLQQSAEADKDRIEKlsaELQRLEERLQEERMEREKLEVELGREK---DC 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1927222988 1734 AEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVrseMDVLIQLKSKAEKET 1787
Cdd:pfam07888 355 NRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL---LEYIRQLEQRLETVA 405
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2084-2236 |
3.55e-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: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2084 EKAKKLAKQAEAAKEKAEREAALLRQQAE-EAERQKAAAEQEAANQAKAQEDAERLRKEAEFEA---AKRAQAENAALKQ 2159
Cdd:COG2268 192 RKIAEIIRDARIAEAEAERETEIAIAQANrEAEEAELEQEREIETARIAEAEAELAKKKAEERReaeTARAEAEAAYEIA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2160 KQQADAEMAKHKKLAEQT------LKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRlkdevdDAVKQRGQVEEELLKV 2233
Cdd:COG2268 272 EANAEREVQRQLEIAEREreielqEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEA------EAIRAKGLAEAEGKRA 345
|
...
gi 1927222988 2234 KVQ 2236
Cdd:COG2268 346 LAE 348
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1140-1567 |
3.65e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1140 KLKKMRAEAEGEQPVFDSLEAELKKATAVSDKMSRVHSERDAELDHYRQLLSSLQD--RWKAVFSQIDLRQRELEQLGRQ 1217
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1218 LGYYRESYDWLIRWINDAKQRQEKIQAVTITDSKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDyELQLVA 1297
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE-ELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1298 YKAQVEPLASPLKKTKLDSASDNIIqeyVTLRTKYSELMTLTSQYIKFITDSQ-------RRLEDEEKAAEKLKAEEQKK 1370
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAAAL---LALLGLGGSLLSLILTIAGVLFLVLgllallfLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1371 MAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAvvDAEKQKHNIQLELHELKNLSEQQIMDKSKQVD 1450
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA--EELEEELQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1451 DAL---QSRVKIEEEIRLIRLQLE--TTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEE 1525
Cdd:COG4717 389 AALeqaEEYQELKEELEELEEQLEelLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1927222988 1526 lkrkaeaekeaakqkqkalEDLENLKRQAEEAERQVKQAEIE 1567
Cdd:COG4717 469 -------------------GELAELLQELEELKAELRELAEE 491
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
36-153 |
3.78e-06 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 49.66 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 36 DGRKDERDRVQKKTFTKWVNK---------HLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKL 102
Cdd:cd21323 15 EGTQHSYSEEEKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTIS 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1927222988 103 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQI 153
Cdd:cd21323 95 ENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1401-2092 |
4.11e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1401 ELKLRmQEEVNRREDAVVDAEKQKHNIQLELHELKNlSEQQIMDKSKQVDDALQsrvKIEEEIRLIRLQLETTVKQKSTA 1480
Cdd:TIGR04523 48 ELKNK-EKELKNLDKNLNKDEEKINNSNNKIKILEQ-QIKDLNDKLKKNKDKIN---KLNSDLSKINSEIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1481 ESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQ--AEEAE 1558
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKllKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1559 RQVKQAEIEKERqiqvahvaaqksaaaELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEK 1638
Cdd:TIGR04523 203 LSNLKKKIQKNK---------------SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1639 ELEKwrqkanealrlrLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEmaenELERQrkvaestaqqkl 1718
Cdd:TIGR04523 268 QLSE------------KQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS----ELKNQ------------ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1719 taEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKaEKETMSNSERSKQLL 1798
Cdd:TIGR04523 320 --EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS-YKQEIKNLESQINDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1799 EveaTKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEaerILKEKlAAISDATRLKTEAEIALKEKEAENERLRRQ 1878
Cdd:TIGR04523 397 E---SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET---IIKNN-SEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1879 AEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDdtlkqrrvVEEEIRILKLNFEKASSGKLDLELELN 1958
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD--------LTKKISSLKEKIEKLESEKKEKESKIS 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1959 KLKNIAEETQQSKLRAEEEAEKLRKlaleeekrrreaeekVKKIAAAEEeaarqrqaaqdELDRLKKKAEEarKQKDDAD 2038
Cdd:TIGR04523 542 DLEDELNKDDFELKKENLEKEIDEK---------------NKEIEELKQ-----------TQKSLKKKQEE--KQELIDQ 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 2039 KEAEKQILMAQQAA--QKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQ 2092
Cdd:TIGR04523 594 KEKEKKDLIKEIEEkeKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1459-2312 |
4.23e-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: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1459 IEEEIRLIRLQLEttVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKL-RKQVNEETQKKRMAEEElkrkaeaekeaa 1537
Cdd:COG3096 302 AEEQYRLVEMARE--LEELSARESDLEQDYQAASDHLNLVQTALRQQEKIeRYQEDLEELTERLEEQE------------ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1538 kqkqkalEDLENLKRQAEEAERQVKQAEIEKER--------------------QIQVAhVAAQKSAAAELQSKHMS---F 1594
Cdd:COG3096 368 -------EVVEEAAEQLAEAEARLEAAEEEVDSlksqladyqqaldvqqtraiQYQQA-VQALEKARALCGLPDLTpenA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1595 VEKTSKLEESLKQEHGAVLQLQHE---AAALKKQQEDAERAREEAEKELEKWR--QKANEALR----LRLQAEEEAH-KK 1664
Cdd:COG3096 440 EDYLAAFRAKEQQATEEVLELEQKlsvADAARRQFEKAYELVCKIAGEVERSQawQTARELLRryrsQQALAQRLQQlRA 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1665 SLAQ-EDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSlled 1743
Cdd:COG3096 520 QLAElEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK---- 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1744 ELYRLKNEVVAAQQQRKQLEDEL-AKVRSEMDVLIQLKSKAEKETMSNSERS-----KQLLE-----------VEATKMR 1806
Cdd:COG3096 596 ELAARAPAWLAAQDALERLREQSgEALADSQEVTAAMQQLLEREREATVERDelaarKQALEsqierlsqpggAEDPRLL 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1807 DLAE-----------------EASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAIS-------DATRLKTEAE 1862
Cdd:COG3096 676 ALAErlggvllseiyddvtleDAPYFSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLYLIEgdpdsfdDSVFDAEELE 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1863 IALKEKEAENE-RLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVD--DTLKQRRVV------E 1933
Cdd:COG3096 756 DAVVVKLSDRQwRYSRFPEVPLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAfsQFVGGHLAVafapdpE 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1934 EEIRilKLNFEKAssgklDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRReaeekvkkiaaaeeeaarqr 2013
Cdd:COG3096 836 AELA--ALRQRRS-----ELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLAD-------------------- 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2014 qaaqdelDRLKKKAEEARKQKDDADKeaekqilmAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAK----KL 2089
Cdd:COG3096 889 -------ETLADRLEELREELDAAQE--------AQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKeqqrRL 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2090 AKQAEAAKEKAEREAALlrqQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEfEAAKRAQAEnaaLKQKQQADAEMAK 2169
Cdd:COG3096 954 KQQIFALSEVVQRRPHF---SYEDAVGLLGENSDLNEKLRARLEQAEEARREAR-EQLRQAQAQ---YSQYNQVLASLKS 1026
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2170 HKKLAEQTLKqkfQVEQELTKVKLKLDETDKQKSvlDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELlklklriee 2249
Cdd:COG3096 1027 SRDAKQQTLQ---ELEQELEELGVQADAEAEERA--RIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSL--------- 1092
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 2250 eNQRLIKKDKDNTQkfLAKEADNMKKLAEDAARLSVEAQEAARL--RQIAEDDLNQQRALADKML 2312
Cdd:COG3096 1093 -QKRLRKAERDYKQ--EREQVVQAKAGWCAVLRLARDNDVERRLhrRELAYLSADELRSMSDKAL 1154
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2318-2579 |
4.24e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2318 AIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLdeeteeyqKSLEAERKRQLEIIAESEK-LKLQVSQLSEAQ 2396
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL--------AALERRIAALARRIRALEQeLAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2397 AKAQEEAKKFKKQADSIASRLhetelATQEKMTVVEKLEVarLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEM 2476
Cdd:COG4942 90 KEIAELRAELEAQKEELAELL-----RALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2477 AdAQQKQIEHEKTVLQQtflsekemllkkeklieeekkrLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAAL 2556
Cdd:COG4942 163 A-ALRAELEAERAELEA----------------------LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
250 260
....*....|....*....|...
gi 1927222988 2557 NKQKEAEKEMHNKQKEMKELERK 2579
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAER 242
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
2285-2621 |
4.24e-06 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 53.41 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2285 VEAQEAARLRQIAEDDLNQQRAladkmlkekmQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLE--DKQLMQQR--LDEE 2360
Cdd:pfam15818 10 LEALEELRMRREAETQYEEQIG----------KIIVETQELKWQKETLQNQKETLAKQHKEAMAvfKKQLQMKMcaLEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2361 TEEYQKSLEAERKrqlEIIAESEKLK-LQVSQ------LSEAQAKAQ------EEAKK----FKKQADSIASRL------ 2417
Cdd:pfam15818 80 KGKYQLATEIKEK---EIEGLKETLKaLQVSKyslqkkVSEMEQKLQlhllakEDHHKqlneIEKYYATITGQFglvken 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2418 -----HETELATQ--EKMTVVEKLEVARLTSSKEadDLRKAIADLEKEK----SRLKKEAEDLQNKSKEMADAQQ----- 2481
Cdd:pfam15818 157 hgkleQNVQEAIQlnKRLSALNKKQESEICSLKK--ELKKVTSDLIKSKvtcqYKMGEENINLTIKEQKFQELQErlnme 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2482 ----KQIEHEKTVLQ---QTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLqatmda 2554
Cdd:pfam15818 235 lelnKKINEEITHIQeekQDIIISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKF------ 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2555 aLNKQKEAEKEMHNKQKEMKELERKRLE---QERILAEENQKLREKLQQLEEAQKDQPDKEVIHVTMVET 2621
Cdd:pfam15818 309 -LNLQNEHEKALGTWKKHVEELNGEINEiknELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPEVNN 377
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
950-1569 |
4.50e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 950 DDRMQIEEDYTKSTQHFDSLIRSMEKGLMVVrhkgqqdetlcknyLSEIKDLRLRIEDCEaGTVARIRRpvEKEPLKECV 1029
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEV--------------LREINEISSELPELR-EELEKLEK--EVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1030 QKTTEQKKvqvELEGLKKDLNKVSAKTKEvlaspqqtasapvLRSELDLTVekmdhthmlssvylEKLKTVEMVIRNTQG 1109
Cdd:PRK03918 238 EEIEELEK---ELESLEGSKRKLEEKIRE-------------LEERIEELK--------------KEIEELEEKVKELKE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1110 AEGVLKQYEDClrevhtvpndVKEVETYRTKLKKMRAEAEGEQPVFDSLEAELKKAtavSDKMSRVhSERDAELDHYRQL 1189
Cdd:PRK03918 288 LKEKAEEYIKL----------SEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL---EEKEERL-EELKKKLKELEKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1190 LSSLQDRWKAvFSQIDLRQRELEQLGRQLGYYreSYDWLIRWINDAKQRQEKIQA--VTITDSK-TLKEQLAQEKKLLEE 1266
Cdd:PRK03918 354 LEELEERHEL-YEEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEeiSKITARIgELKKEIKELKKAIEE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1267 VEGNKDKVDECQKyakayiDTIKDYELQLVA-YKAQVEPLASPLKktKLDSASDNIIQEYVTLRTKYSElmtltsqyikf 1345
Cdd:PRK03918 431 LKKAKGKCPVCGR------ELTEEHRKELLEeYTAELKRIEKELK--EIEEKERKLRKELRELEKVLKK----------- 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1346 itdsQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMqEEVNRREDAVVDAEKQKH 1425
Cdd:PRK03918 492 ----ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL-EKLEELKKKLAELEKKLD 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1426 NIQLELHELKNlseqQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEA 1505
Cdd:PRK03918 567 ELEEELAELLK----ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1927222988 1506 EKLRKQVNEetQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKE 1569
Cdd:PRK03918 643 EELRKELEE--LEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1700-1923 |
4.54e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1700 ENELERQRKVAEsTAQQKLTA---EQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVL 1776
Cdd:COG3206 181 EEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1777 iqlkskaeketmSNSERSKQLLEVEATKMRDLAEEASKLRaiaeeAKH-QRQVAEEEAARQRAEAERILKEKLAAI-SDA 1854
Cdd:COG3206 260 ------------LQSPVIQQLRAQLAELEAELAELSARYT-----PNHpDVIALRAQIAALRAQLQQEAQRILASLeAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222988 1855 TRLKTEAEIALKEKEAENERLRRQAEDEAyQRKALEDQANQHKQQIEEkivLLKKSSEAEMERQRAIVD 1923
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYES---LLQRLEEARLAEALTVGN 387
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2132-2408 |
4.72e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.84 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2132 QEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQ---ELTKVKLKLDETDKQKSVLDEE 2208
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDElneKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2209 LQRLKDEVDDAVKQRGQVEeellKVKVQMEELLK----LKLRIEEENQrLIKKDKDntqkfLAKEADNMKKLAEDAARLS 2284
Cdd:COG1340 94 LDELRKELAELNKAGGSID----KLRKEIERLEWrqqtEVLSPEEEKE-LVEKIKE-----LEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2285 VEAQEAARLRQIAEDDLNQQRALADKM--LKEKMQAI-QEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLdeet 2361
Cdd:COG1340 164 ELRAELKELRKEAEEIHKKIKELAEEAqeLHEEMIELyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL---- 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1927222988 2362 EEYQKSLEAERKRQLEIIAESEKlklqvsqlSEAQAKAQEEAKKFKK 2408
Cdd:COG1340 240 RELRKELKKLRKKQRALKREKEK--------EELEEKAEEIFEKLKK 278
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1693-1926 |
4.76e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1693 LKQKEMAENELERQRKVAESTAQQKLTAEQElirlradfdnAEQQRsLLEDELYRLknevvAAQQQRKQLEDELAKVRSE 1772
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQA----------AEQER-LKQLEKERL-----AAQEQKKQAEEAAKQAALK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1773 mdvliqlKSKAEKETMSNSERSKQLLEVEATKMRDLAEEAsklraiAEEAKHQRQVAEEEAARQRAEAERILKEKLAAIS 1852
Cdd:PRK09510 131 -------QKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKA------AAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAA 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1927222988 1853 DAtrlKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDqanqhKQQIEEKIVLLKKSSEAEMERQRAIVDDTL 1926
Cdd:PRK09510 198 EA---KKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAE-----AKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1877-2118 |
4.80e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1877 RQAEDEAYQRKALEDQANQHKQQIEEkivlLKKSSEAEMERQRAivddtLKQRRVVEEEIRIlklnfEKASSGKLDLELE 1956
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEE----LQQKQAAEQERLKQ-----LEKERLAAQEQKK-----QAEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1957 LNKLKNIAEETQQSKLRAEEEAEKLRKLAleeekrrreaeekvKKIAAAEEEAarqrqaaqDELDRLKKKAEEARKQkdd 2036
Cdd:PRK09510 132 KQAEEAAAKAAAAAKAKAEAEAKRAAAAA--------------KKAAAEAKKK--------AEAEAAKKAAAEAKKK--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2037 adKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTimqtklkeeyEKAKKLAKQAEAAKEKAEREAAllRQQAEEAER 2116
Cdd:PRK09510 187 --AEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA----------EAKAAAAKAAAEAKAAAEKAAA--AKAAEKAAA 252
|
..
gi 1927222988 2117 QK 2118
Cdd:PRK09510 253 AK 254
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2145-2550 |
5.00e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2145 EAAKRAQAENAALKQKQQADAEmakhKKLAEQtlkqkfqvEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRG 2224
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSR----RQLAAE--------QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2225 QVEeellKVKVQMEELLKLKLRIEEenqrlikkdkdntQKFLAKEADNMKKLAEdaARLSVEAQEAARLR-QIAED---- 2299
Cdd:PRK04863 346 QQE----KIERYQADLEELEERLEE-------------QNEVVEEADEQQEENE--ARAEAAEEEVDELKsQLADYqqal 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2300 DLNQQRALAdkmlkekmqaIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETE--EYQKSLEAERKRQLE 2377
Cdd:PRK04863 407 DVQQTRAIQ----------YQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLslEQKLSVAQAAHSQFE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2378 IIAES-EKLKLQVSQlSEAQAKAQE---EAKKFKKQADS---IASRLHETELATQEKMTVVEKLEVARLTSSKEADDlrk 2450
Cdd:PRK04863 477 QAYQLvRKIAGEVSR-SEAWDVAREllrRLREQRHLAEQlqqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD--- 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2451 aIADLEKEKSRLKKEAEDLqNKSKEMADAQQKQIEHEKTVLQQTFlSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKAL 2530
Cdd:PRK04863 553 -EDELEQLQEELEARLESL-SESVSEARERRMALRQQLEQLQARI-QRLAARAPAWLAAQDALARLREQSGEEFEDSQDV 629
|
410 420 430
....*....|....*....|....*....|....*..
gi 1927222988 2531 -----------------KDEQERQKQQMEDEKKKLQA 2550
Cdd:PRK04863 630 teymqqllerereltveRDELAARKQALDEEIERLSQ 666
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1672-2034 |
5.12e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1672 EKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNE 1751
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1752 VVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIaeeakhQRQVAEE 1831
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL------EEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1832 EAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSS 1911
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1912 EAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKR 1991
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1927222988 1992 RREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQK 2034
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
620-712 |
5.34e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.71 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 620 HAFVSAATKELMWLNDKEEEEVNFDWSDRNSNMTAKKDNYSGLMRELELREKKVNDIQATGDKLVRDGHPGKKTVESFTA 699
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1927222988 700 ALQTQWSWILQLC 712
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3920-3958 |
5.56e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.78 E-value: 5.56e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1927222988 3920 YLEGTSCIAGVFLETSKERLSIYQAMKKNMIRPGTAFEL 3958
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1866-2182 |
5.57e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.77 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1866 KEKEAENERLRRQAEDEAyqrKALEDQANQHKQQIEEkivlLKKSSEAEMERQRAivddtLKQRRVVEEEIRilklNFEK 1945
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAA---KKEQERQKKLEQQAEE----AEKQRAAEQARQKE-----LEQRAAAEKAAK----QAEQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1946 ASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLAleeekrrreaeekvkkiaaaeeeaarqrqaAQDELDRLKK 2025
Cdd:TIGR02794 110 AAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAA------------------------------KQAEEEAKAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2026 KAEEARKQKDDADKEAEKQILMAQQAAQKCsaaeqqvqsvlaqqkedtimqtklkeeyeKAKKLAKQAEAAKEKAEREAA 2105
Cdd:TIGR02794 160 AAAEAKKKAEEAKKKAEAEAKAKAEAEAKA-----------------------------KAEEAKAKAEAAKAKAAAEAA 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222988 2106 LLRQQAEEAERQKAaaeqeaanqakAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKF 2182
Cdd:TIGR02794 211 AKAEAEAAAAAAAE-----------AERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQNL 276
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1680-2136 |
5.65e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.60 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1680 REAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQR 1759
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1760 KQLEDELAKVRSEmdvliqlkskAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAE 1839
Cdd:COG5278 162 ALALAALLLAAAA----------LLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1840 AERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQR 1919
Cdd:COG5278 232 LELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1920 AIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKV 1999
Cdd:COG5278 312 AAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2000 KKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKL 2079
Cdd:COG5278 392 VLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAV 471
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222988 2080 KEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAE 2136
Cdd:COG5278 472 AALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASA 528
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1439-1753 |
6.09e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1439 EQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQK 1518
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1519 KRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKT 1598
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1599 SKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEAlrlRLQAEEEAHKKSLAQEDAEKQKEEA 1678
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV---ILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 1679 EREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVV 1753
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDV 355
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2080-2292 |
6.31e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 52.64 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2080 KEEYEKAKKLAKQAEAAKEKAE--REAALLRQQAEEA-ERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAA 2156
Cdd:PRK05035 464 REKAAREARHKKAAEARAAKDKdaVAAALARVKAKKAaATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAA 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2157 LKQKQQADAEM--AKHKKLAEQTLKQKFQVEQELTKVKL--KLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLK 2232
Cdd:PRK05035 544 DPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDPKKAAVaaAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIAR 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222988 2233 VKVQMEELLKLKLRIEEENQRL-----------IKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAAR 2292
Cdd:PRK05035 624 AKAKKAEQQANAEPEEPVDPRKaavaaaiarakARKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQ 694
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2169-2486 |
6.77e-06 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 51.49 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2169 KHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIE 2248
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2249 EENQRLIkkdkdNTQKFLAKEadnmkklaEDAARLSVEAQEAARLRQIaEDDLNQQRALADKMLKEKMQaiqeasrLRAE 2328
Cdd:pfam09728 81 KQNKKLK-----EESKKLAKE--------EEEKRKELSEKFQSTLKDI-QDKMEEKSEKNNKLREENEE-------LREK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2329 AEMLQRQKDLAQEQAQKLLEDKQLMQQRLdeETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKK 2408
Cdd:pfam09728 140 LKSLIEQYELRELHFEKLLKTKELEVQLA--EAKLQQATEEEEKKAQEKEVAKARELKAQVQTLSETEKELREQLNLYVE 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 2409 QADSIASRLhetelatqekmtvvEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEH 2486
Cdd:pfam09728 218 KFEEFQDTL--------------NKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEE 281
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2320-2488 |
7.10e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2320 QEASRLRAEaemlQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLE----AERKRQLEIIAESEKLKLQVSQLSEA 2395
Cdd:PRK09510 70 QQKSAKRAE----EQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEqkkqAEEAAKQAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2396 QAKAQEEAKKF---KKQADSIASRLHETELA------TQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKS--RLKK 2464
Cdd:PRK09510 146 KAKAEAEAKRAaaaAKKAAAEAKKKAEAEAAkkaaaeAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAaaEAKA 225
|
170 180
....*....|....*....|....
gi 1927222988 2465 EAEDLQNKSKEMADAQQKQIEHEK 2488
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEK 249
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1669-2072 |
7.65e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1669 EDAEKQKEEAEREAKKRAKAEDsALKQKEMAENELERQRKVAEStAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRL 1748
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQE-ELEELEEELEELEAELEELRE-ELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1749 KN---EVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEveaTKMRDLAEEASKLRAIAEEAKHQ 1825
Cdd:COG4717 152 EErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ---QRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1826 RQVAEEEAARQrAEAERILKEKLAAISDATRLKTEAE-------------------------IALKEKEAENERLRRQAE 1880
Cdd:COG4717 229 LEQLENELEAA-ALEERLKEARLLLLIAAALLALLGLggsllsliltiagvlflvlgllallFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1881 DEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKAS---SGKLDLELEL 1957
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1958 NKLKNIAEETQQSKLRAEEEAEKLRKL-----ALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARK 2032
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELlgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1927222988 2033 QKDDADKEAEKQILMAQ-----QAAQKCSAAEQQVQSVLAQQKED 2072
Cdd:COG4717 468 DGELAELLQELEELKAElrelaEEWAALKLALELLEEAREEYREE 512
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
45-146 |
9.14e-06 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 47.80 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 45 VQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRF----HKLQNVQIALDFLKHRQVKLV 120
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1927222988 121 NIRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
2035-2243 |
1.06e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 50.88 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2035 DDADKEAEKQILMAQQAAQKcsAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEA 2114
Cdd:pfam00529 52 DPTDYQAALDSAEAQLAKAQ--AQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2115 ErqkaAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKH-KKLAEQTLKQKFQVEQELTKVKL 2193
Cdd:pfam00529 130 R----VLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEvRSELSGAQLQIAEAEAELKLAKL 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222988 2194 KLDETDkQKSVLDEELQRLKDEVDDAVKQRGQ-----------------VEEELLKVKVQMEELLKL 2243
Cdd:pfam00529 206 DLERTE-IRAPVDGTVAFLSVTVDGGTVSAGLrlmfvvpednllvpgmfVETQLDQVRVGQPVLIPF 271
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1322-1772 |
1.07e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1322 IQEYVTLRTKYSELMTLTSQYIKfITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHA--KAIAKAEKEA 1399
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1400 QELKLRMQEEVNRREDaVVDAEKQKHNIQLELHELKNLS----EQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLEttvk 1475
Cdd:COG4717 149 EELEERLEELRELEEE-LEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELE---- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1476 qksTAESELKQLRDRAAEAEKLRKAAQEEAEKL--RKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQ 1553
Cdd:COG4717 224 ---ELEEELEQLENELEAAALEERLKEARLLLLiaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1554 AEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKH-MSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQedaera 1632
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEElLELLDRIEELQELLREAEELEEELQLEELEQEIAA------ 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1633 reeaekELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAED-----SALKQKEMAENELERQR 1707
Cdd:COG4717 375 ------LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeeleEELEELEEELEELEEEL 448
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 1708 KVAeSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSE 1772
Cdd:COG4717 449 EEL-REELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2249-2449 |
1.16e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2249 EENQRLIKKDKDNTQKFLAKEADNMKKLAEDAAR-----------LSVEAQEAARLRQIAE------------DDLNQQR 2305
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAaleefrqknglVDLSEEAKLLLQQLSElesqlaearaelAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2306 ALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQA---QKLLEDKQLMQQrLDEETEEYQKSLEAERKRQL-EIIAE 2381
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAelsARYTPNHPDVIA-LRAQIAALRAQLQQEAQRILaSLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 2382 SEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLR 2449
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1251-1786 |
1.17e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1251 KTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQveplasplkKTKLDSASDNIIQEYVTLRT 1330
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE---------KLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1331 KYSELMTLTSQYiKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDK-QKQLAEVhakaIAKAEKEAQELKlRMQEE 1409
Cdd:TIGR04523 202 LLSNLKKKIQKN-KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtQTQLNQL----KDEQNKIKKQLS-EKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1410 VNRREDAVVDAEKQKHNIQLELHELKNLSEQQIMDKSKqvddalqsrvkieEEIRLIRLQLETTVKQKSTAESELKQLRD 1489
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK-------------SELKNQEKKLEEIQNQISQNNKIISQLNE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1490 RAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEElkrkaeaekeaakqKQKALEDLENLKRQAEEAERQV-KQAEIEK 1568
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE--------------NQSYKQEIKNLESQINDLESKIqNQEKLNQ 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1569 ERQIQVAHVAAQKSaaaELQSKHMSFVEKTSKLEESLKqehgavlQLQHEAAALKKQQEDAERAREEAEKELEKWRQKAN 1648
Cdd:TIGR04523 409 QKDEQIKKLQQEKE---LLEKEIERLKETIIKNNSEIK-------DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1649 EalrlrLQAEEEAHKKSLAQEDAE-----KQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQE 1723
Cdd:TIGR04523 479 K-----IKQNLEQKQKELKSKEKElkklnEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 1724 LIR--LRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKE 1786
Cdd:TIGR04523 554 LKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE 618
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1685-1860 |
1.30e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1685 RAKAEDSALKQKEMAENELERQRKVAESTAQQKLT-AEQELIRLRADFDNAEQQRsllEDELYRLKNEVvaaQQQRKQLE 1763
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRER---RNELQKLEKRL---LQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1764 DELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDL-------AEEASK--LRAIAEEAKHQRQV----AE 1830
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisgltAEEAKEilLEKVEEEARHEAAVlikeIE 179
|
170 180 190
....*....|....*....|....*....|.
gi 1927222988 1831 EEAarqRAEAERILKEKLA-AIsdaTRLKTE 1860
Cdd:PRK12704 180 EEA---KEEADKKAKEILAqAI---QRCAAD 204
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1653-1975 |
1.42e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1653 LRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFD 1732
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1733 NAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQL-LEVEATKMRDLAEE 1811
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALeQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1812 ASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALED 1891
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1892 QANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSK 1971
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
....
gi 1927222988 1972 LRAE 1975
Cdd:COG4372 345 LLLV 348
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1915-2625 |
1.43e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 51.29 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1915 MERQRAIVDDTLKQRRVVEEEIRILKlnfekassgkldlelelnklkniaEETQQSKLRAEEEAEKLRKLALeeekrrre 1994
Cdd:pfam07111 61 LSQQAELISRQLQELRRLEEEVRLLR------------------------ETSLQQKMRLEAQAMELDALAV-------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1995 aeekvkkiaaaeeeAARQRQAAQDELDRLKKKAEEARKQKDDAD-KEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDt 2073
Cdd:pfam07111 109 --------------AEKAGQAEAEGLRAALAGAEMVRKNLEEGSqRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEG- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2074 iMQTKLKEEYEKAKKLAKQAeaakEKAEREAALLRQQaeeaerqkaaaeqeaanQAKAQEDAErlrkeaefeaAKRAQAE 2153
Cdd:pfam07111 174 -LEKSLNSLETKRAGEAKQL----AEAQKEAELLRKQ-----------------LSKTQEELE----------AQVTLVE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2154 NAalkqkqqadaemakhkklaeqtlkQKFQVEQELTKVKLKLDETDKQKsvLDEELQRLKDEVDDAvkqrgQVEEELLKV 2233
Cdd:pfam07111 222 SL------------------------RKYVGEQVPPEVHSQTWELERQE--LLDTMQHLQEDRADL-----QATVELLQV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2234 KVQ-MEELLKLKlriEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVeaqeaarlrQIAEDDLNQQRALadKML 2312
Cdd:pfam07111 271 RVQsLTHMLALQ---EEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMV---------QLKAQDLEHRDSV--KQL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2313 KEKMQAIQEasrlraeaemlqRQKDLAQEQA--QKLLEDK--QLMQQRLDEET--EEYQKSLEAERKRQLEIIAESEKLK 2386
Cdd:pfam07111 337 RGQVAELQE------------QVTSQSQEQAilQRALQDKaaEVEVERMSAKGlqMELSRAQEARRRQQQQTASAEEQLK 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2387 LQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTV----VEKLEVA--RLTSSKEADDLRKAIADLEKEKS 2460
Cdd:pfam07111 405 FVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIkglmARKVALAqlRQESCPPPPPAPPVDADLSLELE 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2461 RLKKEAEDLQ--------------NKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKK 2526
Cdd:pfam07111 485 QLREERNRLDaelqlsahliqqevGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASL 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2527 AKALKDEQERQKQQMEDEKKKLQATMDAALNKQK----EAEKEMHNKQKEMKELERKRLEQErilaEENQKLReKLQqlE 2602
Cdd:pfam07111 565 RQELTQQQEIYGQALQEKVAEVETRLREQLSDTKrrlnEARREQAKAVVSLRQIQHRATQEK----ERNQELR-RLQ--D 637
|
730 740
....*....|....*....|...
gi 1927222988 2603 EAQKDQPDKEVIHVTMVETTKNV 2625
Cdd:pfam07111 638 EARKEEGQRLARRVQELERDKNL 660
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2059-2460 |
1.44e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.84 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2059 EQQVQSVLAQQKEDTIMQTKLKEE---YEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERqkaaaeqeaaNQAKAQEDA 2135
Cdd:pfam19220 37 EAILRELPQAKSRLLELEALLAQEraaYGKLRRELAGLTRRLSAAEGELEELVARLAKLEA----------ALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2136 ERLRKEaefEAAKRAQAENaaLKQKQQADAEMAKHKKLAEQTLKQKFQVeqeltkvklkldetdkqksvLDEELQRLKDE 2215
Cdd:pfam19220 107 EELRIE---LRDKTAQAEA--LERQLAAETEQNRALEEENKALREEAQA--------------------AEKALQRAEGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2216 VDDAVKQRGQVEEELLKVKVQMEE----LLKLKLRIEEENQRLikkdkdntqkflakeADNMKKLAEDAARLSVEAQEAA 2291
Cdd:pfam19220 162 LATARERLALLEQENRRLQALSEEqaaeLAELTRRLAELETQL---------------DATRARLRALEGQLAAEQAERE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2292 RLRQIAEDDLNQQRAlADKMLKEKMQAIQE----ASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEyqks 2367
Cdd:pfam19220 227 RAEAQLEEAVEAHRA-ERASLRMKLEALTAraaaTEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAG---- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2368 LEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLhETELATQEKmtvveKLEVARLTSSKEADD 2447
Cdd:pfam19220 302 LEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASL-SDRIAELTK-----RFEVERAALEQANRR 375
|
410
....*....|...
gi 1927222988 2448 LRkaiADLEKEKS 2460
Cdd:pfam19220 376 LK---EELQRERA 385
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2301-2623 |
1.48e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2301 LNQQRALADKMLKEKMQAIQEASRLRAEAEMLqrqKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIA 2380
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSLHGKAELLTLRSQLL---TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2381 ESEKLKLQvSQLSEAQAKAQE---EAKKFKKQADSIASRLHETELAT-QEKMTVVEKLEVARLTSSKEADDLRKAIadLE 2456
Cdd:TIGR00618 252 QEEQLKKQ-QLLKQLRARIEElraQEAVLEETQERINRARKAAPLAAhIKAVTQIEQQAQRIHTELQSKMRSRAKL--LM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2457 KEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFE-EEVKKAKALKDEQE 2535
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQkLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2536 RQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEE-NQKLREKLQQLEeaqkdqpDKEVI 2614
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsAQSLKEREQQLQ-------TKEQI 481
|
....*....
gi 1927222988 2615 HVTMVETTK 2623
Cdd:TIGR00618 482 HLQETRKKA 490
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
36-154 |
1.64e-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: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 36 DGRKDERDRVQKKTFTKWVNK---------HLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKL 102
Cdd:cd21325 15 EGTQHSYSEEEKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQ 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 103 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQIN 154
Cdd:cd21325 95 ENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2020-2469 |
1.68e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.99 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2020 LDRLKKKAEEARkqkDDADK----EAEKQIlmaQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKlaKQAEA 2095
Cdd:PRK04778 81 LPDIEEQLFEAE---ELNDKfrfrKAKHEI---NEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKD--LYREL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2096 AKEKAERE------AALLRQQAEEAERQKaaaeqeaanqakaqEDAERLRKEAEFEAAK----RAQAENAALKQKqqada 2165
Cdd:PRK04778 153 RKSLLANRfsfgpaLDELEKQLENLEEEF--------------SQFVELTESGDYVEAReildQLEEELAALEQI----- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2166 eMAKHKKLAEQtLKQKFQVE--------QELTKVKLKLDETDkqksvLDEELQRLKDEVDDAVKQRGQ-----VEEELLK 2232
Cdd:PRK04778 214 -MEEIPELLKE-LQTELPDQlqelkagyRELVEEGYHLDHLD-----IEKEIQDLKEQIDENLALLEEldldeAEEKNEE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2233 VKVQMEELLKLkLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEdaarlsveaqEAARLRQ---IAEDDLNQQRALad 2309
Cdd:PRK04778 287 IQERIDQLYDI-LEREVKARKYVEKNSDTLPDFLEHAKEQNKELKE----------EIDRVKQsytLNESELESVRQL-- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2310 kmlKEKMQAIqeasrlraEAEMLQRQKDLA-QEQAQKLLEDKQlmqqrldeetEEYQKSLEaerkrqlEIIAESEKLKLQ 2388
Cdd:PRK04778 354 ---EKQLESL--------EKQYDEITERIAeQEIAYSELQEEL----------EEILKQLE-------EIEKEQEKLSEM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2389 VSQLSEAQAKAQEEAKKFKKQADSI-------------ASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADL 2455
Cdd:PRK04778 406 LQGLRKDELEAREKLERYRNKLHEIkryleksnlpglpEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDV 485
|
490
....*....|....
gi 1927222988 2456 EkeksRLKKEAEDL 2469
Cdd:PRK04778 486 E----TLEEETEEL 495
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1356-1518 |
1.74e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.77 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1356 EEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELK 1435
Cdd:pfam05262 179 DKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1436 NLSEQQIMdKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTaESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEE 1515
Cdd:pfam05262 259 NLPKPADT-SSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAK-DHKAFDLKQESKASEKEAEDKELEAQKKREPVAED 336
|
...
gi 1927222988 1516 TQK 1518
Cdd:pfam05262 337 LQK 339
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1656-1902 |
1.76e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 51.10 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1656 QAEEEAHKKSLAQE--DAEKQ---KEEAEREAKKRAKAEDSALKQKEMaeneleRQRKVAESTAQQKLTAEQELIRLRAD 1730
Cdd:PRK05035 440 AIEQEKKKAEEAKArfEARQArleREKAAREARHKKAAEARAAKDKDA------VAAALARVKAKKAAATQPIVIKAGAR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1731 FDNAE-----QQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEmdvliqlksKAEKETMSNSERskqllevEATKM 1805
Cdd:PRK05035 514 PDNSAviaarEARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAK---------KAAQQAANAEAE-------EEVDP 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1806 RDLAEEASKLRAIAeeAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQ 1885
Cdd:PRK05035 578 KKAAVAAAIARAKA--KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARA 655
|
250
....*....|....*..
gi 1927222988 1886 RKALEDQANQHKQQIEE 1902
Cdd:PRK05035 656 KARKAAQQQANAEPEEA 672
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2246-2414 |
1.80e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.72 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2246 RIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQiAEDDLNQQRaladkmlkeKMQAIQEASRL 2325
Cdd:pfam15709 354 RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQ-EEEERKQRL---------QLQAAQERARQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2326 RAEA---EMLQRQKDLAQEQAQKLLEDKqlmqQRLDEETEEyqksLEAERKRQLEiIAESEKLKLQvSQLSEAQAKAQEE 2402
Cdd:pfam15709 424 QQEEfrrKLQELQRKKQQEEAERAEAEK----QRQKELEMQ----LAEEQKRLME-MAEEERLEYQ-RQKQEAEEKARLE 493
|
170
....*....|..
gi 1927222988 2403 AKKFKKQADSIA 2414
Cdd:pfam15709 494 AEERRQKEEEAA 505
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2018-2608 |
1.86e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2018 DELDRLK--------------KKA----------EEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSvlAQQKEDt 2073
Cdd:PRK04863 390 EEVDELKsqladyqqaldvqqTRAiqyqqavqalERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLS--LEQKLS- 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2074 iMQTKLKEEYEKAKKLAKQA------EAAKEKA---EREAALLRQQAEEAErQKAAAEQEAANQAKAQEDAERLRKEAEF 2144
Cdd:PRK04863 467 -VAQAAHSQFEQAYQLVRKIagevsrSEAWDVArelLRRLREQRHLAEQLQ-QLRMRLSELEQRLRQQQRAERLLAEFCK 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2145 EAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSV---LDEELQRLKDEVDDAVK 2221
Cdd:PRK04863 545 RLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFE 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2222 QRGQVEEELLKVKVQMEELLKLKLRIEEENQRLiKKDKDNTQKFLAKEADNMKKLAED--AARLS-----VEAQEAA--- 2291
Cdd:PRK04863 625 DSQDVTEYMQQLLERERELTVERDELAARKQAL-DEEIERLSQPGGSEDPRLNALAERfgGVLLSeiyddVSLEDAPyfs 703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2292 ----RLRQ-IAEDDLNQ-QRALA------------------------DKMLKEKMQAIQEA------SRLRAE------- 2328
Cdd:PRK04863 704 alygPARHaIVVPDLSDaAEQLAgledcpedlyliegdpdsfddsvfSVEELEKAVVVKIAdrqwrySRFPEVplfgraa 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2329 ----AEMLQRQKDLAQEQAQKLLEDKQLMqQRLDEETEEY-------------QKSLEAERKRQLEIIAESEKLKLQVSQ 2391
Cdd:PRK04863 784 rekrIEQLRAEREELAERYATLSFDVQKL-QRLHQAFSRFigshlavafeadpEAELRQLNRRRVELERALADHESQEQQ 862
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2392 LSEAQAKAQEEAKKFKKQADSIAsrLHETELATQEKMTVVEKLEVArltsSKEADDLR---KAIADLEKEKSRLKKEAED 2468
Cdd:PRK04863 863 QRSQLEQAKEGLSALNRLLPRLN--LLADETLADRVEEIREQLDEA----EEAKRFVQqhgNALAQLEPIVSVLQSDPEQ 936
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2469 LQNKSKEMADAQQKQieheKTVLQQTF-LSE-------------KEMLLKKEKLIEEEKKRLEsQFEEEVKKAKalkdEQ 2534
Cdd:PRK04863 937 FEQLKQDYQQAQQTQ----RDAKQQAFaLTEvvqrrahfsyedaAEMLAKNSDLNEKLRQRLE-QAEQERTRAR----EQ 1007
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2535 ERQKQQMEDEKKKLQATMDAALNKQKEAEKEMhnkQKEMKEL---------ERKRLEQERIlaeeNQKLREKLQQLEEAQ 2605
Cdd:PRK04863 1008 LRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL---KQELQDLgvpadsgaeERARARRDEL----HARLSANRSRRNQLE 1080
|
...
gi 1927222988 2606 KDQ 2608
Cdd:PRK04863 1081 KQL 1083
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1253-1718 |
1.88e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1253 LKEQLAQEKKLLEEVEGNKDKVDecqkyakayIDTIKDYELQLVAYKAQVEPLASPLKK-TKLDSASDNIIQEYVTLRTK 1331
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELN---------LKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1332 YSELMTLTSQY--IKFITDSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHakaiAKAEKEAQELKLRMQEE 1409
Cdd:COG4717 118 LEKLEKLLQLLplYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ----EELEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1410 VNRREDAVVDAEKQKHNIQLELHELknlsEQQIMDKSKQVDDALQSRVKIEEEIRL----IRLQLETTVKQKSTAESELK 1485
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEA----QEELEELEEELEQLENELEAAALEERLkearLLLLIAAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1486 QLRDRAAEA---------------EKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENL 1550
Cdd:COG4717 270 SLILTIAGVlflvlgllallflllAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1551 K---RQAEEAERQVKQAEIEKERQIQVAHVAAQK----SAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQL--QHEAAA 1621
Cdd:COG4717 350 QellREAEELEEELQLEELEQEIAALLAEAGVEDeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELleALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1622 LKKQQEDAERAREEAEKELEKWRQKANEaLRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAedsalkqkEMAEN 1701
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAE-LEAELEQLEEDGELAELLQELEELKAELRELAEEWAAL--------KLALE 500
|
490
....*....|....*..
gi 1927222988 1702 ELERQRKVAESTAQQKL 1718
Cdd:COG4717 501 LLEEAREEYREERLPPV 517
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1350-1526 |
1.96e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1350 QRRLEDEEKaaEKLKAEEQKKMAMMQA--ELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDavvDAEKQKHNI 1427
Cdd:PRK09510 100 QERLKQLEK--ERLAAQEQKKQAEEAAkqAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAA---EAKKKAEAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1428 QLELHELKNLSEQQIMDKSKQVDDAlqsRVKIEEEirlirlqlettVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEK 1507
Cdd:PRK09510 175 AAKKAAAEAKKKAEAEAAAKAAAEA---KKKAEAE-----------AKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEK 240
|
170
....*....|....*....
gi 1927222988 1508 LRKQVNEETQKKRMAEEEL 1526
Cdd:PRK09510 241 AAAAKAAEKAAAAKAAAEV 259
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
41-149 |
1.99e-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: 46.90 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 41 ERDRVQKKTFTKWVNKHLIKSQrqVTDLYEDLRDGHNLISLLEV---------LSGETLPREKGRMRfhKLQNVQIALDF 111
Cdd:cd21329 2 EGESSEERTFRNWMNSLGVNPY--VNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1927222988 112 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1467-1718 |
2.06e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 50.36 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1467 RLQLETTVKQKST---AESELKQLRDRAAEAEKLRKAAqeeaekLRKQVNEETQKkrMAEEELKRKAEAEKEAAKQKQKA 1543
Cdd:PRK07735 36 KLEEENREKEKALpknDDMTIEEAKRRAAAAAKAKAAA------LAKQKREGTEE--VTEEEKAKAKAKAAAAAKAKAAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1544 LedlenlKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALK 1623
Cdd:PRK07735 108 L------AKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1624 KQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKK-SLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENE 1702
Cdd:PRK07735 182 KQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKaSQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTKGAEGK 261
|
250
....*....|....*.
gi 1927222988 1703 LERQRKVAESTAQQKL 1718
Cdd:PRK07735 262 KEEEPKQEEPSVNQPY 277
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1469-1892 |
2.11e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.68 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1469 QLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLE 1548
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1549 NLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQED 1628
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1629 AERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRK 1708
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1709 VAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDElyrlkNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETM 1788
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAE-----AVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELA 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1789 SNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEK 1868
Cdd:COG5278 426 EALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALAL 505
|
410 420
....*....|....*....|....
gi 1927222988 1869 EAENERLRRQAEDEAYQRKALEDQ 1892
Cdd:COG5278 506 AALLLAAAEAALAAALAAALASAE 529
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2308-2605 |
2.24e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2308 ADKMLKEKMQAIQEASRLRAEAEMLQRQkDLAQEQAQKLLEDKQLMQQRLDEET--EEYQKSLEAERKRQ---LEIIAES 2382
Cdd:COG3206 66 SDVLLSGLSSLSASDSPLETQIEILKSR-PVLERVVDKLNLDEDPLGEEASREAaiERLRKNLTVEPVKGsnvIEISYTS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2383 E-----KLKLQ------VSQLSEAQAKAQEEAKKF-KKQADSIASRLHETELAtqekmtvVEKLEVAR--LTSSKEADDL 2448
Cdd:COG3206 145 PdpelaAAVANalaeayLEQNLELRREEARKALEFlEEQLPELRKELEEAEAA-------LEEFRQKNglVDLSEEAKLL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2449 RKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEkemLLKKEKLIEEEKKRLESQFEEEVKKAK 2528
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSARYTPNHPDVI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2529 ALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMK---------ELERKRLEQERILAEEN-QKLREKL 2598
Cdd:COG3206 295 ALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEarlaelpelEAELRRLEREVEVARELyESLLQRL 374
|
....*..
gi 1927222988 2599 QQLEEAQ 2605
Cdd:COG3206 375 EEARLAE 381
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1790-2141 |
2.25e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1790 NSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEA-EIALKEK 1868
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEyEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1869 EAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRaivddtlkqrrvvEEEIRILKLNFEKAss 1948
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEER-------------EEDERILEYLKEKA-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1949 GKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALeeekrrreaeekvkkiaaaeeeaarqrqaaqDELDRLKKKAE 2028
Cdd:pfam13868 166 EREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAER-------------------------------DELRAKLYQEE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2029 EARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIM--QTKLKEEYEKAKKLAKQAEAAKEKAEREAAL 2106
Cdd:pfam13868 215 QERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEefERMLRKQAEDEEIEQEEAEKRRMKRLEHRRE 294
|
330 340 350
....*....|....*....|....*....|....*
gi 1927222988 2107 LRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKE 2141
Cdd:pfam13868 295 LEKQIEEREEQRAAEREEELEEGERLREEEAERRE 329
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2023-2366 |
2.33e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 50.78 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2023 LKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQ----QKEDTIMQTKLKEEYEKAKKLAKQAEAA-- 2096
Cdd:NF033838 144 ATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAElelvKEEAKEPRDEEKIKQAKAKVESKKAEATrl 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2097 -KEKAEREAAllrqqAEEAERQKAAAEQEAANQAKAQEDAERLRKEaefeaAKRAQAENAALKQKQQADAEmAKHKKLAE 2175
Cdd:NF033838 224 eKIKTDREKA-----EEEAKRRADAKLKEAVEKNVATSEQDKPKRR-----AKRGVLGEPATPDKKENDAK-SSDSSVGE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2176 QTLKQ-KFQVEQELTKVKLKLDETDKQKSVLDEELQRlkdevDDAVKQRGQVEEELLKVKVQMEElLKLKLRIEEenqrl 2254
Cdd:NF033838 293 ETLPSpSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRR-----NYPTNTYKTLELEIAESDVKVKE-AELELVKEE----- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2255 ikkdkdntqkflAKEADNMKKLAEDAARLSVEAQEAARLRQI------AEDDLNQQRALADKMLKEKMQAIQEASRLRAE 2328
Cdd:NF033838 362 ------------AKEPRNEEKIKQAKAKVESKKAEATRLEKIktdrkkAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPE 429
|
330 340 350
....*....|....*....|....*....|....*...
gi 1927222988 2329 AEMLQRQKDLAQEQAQKlLEDKQLMQQRLDEETEEYQK 2366
Cdd:NF033838 430 KPAPKPEKPAEQPKAEK-PADQQAEEDYARRSEEEYNR 466
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2046-2292 |
2.44e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2046 LMAQQAAQKCSAAEQQVQSVLAQQKEdtimqtkLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAaaeQEA 2125
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAE-------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA---ALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2126 ANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQkfqveqeLTKVKLKLDETDKQKSVL 2205
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR-------LQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2206 DEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLiKKDKDNTQKFLAKEADNMKKLAEDAARLSV 2285
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL-EKELAELAAELAELQQEAEELEALIARLEA 234
|
....*..
gi 1927222988 2286 EAQEAAR 2292
Cdd:COG4942 235 EAAAAAE 241
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1428-1788 |
2.45e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1428 QLELHELKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRaaeaeklRKAAQEEAEK 1507
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE-------LEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1508 LRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAEL 1587
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1588 QSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLA 1667
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1668 QEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYR 1747
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1927222988 1748 LKNEVVAAQQQ---RKQLEDELAKVRSEMDVLIQLKSKAEKETM 1788
Cdd:COG4372 325 AKKLELALAILlaeLADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2079-2411 |
2.52e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2079 LKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEaefEAAKRAQAENAALK 2158
Cdd:pfam13868 1 LRENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEK---EEERKEERKRYRQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2159 QKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKL----KLDETDKQKSVLDEELQRLKDEVDDAV-KQRGQVEEELLKV 2233
Cdd:pfam13868 78 LEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEedqaEAEEKLEKQRQLREEIDEFNEEQAEWKeLEKEEEREEDERI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2234 KVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEdaarlsveaQEAARLRQIAEDdlnQQRALADKMLK 2313
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAE---------RDELRAKLYQEE---QERKERQKERE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2314 EKMQAIQEASRLRAE-AEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQL 2392
Cdd:pfam13868 226 EAEKKARQRQELQQArEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQ 305
|
330
....*....|....*....
gi 1927222988 2393 SEAQAKAQEEAKKFKKQAD 2411
Cdd:pfam13868 306 RAAEREEELEEGERLREEE 324
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4128-4156 |
2.57e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.57e-05
10 20
....*....|....*....|....*....
gi 1927222988 4128 VRKRRVVIVDPETGKEMTVYEAYRKGLID 4156
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2729-2762 |
2.57e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.57e-05
10 20 30
....*....|....*....|....*....|....
gi 1927222988 2729 LLEAQAATGSILDPIKNQKLSVNEAVKEGVIGPE 2762
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1826-2065 |
3.25e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1826 RQVAEEEAARQRAEAERILKEklaAISDATRLKTEAEIALKEkeaENERLRRQAEDEAYQRKA----LEDQANQHKQQIE 1901
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEE---AKKEAEAIKKEALLEAKE---EIHKLRNEFEKELRERRNelqkLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1902 EKIVLLKKSsEAEMERQRAIVDDTLKQRRVVEEEIRILKLNfekassgkldlelELNKLKNIA----EETQQSKL-RAEE 1976
Cdd:PRK12704 100 RKLELLEKR-EEELEKKEKELEQKQQELEKKEEELEELIEE-------------QLQELERISgltaEEAKEILLeKVEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1977 EAEKlrklaleeekrrreaeekvkkiaaaeeeaarqrqaaqdELDRLKKKAEEarKQKDDADKEAEKQILmaqQAAQKCS 2056
Cdd:PRK12704 166 EARH--------------------------------------EAAVLIKEIEE--EAKEEADKKAKEILA---QAIQRCA 202
|
250
....*....|..
gi 1927222988 2057 ---AAEQQVQSV 2065
Cdd:PRK12704 203 adhVAETTVSVV 214
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1547-1720 |
3.45e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.87 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1547 LENL-KRQAEE--AERQVKQAEIEKERQIQVAhVAAQKSAAAELQSKhmsfvektskleeslkQEHGAVLQLQHEAAALK 1623
Cdd:COG2268 186 LDALgRRKIAEiiRDARIAEAEAERETEIAIA-QANREAEEAELEQE----------------REIETARIAEAEAELAK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1624 KQQEDAERARE---EAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAE 1700
Cdd:COG2268 249 KKAEERREAETaraEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE 328
|
170 180
....*....|....*....|
gi 1927222988 1701 NELERQRKVAESTAQQKLTA 1720
Cdd:COG2268 329 AEAIRAKGLAEAEGKRALAE 348
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2444-2612 |
3.99e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.95 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2444 EADDLRKAIADLEKEKS--------RLKKEAEDLQNKSKEMADA---QQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEE 2512
Cdd:pfam15709 317 EEDPSKALLEKREQEKAsrdrlraeRAEMRRLEVERKRREQEEQrrlQQEQLERAEKMREELELEQQRRFEEIRLRKQRL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2513 KKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAalNKQKEAEKEMHNKQKEmKELERKRLEQERILAE--E 2590
Cdd:pfam15709 397 EEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRK--KQQEEAERAEAEKQRQ-KELEMQLAEEQKRLMEmaE 473
|
170 180
....*....|....*....|..
gi 1927222988 2591 NQKLREKLQQLEEAQKDQPDKE 2612
Cdd:pfam15709 474 EERLEYQRQKQEAEEKARLEAE 495
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2318-2608 |
4.34e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.48 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2318 AIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLE----AERKRQLEIIAESEKLKLQVSQLS 2393
Cdd:pfam02029 15 AREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDrtakREERRQKRLQEALERQKEFDPTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2394 EA-------QAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEK----LEVARLTSSKEADDLRKAIADLEKEKSRL 2462
Cdd:pfam02029 95 DEkesvaerKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQenkwSTEVRQAEEEGEEEEDKSEEAEEVPTENF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2463 KKEAEDLQNKSKEMADA-------QQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQE 2535
Cdd:pfam02029 175 AKEEVKDEKIKKEKKVKyeskvflDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2536 RQKQQMEDEK-KKLQatmdaalNKQKEAEKEMHNKQKEMK---------ELERKRLEQERILAEENQKLREKLQ----QL 2601
Cdd:pfam02029 255 RRRQEKESEEfEKLR-------QKQQEAELELEELKKKREerrklleeeEQRRKQEEAERKLREEEEKRRMKEEierrRA 327
|
....*..
gi 1927222988 2602 EEAQKDQ 2608
Cdd:pfam02029 328 EAAEKRQ 334
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2073-2335 |
4.62e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2073 TIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAAlLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQA 2152
Cdd:PRK05035 440 AIEQEKKKAEEAKARFEARQARLEREKAAREAR-HKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSA 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2153 ENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAV-----KQRGQVE 2227
Cdd:PRK05035 519 VIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIarakaKKAAQQA 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2228 EELLKVKVQMEELLKlKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARlsveAQEAARLRQIAEDDLNQQRAL 2307
Cdd:PRK05035 599 ASAEPEEQVAEVDPK-KAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI----ARAKARKAAQQQANAEPEEAE 673
|
250 260
....*....|....*....|....*...
gi 1927222988 2308 ADKmlKEKMqaiqEASRLRAEAEMLQRQ 2335
Cdd:PRK05035 674 DPK--KAAV----AAAIARAKAKKAAQQ 695
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
47-112 |
4.80e-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: 45.34 E-value: 4.80e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 47 KKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPREK----GRMRFHKLQNVQIALDFL 112
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1159-1897 |
4.84e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1159 EAELKKATAVSDKMSRVHSERDAELDHYRQLLSSLQDRWKAVFSQIDLRQRELEQLGRQLGYYREsydwlirwindAKQR 1238
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQ-----------AVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1239 QEKIQAV------TITDSKTLKEQL-AQEKKLLEEVEGNKDKVDECQKyAKAYIDtiKDYELqlvaykaqVEPLASPLKK 1311
Cdd:COG3096 422 LEKARALcglpdlTPENAEDYLAAFrAKEQQATEEVLELEQKLSVADA-ARRQFE--KAYEL--------VCKIAGEVER 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1312 TKLDSASDNIIQEYVTLRTKYSELMTLTSQYikfiTDSQRRLEdEEKAAEKLKAEEQKKMAmmqAELDKQKQLAEVHAKA 1391
Cdd:COG3096 491 SQAWQTARELLRRYRSQQALAQRLQQLRAQL----AELEQRLR-QQQNAERLLEEFCQRIG---QQLDAAEELEELLAEL 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1392 IAKAE------KEAQELKLRMQ---EEVNRREDAVVDAEKQKHNIQLELHELKNLSEQQIMDkSKQVDDALQSRVKIE-- 1460
Cdd:COG3096 563 EAQLEeleeqaAEAVEQRSELRqqlEQLRARIKELAARAPAWLAAQDALERLREQSGEALAD-SQEVTAAMQQLLEREre 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1461 -----EEIRLIRLQLETTVKQKSTA----ESELKQLRDR-----------------AAEAEKLR------------KAAQ 1502
Cdd:COG3096 642 atverDELAARKQALESQIERLSQPggaeDPRLLALAERlggvllseiyddvtledAPYFSALYgparhaivvpdlSAVK 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1503 E---------------------------EAEKLRKQV---NEETQKK-----------RMAEEelKRkaeaekeaakqkq 1541
Cdd:COG3096 722 EqlagledcpedlyliegdpdsfddsvfDAEELEDAVvvkLSDRQWRysrfpevplfgRAARE--KR------------- 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1542 kaledLENLKRQAEEAERQVKQAEIEKERQIQVAH-----------VAAQKSAAAELQSKHmsfvEKTSKLEESLKQEHG 1610
Cdd:COG3096 787 -----LEELRAERDELAEQYAKASFDVQKLQRLHQafsqfvgghlaVAFAPDPEAELAALR----QRRSELERELAQHRA 857
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1611 AVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEA------HKKSLAQED-------AEKQKEE 1677
Cdd:COG3096 858 QEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAqafiqqHGKALAQLEplvavlqSDPEQFE 937
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1678 AEREAKKRAKAEDSALKQKEMAENELeRQRKV--AESTAQQKLTAEQELI-RLRADFDNAEQQRSLLEDelyrlknevvA 1754
Cdd:COG3096 938 QLQADYLQAKEQQRRLKQQIFALSEV-VQRRPhfSYEDAVGLLGENSDLNeKLRARLEQAEEARREARE----------Q 1006
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1755 AQQQRKQLEDELAkvrsemdVLIQLKSKAEketmsnserskqlleveaTKMRDLAEEASKLRAIAEEAKHQrqvAEEEAA 1834
Cdd:COG3096 1007 LRQAQAQYSQYNQ-------VLASLKSSRD------------------AKQQTLQELEQELEELGVQADAE---AEERAR 1058
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 1835 RQRAEaeriLKEKLAAiSDATRLKTEAEIALKEKEAEN--ERLRRQAEDEAYQRKaledQANQHK 1897
Cdd:COG3096 1059 IRRDE----LHEELSQ-NRSRRSQLEKQLTRCEAEMDSlqKRLRKAERDYKQERE----QVVQAK 1114
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1350-1506 |
5.68e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.10 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1350 QRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKA------IAKAEKEAQELKLRMQEEVNRREdAVVDAEkq 1423
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReietarIAEAEAELAKKKAEERREAETAR-AEAEAA-- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1424 khniqlelhelknLSEQQImdkskqvddalQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDR--AAEAEKLRKAA 1501
Cdd:COG2268 268 -------------YEIAEA-----------NAEREVQRQLEIAEREREIELQEKEAEREEAELEADVrkPAEAEKQAAEA 323
|
....*
gi 1927222988 1502 QEEAE 1506
Cdd:COG2268 324 EAEAE 328
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2237-2428 |
5.80e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2237 MEELLKLKLRIEEENQRL--IKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKmLKE 2314
Cdd:COG1579 2 MPEDLRALLDLQELDSELdrLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2315 KMQAIQEASrlraEAEMLQRQKDlAQEQAQKLLEDKQLmqqRLDEETEEYQKSLEAERKRQLEIIAESEKLKlqvSQLSE 2394
Cdd:COG1579 81 QLGNVRNNK----EYEALQKEIE-SLKRRISDLEDEIL---ELMERIEELEEELAELEAELAELEAELEEKK---AELDE 149
|
170 180 190
....*....|....*....|....*....|....
gi 1927222988 2395 AQAKAQEEAKKFKKQADSIASRLHETELATQEKM 2428
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKIPPELLALYERI 183
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2076-2181 |
6.22e-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: 46.32 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2076 QTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEE--AERQKAAAEQEAANQAKAQEDAERLRKEAEfeaAKRAQAE 2153
Cdd:COG0711 33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEiiAEARKEAEAIAEEAKAEAEAEAERIIAQAE---AEIEQER 109
|
90 100
....*....|....*....|....*...
gi 1927222988 2154 NAALKQKQQADAEMAkhKKLAEQTLKQK 2181
Cdd:COG0711 110 AKALAELRAEVADLA--VAIAEKILGKE 135
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1127-1301 |
6.24e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 47.44 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1127 VPNDVKEVETYRTKLKKMRAEAEGEQPVFDSLEAElkkatavSDKMSRVHSERDAELdhyRQLLSSLQDRWKAVFSQIDL 1206
Cdd:cd00176 28 YGDDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHPDAEEI---QERLEELNQRWEELRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1207 RQRELEQLGRQLGYYRESYDwLIRWINDAKQRQEKIQavTITDSKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYID 1286
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLE 174
|
170
....*....|....*
gi 1927222988 1287 TIKDYELQLVAYKAQ 1301
Cdd:cd00176 175 EGHPDADEEIEEKLE 189
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
46-153 |
6.29e-05 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 46.16 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 46 QKKTFTKWVNK---------HLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 112
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1927222988 113 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQI 153
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1754-1927 |
6.36e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 49.25 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1754 AAQQQRKQLEDElAKVRSEmdvLIQLKSKAEKEtmsnsERSKQLLEVEAtkmRDLAEEAS-KLRAIAEeakhqrqvAEEE 1832
Cdd:PTZ00491 667 AARHQAELLEQE-ARGRLE---RQKMHDKAKAE-----EQRTKLLELQA---ESAAVESSgQSRAEAL--------AEAE 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1833 AARQRAEAErilkeklaaiSDATRLKTEAEIALKEKEAENERLRRQAEdeayqrkaledqANQHKQQIEEKIVLLKKSSE 1912
Cdd:PTZ00491 727 ARLIEAEAE----------VEQAELRAKALRIEAEAELEKLRKRQELE------------LEYEQAQNELEIAKAKELAD 784
|
170
....*....|....*....
gi 1927222988 1913 AEMERQRAIVD----DTLK 1927
Cdd:PTZ00491 785 IEATKFERIVEalgrETLI 803
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2024-2475 |
6.83e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.88 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2024 KKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAERE 2103
Cdd:COG3064 26 RAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2104 AALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQ 2183
Cdd:COG3064 106 AAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2184 VEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQ 2263
Cdd:COG3064 186 AAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2264 KFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADkmlkekmqAIQEASRLRAEAEMLQRQKDLAQEQA 2343
Cdd:COG3064 266 AAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAV--------AAEEAVLAAAAAAGALVVRGGGAASL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2344 QKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELA 2423
Cdd:COG3064 338 EAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASA 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 2424 TQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKE 2475
Cdd:COG3064 418 VELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAV 469
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2056-2202 |
7.05e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.30 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2056 SAAEQQVQSvLAQQKEDTImqtklKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEaanqaKAQEDA 2135
Cdd:TIGR02794 46 GAVAQQANR-IQQQKKPAA-----KKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAE-----QAAKQA 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222988 2136 ERLRKEAEfEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVE--QELTKVKLKLDETDKQK 2202
Cdd:TIGR02794 115 EEKQKQAE-EAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEakKKAEEAKKKAEAEAKAK 182
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1712-1864 |
7.40e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 49.25 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1712 STAQQKLTAEQELIRLradfdnaEQQ-RSLLEdeLYRLKNEVVAAQQQRK--QLEDELAKVRSemdvliQLKSKAEKETM 1788
Cdd:PTZ00491 660 TTKSQEAAARHQAELL-------EQEaRGRLE--RQKMHDKAKAEEQRTKllELQAESAAVES------SGQSRAEALAE 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1789 SNSERSKQLLEVEATKMRDLAE------EASKLRAIAE-EAKHQRQVAEEEAARQRAEAErILKEKLAAISDATRLKTEA 1861
Cdd:PTZ00491 725 AEARLIEAEAEVEQAELRAKALrieaeaELEKLRKRQElELEYEQAQNELEIAKAKELAD-IEATKFERIVEALGRETLI 803
|
...
gi 1927222988 1862 EIA 1864
Cdd:PTZ00491 804 AIA 806
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2025-2361 |
7.73e-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: 48.49 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2025 KKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREA 2104
Cdd:pfam15558 18 KEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2105 ALLRQQaeEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAEnaalkQKQQADAEMAKHKK-LAEQTLKQKFQ 2183
Cdd:pfam15558 98 EQAEDQ--ENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNS-----LQLQERLEEACHKRqLKEREEQKKVQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2184 VE--QELTKVKLKLDETDKQkSVLDEELQRLKDEVDDAVKQ---RGQVEEEL--LKVKVQMEE--LLKLKLRIEEENQRl 2254
Cdd:pfam15558 171 ENnlSELLNHQARKVLVDCQ-AKAEELLRRLSLEQSLQRSQenyEQLVEERHreLREKAQKEEeqFQRAKWRAEEKEEE- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2255 ikkdKDNTQKFLAKEADNMKKLAEDAARLSVEaQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQE----ASRLRAEAE 2330
Cdd:pfam15558 249 ----RQEHKEALAELADRKIQQARQVAHKTVQ-DKAQRARELNLEREKNHHILKLKVEKEEKCHREGikeaIKKKEQRSE 323
|
330 340 350
....*....|....*....|....*....|.
gi 1927222988 2331 MLQRQKDLAQEQAQKLLEDKQLMQQRLDEET 2361
Cdd:pfam15558 324 QISREKEATLEEARKTARASFHMREKVREET 354
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1665-1918 |
8.26e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.99 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1665 SLAQEDAEKQKEEAEREAKKRAKAEdsalKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADfdnAEQQRSLLEDE 1744
Cdd:pfam00038 22 FLEQQNKLLETKISELRQKKGAEPS----RLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLA---AEDFRQKYEDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1745 LyRLKNEVVAA-QQQRKQLEDE-LAKVRSEMDV------LIQLKSKAE---KETMSNSERSKQLLEVEATKMRDLAeeas 1813
Cdd:pfam00038 95 L-NLRTSAENDlVGLRKDLDEAtLARVDLEAKIeslkeeLAFLKKNHEeevRELQAQVSDTQVNVEMDAARKLDLT---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1814 klRAIAEeakhQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERL--RRQAEDEAY--QRKAL 1889
Cdd:pfam00038 170 --SALAE----IRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTiqSLEIELQSLkkQKASL 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1927222988 1890 EDQ--------ANQHKQ------QIEEKIVLLKksseAEMERQ 1918
Cdd:pfam00038 244 ERQlaeteeryELQLADyqelisELEAELQETR----QEMARQ 282
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2018-2479 |
8.37e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.97 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2018 DELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAK 2097
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2098 EKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQE---DAERLRKEAEFEAAKRAQ--AENAALKQKQQADAEMAKHKK 2172
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSslaEAEQRIKELEFEIQSQEQdsEIVKNSKSELARIPELEKELE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2173 ------------------LAEQT--LKQKFQ-----------VEQELTKVKLKLDETDK--QKSVLD-----------EE 2208
Cdd:pfam05557 208 rlrehnkhlnenienkllLKEEVedLKRKLEreekyreeaatLELEKEKLEQELQSWVKlaQDTGLNlrspedlsrriEQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2209 LQR----LKDEVDDAV-------KQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKdkdntQKFLAKEADNMKKL- 2276
Cdd:pfam05557 288 LQQreivLKEENSSLTssarqleKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRR-----VLLLTKERDGYRAIl 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2277 ---------AEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQ------- 2340
Cdd:pfam05557 363 esydkeltmSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADpsyskee 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2341 -EQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHE 2419
Cdd:pfam05557 443 vDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKK 522
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2420 TELATQEKMTVVEKlevARLTSSKEADDLRKAIADLEKEKSRLKkeaEDLQNKSKEMADA 2479
Cdd:pfam05557 523 LEDDLEQVLRLPET---TSTMNFKEVLDLRKELESAELKNQRLK---EVFQAKIQEFRDV 576
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2013-2152 |
8.61e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.46 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2013 RQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSvlAQQKEDTIMQTKLKEEYEKAKKLAKQ 2092
Cdd:pfam05262 215 AQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADT--SSPKEDKQVAENQKREIEKAQIEIKK 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 2093 AEAAKEKAEREAA--LLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQA 2152
Cdd:pfam05262 293 NDEEALKAKDHKAfdLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNED 354
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1730-1882 |
8.66e-05 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 48.77 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1730 DFDNAEQQRSLlEDELYRLKNEVVAAQQQ-----RKQLEDELAKVRSE-MDVLIqLKSKAEKEtmsnsERSKQLLEVEAt 1803
Cdd:pfam04147 120 DFDDDDDDDSE-EEEDGQLDLKRVRRAHFgggedDEEEEPERKKSKKEvMEEVI-AKSKLHKY-----ERQKAKEEDEE- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1804 kMR-----DLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAE--RILKE----KLAAISDatRLKTEAEIALKEKE--- 1869
Cdd:pfam04147 192 -LReeldkELKDLRSLLSGSKRPKPEQAKKPEEKPDRKKPDDDydKLVRElafdKRAKPSD--RTKTEEELAEEEKErle 268
|
170
....*....|....*
gi 1927222988 1870 -AENERLRR-QAEDE 1882
Cdd:pfam04147 269 kLEEERLRRmRGEED 283
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1750-1871 |
8.73e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.05 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1750 NEVVAA-QQQRKQLEDELAKVRSemdvliqLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQ--R 1826
Cdd:PRK00409 519 NELIASlEELERELEQKAEEAEA-------LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiiK 591
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1927222988 1827 QVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAE 1871
Cdd:PRK00409 592 ELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3995-4026 |
8.75e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 8.75e-05
10 20 30
....*....|....*....|....*....|..
gi 1927222988 3995 KLLSAERAVTGYRDPYSGKTISLFQAMKKGLI 4026
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2024-2304 |
9.09e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2024 KKKAEEARKQKDDADKEAEKQILMAQQAA----QKCSAAEQQVQSVLAQQKE-----DTIMQTKLKEEYEKAKKLAKQAE 2094
Cdd:pfam17380 306 EEKAREVERRRKLEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEErkrelERIRQEEIAMEISRMRELERLQM 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2095 AAKEKAER-----EAALlRQQAEEAERQKAAAEQ-----------EAANqakaQEDAERLRKEAEFEAAKRAQAEnaaLK 2158
Cdd:pfam17380 386 ERQQKNERvrqelEAAR-KVKILEEERQRKIQQQkvemeqiraeqEEAR----QREVRRLEEERAREMERVRLEE---QE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2159 QKQQAdaemakhkklaeQTLKQKfqvEQELTKVKLKLDEtDKQKSVLDEELQRLKDEVDDAVKQRGQVEEElLKVKVQME 2238
Cdd:pfam17380 458 RQQQV------------ERLRQQ---EEERKRKKLELEK-EKRDRKRAEEQRRKILEKELEERKQAMIEEE-RKRKLLEK 520
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222988 2239 ELLKLKLRIEEENQRLIKKDKDNTQKFLAKE---ADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQ 2304
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERRKQQEMEERrriQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1349-1527 |
9.62e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1349 SQRRLEDEEKAAEKLKAEEQKKmammqAELDKQKQLAEvhakaiakAEKEAQELKLRMQEEVNRREDavvdaekqkhniq 1428
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKE-----AEAIKKEALLE--------AKEEIHKLRNEFEKELRERRN------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1429 lelhELKNLsEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRaaEAEKLRKAA---QEEA 1505
Cdd:PRK12704 83 ----ELQKL-EKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE--QLQELERISgltAEEA 155
|
170 180
....*....|....*....|....*...
gi 1927222988 1506 -EKLRKQVNEETQKKRMA-----EEELK 1527
Cdd:PRK12704 156 kEILLEKVEEEARHEAAVlikeiEEEAK 183
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1466-1814 |
9.68e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.75 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1466 IRLQLETTVKQKSTAESE--LKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKqkqka 1543
Cdd:PRK11281 41 VQAQLDALNKQKLLEAEDklVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETR----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1544 lEDLENLK-RQAEE--AERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLK--QEHGAVL----- 1613
Cdd:PRK11281 116 -ETLSTLSlRQLESrlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKggKVGGKALrpsqr 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1614 -QLQHEAAALKKQ---QEDAERAREEAEKELEKWRQKANEALRlRLQAE-----EEAHKKSLAQedAEKQKEEAErEAKK 1684
Cdd:PRK11281 195 vLLQAEQALLNAQndlQRKSLEGNTQLQDLLQKQRDYLTARIQ-RLEHQlqllqEAINSKRLTL--SEKTVQEAQ-SQDE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1685 RAKAEDSALKQKEMAENELERQRKVAESTAQQKLTaeQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAA----QQQR- 1759
Cdd:PRK11281 271 AARIQANPLVAQELEINLQLSQRLLKATEKLNTLT--QQNLRVKNWLDRLTQSERNIKEQISVLKGSLLLSrilyQQQQa 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 1760 -------KQLEDELAKVRSEM-------DVLIQLKS------KAEKETMSNSERsKQLLEVEATKmRDLAEEASK 1814
Cdd:PRK11281 349 lpsadliEGLADRIADLRLEQfeinqqrDALFQPDAyidkleAGHKSEVTDEVR-DALLQLLDER-RELLDQLNK 421
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1575-1795 |
9.77e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1575 AHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQK--ANEALR 1652
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1653 LRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMA---------ENELERQRKVAESTAQQKLTAEQE 1723
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaparREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 1724 LIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSK 1795
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1475-1747 |
1.02e-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: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1475 KQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVneetQKKRMAEEelkrkaeaekeaakqkqkaledlenlKRQA 1554
Cdd:TIGR02794 58 QKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELE----QRAAAEKA--------------------------AKQA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1555 EEAerqvKQAEIEKERQiqvAHVAAQKSAAaelqskhmsfvEKTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERARE 1634
Cdd:TIGR02794 108 EQA----AKQAEEKQKQ---AEEAKAKQAA-----------EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1635 EAEKELEKWRQKANEALRlRLQAEEEAHKKSLAQEDAE---KQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAE 1711
Cdd:TIGR02794 170 EAKKKAEAEAKAKAEAEA-KAKAEEAKAKAEAAKAKAAaeaAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
|
250 260 270
....*....|....*....|....*....|....*.
gi 1927222988 1712 STAQQKLTAEQELIRLRADFDNAEQQRsLLEDELYR 1747
Cdd:TIGR02794 249 QGGARGAAAGSEVDKYAAIIQQAIQQN-LYDDPSFR 283
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1792-2030 |
1.03e-04 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 48.60 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1792 ERSKQLLEVEATKM----RDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDAtrlKTEAEIALKE 1867
Cdd:COG1193 503 ERARELLGEESIDVekliEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKA---REEAEEILRE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1868 KEAENERLRRQAEdeayQRKALEDQANQHKQQIEEkivlLKKSSEAEMERQRAIVDDTLKQRRVVE-EEIRILKLNfeka 1946
Cdd:COG1193 580 ARKEAEELIRELR----EAQAEEEELKEARKKLEE----LKQELEEKLEKPKKKAKPAKPPEELKVgDRVRVLSLG---- 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1947 SSGKLdleLELNKLKNIaeETQQSKLRAEEEAEKLRKLAleeekrrREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKK 2026
Cdd:COG1193 648 QKGEV---LEIPKGGEA--EVQVGILKMTVKLSDLEKVE-------KKKPKKPKKRPAGVSVSVSKASTVSPELDLRGMR 715
|
....
gi 1927222988 2027 AEEA 2030
Cdd:COG1193 716 VEEA 719
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2049-2175 |
1.05e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 48.86 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2049 QQAAQKCSAAEQQVQSVLAQQKedtiMQTKLKEEYEKAKKLAKQAEA----------AKEKAEREAALLRQQAE-EAERQ 2117
Cdd:PTZ00491 666 AAARHQAELLEQEARGRLERQK----MHDKAKAEEQRTKLLELQAESaavessgqsrAEALAEAEARLIEAEAEvEQAEL 741
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 2118 KAAaeqeaanqakaqedAERLRKEAEFEaAKRAQAENAALKQKQQADAEMAKHKKLAE 2175
Cdd:PTZ00491 742 RAK--------------ALRIEAEAELE-KLRKRQELELEYEQAQNELEIAKAKELAD 784
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2084-2181 |
1.06e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 45.54 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2084 EKAKKLAKQAEAAkEKAEREAALLRQQAEEAERQkaaaeqeaanqakAQEDAERLRKEAEFEAAK-----RAQAENAALK 2158
Cdd:PRK05759 35 ERQKKIADGLAAA-ERAKKELELAQAKYEAQLAE-------------ARAEAAEIIEQAKKRAAQiieeaKAEAEAEAAR 100
|
90 100
....*....|....*....|...
gi 1927222988 2159 QKQQADAEMAKHKKLAEQTLKQK 2181
Cdd:PRK05759 101 IKAQAQAEIEQERKRAREELRKQ 123
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2247-2445 |
1.13e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2247 IEEENQRLIKKDKdntqkflaKEADNMKKLAEdaarlsVEAQEAA-RLRQIAEDDLNQQRALADKMLKekmQAIQEASRL 2325
Cdd:PRK12704 36 AEEEAKRILEEAK--------KEAEAIKKEAL------LEAKEEIhKLRNEFEKELRERRNELQKLEK---RLLQKEENL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2326 RAEAEMLQRQKDLAQEQAQKLLEdkqlMQQRLDEETEEYQKsLEAERKRQLEIIaeseklklqvSQLSEAQAKAQ--EEA 2403
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQ----KQQELEKKEEELEE-LIEEQLQELERI----------SGLTAEEAKEIllEKV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1927222988 2404 KKfKKQADsIASRLHETElatqekmtvveklEVARLTSSKEA 2445
Cdd:PRK12704 164 EE-EARHE-AAVLIKEIE-------------EEAKEEADKKA 190
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1726-1979 |
1.14e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1726 RLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLedelakvrsemdvliqlksKAEKETMSNSERSKQLLEveatKM 1805
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEF-------------------RQKNGLVDLSEEAKLLLQ----QL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1806 RDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIAlkekeaeneRLRRQAEDEAYQ 1885
Cdd:COG3206 222 SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELA---------ELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1886 RKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTlkQRRVVEEEIRILKLNfekassgklDLELELNKLK---N 1962
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASL--QAQLAQLEARLAELP---------ELEAELRRLErevE 361
|
250
....*....|....*..
gi 1927222988 1963 IAEETQQSKLRAEEEAE 1979
Cdd:COG3206 362 VARELYESLLQRLEEAR 378
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1354-1589 |
1.21e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1354 EDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKaIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHE 1433
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1434 LKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLEttvKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVN 1513
Cdd:COG3883 109 LGSESFSDFLDRLSALSKIADADADLLEELKADKAELE---AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 1514 EETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQS 1589
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGS 261
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2337-2565 |
1.21e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2337 DLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASr 2416
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2417 lhetelATQEKMTVVEKLEVarLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQnkskemadAQQKQIEHEKTVLQQtfl 2496
Cdd:COG3883 94 ------ALYRSGGSVSYLDV--LLGSESFSDFLDRLSALSKIADADADLLEELK--------ADKAELEAKKAELEA--- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222988 2497 sEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKE 2565
Cdd:COG3883 155 -KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2018-2239 |
1.25e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2018 DELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEdtiMQTKLKEEYEKAKKLAKQAEAAK 2097
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA---LEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2098 EKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAER-LRKEAEFEAAKRAQAEnaALKQKQQadaEMAKHKKLAEQ 2176
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRrLQYLKYLAPARREQAE--ELRADLA---ELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222988 2177 TLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEE 2239
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2146-2360 |
1.35e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2146 AAKRAQAENAA---LKQKQQADAEMAKhkklAEQTLkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQ 2222
Cdd:COG3206 167 ELRREEARKALeflEEQLPELRKELEE----AEAAL-EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2223 RGQVEEELLKVKVQMEELL------KLKLRIEEENQRLIKKDKDNT------QKFLAKEADNMKKLAEDAARLSVEAQEA 2290
Cdd:COG3206 242 LAALRAQLGSGPDALPELLqspviqQLRAQLAELEAELAELSARYTpnhpdvIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2291 ARLRQIAEDDLNQQraladkmLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLedKQLMQQRLDEE 2360
Cdd:COG3206 322 LEALQAREASLQAQ-------LAQLEARLAELPELEAELRRLEREVEVARELYESLL--QRLEEARLAEA 382
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2059-2257 |
1.38e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.28 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2059 EQQVQSVLAQQKEdtimqtkLKEEYEKAKKLAKQAEAAKEKAEREAALLrQQAEEAERQkaaaeqeaanqaKAQEDAERL 2138
Cdd:PRK00409 519 NELIASLEELERE-------LEQKAEEAEALLKEAEKLKEELEEKKEKL-QEEEDKLLE------------EAEKEAQQA 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2139 RKEAEFEAAK-------RAQAENAALKQKQQADA--EMAKHKKLAEQTLKQKFQVEQELT---KVKLKldeTDKQKSVLD 2206
Cdd:PRK00409 579 IKEAKKEADEiikelrqLQKGGYASVKAHELIEArkRLNKANEKKEKKKKKQKEKQEELKvgdEVKYL---SLGQKGEVL 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1927222988 2207 EELQrlKDEVddavkqrgQVEEELLKVKVQMEELLKLKLRIEEENQRLIKK 2257
Cdd:PRK00409 656 SIPD--DKEA--------IVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTV 696
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
46-153 |
1.38e-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: 44.96 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 46 QKKTFTKWVN---------KHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 112
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1927222988 113 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQI 153
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2019-2350 |
1.48e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2019 ELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKE 2098
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2099 KAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTL 2178
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2179 KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKD 2258
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2259 KDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDL 2338
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
330
....*....|..
gi 1927222988 2339 AQEQAQKLLEDK 2350
Cdd:COG4372 359 LSKGAEAGVADG 370
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
52-142 |
1.69e-04 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 43.83 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 52 KWVNKHLIKSQRQ---VTDLYEDLRDGHNLISLLEVLSGETLPREKGRM---RFHKLQNVQIALDFLkhRQVKLVN-IRN 124
Cdd:cd21218 17 RWVNYHLKKAGPTkkrVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAA--EKLGCKYfLTP 94
|
90
....*....|....*...
gi 1927222988 125 DDIADGNPKLTLGLIWTI 142
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2431-2598 |
1.75e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2431 VEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKskeMADAQQKQIEHEKTVLQQTFLSEKEMLLkkeklie 2510
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---IKKYEEQLGNVRNNKEYEALQKEIESLK------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2511 eekkRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAalnKQKEAEKEMHNKQKEMKELERKRLEQERILAEE 2590
Cdd:COG1579 103 ----RRISDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
....*...
gi 1927222988 2591 NQKLREKL 2598
Cdd:COG1579 176 LLALYERI 183
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1810-2162 |
1.82e-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: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1810 EEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAL 1889
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1890 EDQANQHKQQI---EEKIVLLKKSS---EAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNI 1963
Cdd:pfam07888 121 LAQRAAHEARIrelEEDIKTLTQRVlerETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1964 AEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAqdelDRLKKKAEEARKQKDDADKEAEK 2043
Cdd:pfam07888 201 LAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV----EGLGEELSSMAAQRDRTQAELHQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2044 QILMAQQAAQKCSAAEQQVQSVLAQ-QKEDTIMQTKLKEEYEKAKKLAKQAEAAKEkaereaallRQQAEEAERQKAAAE 2122
Cdd:pfam07888 277 ARLQAAQLTLQLADASLALREGRARwAQERETLQQSAEADKDRIEKLSAELQRLEE---------RLQEERMEREKLEVE 347
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1927222988 2123 QEAANQAKAQEDAERLRKEAEFEAAKR-AQAENAALKQKQQ 2162
Cdd:pfam07888 348 LGREKDCNRVQLSESRRELQELKASLRvAQKEKEQLQAEKQ 388
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1721-1904 |
1.83e-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: 46.46 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1721 EQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKetmsnserskQLLEV 1800
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----------QLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1801 EATKMrdlaeeaskLRAIAEEakhqrqvaEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAE 1880
Cdd:COG1579 86 RNNKE---------YEALQKE--------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|....
gi 1927222988 1881 DEAYQRKALEDQANQHKQQIEEKI 1904
Cdd:COG1579 149 EELAELEAELEELEAEREELAAKI 172
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2443-2603 |
1.85e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2443 KEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEmADAQQKQIEHEKTVLQQtflsekemllkkeklieeEKKRLESQFEE 2522
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELEIEEVEA------------------RIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2523 eVKKAKALK------DEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLRE 2596
Cdd:COG1579 85 -VRNNKEYEalqkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*..
gi 1927222988 2597 KLQQLEE 2603
Cdd:COG1579 164 EREELAA 170
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2021-2169 |
1.86e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.56 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2021 DRLKKKAEEARKQkDDADKEAEKQILMAQQAAQKcsAAEQQVQSVLAQQkedtimQTKLKEEyEKAKKLAKQAEAAKEKA 2100
Cdd:COG2268 245 ELAKKKAEERREA-ETARAEAEAAYEIAEANAER--EVQRQLEIAERER------EIELQEK-EAEREEAELEADVRKPA 314
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222988 2101 EREAALLRQQAE-EAERQKAaaeqeaanqaKAQEDAERLRKEAE-FEAAKRAQAENAALKQKQQADAEMAK 2169
Cdd:COG2268 315 EAEKQAAEAEAEaEAEAIRA----------KGLAEAEGKRALAEaWNKLGDAAILLMLIEKLPEIAEAAAK 375
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1807-2043 |
1.87e-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: 47.07 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1807 DLAEEASKLRAIAEEAKHQRQvAEEEAARQRAEAERILKEKLAAISDATRL--KTEAEIALKEKEAE--NERLRRQAEDE 1882
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEK-ELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAelEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1883 AYQRKALEDQ--ANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRvveEEIRILKLNFEKASSGKLDLELELNKL 1960
Cdd:COG4942 100 EAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1961 KNIAEETQQSKLRAEEEAEKLRKLAleeekrrREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKE 2040
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLL-------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 1927222988 2041 AEK 2043
Cdd:COG4942 250 ALK 252
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1174-1984 |
2.00e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1174 RVHSERdaELDHYRQLLSSLQDRWKAVFSQIDLRqRELEQLGRQLGY----YRESYDWLIRwINDAKQRQEKIQAVtITD 1249
Cdd:PRK04863 282 RVHLEE--ALELRRELYTSRRQLAAEQYRLVEMA-RELAELNEAESDleqdYQAASDHLNL-VQTALRQQEKIERY-QAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1250 SKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDyelQLVAYKaqveplasplkkTKLDSASDNIIQ--EYVT 1327
Cdd:PRK04863 357 LEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKS---QLADYQ------------QALDVQQTRAIQyqQAVQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1328 LRTKYSELMTLTSQYIKFITDSQRRLEDEEKAA-EKLKAEEQKkMAMMQAELDKQKQLAEVHAKAIA-----KAEKEAQE 1401
Cdd:PRK04863 422 ALERAKQLCGLPDLTADNAEDWLEEFQAKEQEAtEELLSLEQK-LSVAQAAHSQFEQAYQLVRKIAGevsrsEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1402 LKLRMQEEVNRREdavvdaekQKHNIQLELHELKNLSEQQ----------IMDKSKQVDDALQ-SRVKIEEEIRLIRL-- 1468
Cdd:PRK04863 501 LLRRLREQRHLAE--------QLQQLRMRLSELEQRLRQQqraerllaefCKRLGKNLDDEDElEQLQEELEARLESLse 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1469 QLETTVKQKSTAESELKQLRDRAAEAEKLR---KAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKqkalE 1545
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARIQRLAARApawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVER----D 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1546 DLENLKRQAEEAERQVKQAE-IEKERQIQVA-----------------HVAAQKSAAAElQSKHMSFVEKTSKLEESLKQ 1607
Cdd:PRK04863 649 ELAARKQALDEEIERLSQPGgSEDPRLNALAerfggvllseiyddvslEDAPYFSALYG-PARHAIVVPDLSDAAEQLAG 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1608 EHGA---VLQLQHEAAALKkqqedaerAREEAEKELEK----------WR-----------QKANEALRLRLQAEEEAHK 1663
Cdd:PRK04863 728 LEDCpedLYLIEGDPDSFD--------DSVFSVEELEKavvvkiadrqWRysrfpevplfgRAAREKRIEQLRAEREELA 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1664 KSLAQEDAEKQKEEAEREAKKR--------AKAED--SALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDN 1733
Cdd:PRK04863 800 ERYATLSFDVQKLQRLHQAFSRfigshlavAFEADpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNR 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1734 AEQQRSLLEDElyRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQlkskaeketmsnserskqlLEVEATKMRDLAEEAS 1813
Cdd:PRK04863 880 LLPRLNLLADE--TLADRVEEIREQLDEAEEAKRFVQQHGNALAQ-------------------LEPIVSVLQSDPEQFE 938
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1814 KLRAIAEEAKHQRQvaeeeAARQRAEAeriLKEklaAISDATRLKTEAEIALKEKEAE-NERLRRQAEDEAYQRKALEDQ 1892
Cdd:PRK04863 939 QLKQDYQQAQQTQR-----DAKQQAFA---LTE---VVQRRAHFSYEDAAEMLAKNSDlNEKLRQRLEQAEQERTRAREQ 1007
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1893 ANQHKQQIEEKI-VLLKKSSEAEMERQraivddtlkQRRVVEEEIRILKLNF-----EKASSGKLDLELEL--NKLKNIA 1964
Cdd:PRK04863 1008 LRQAQAQLAQYNqVLASLKSSYDAKRQ---------MLQELKQELQDLGVPAdsgaeERARARRDELHARLsaNRSRRNQ 1078
|
890 900
....*....|....*....|..
gi 1927222988 1965 EETQQSKLRAEEEA--EKLRKL 1984
Cdd:PRK04863 1079 LEKQLTFCEAEMDNltKKLRKL 1100
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1348-1585 |
2.03e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1348 DSQRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELklrmQEEVNRREDAVVDAEKQ-KHN 1426
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREElGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1427 IQLELHELKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAE 1506
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222988 1507 KLRKQVNEETQKKRMAEEELKRkaeaekeaakqkqkALEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAA 1585
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAA--------------AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1104-1984 |
2.09e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.12 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1104 IRNTQgAEGVLKQYEDCLREVHTVpnDVKEVETYRT--KLKKMRAEAEGEQPVFDSLEAELKKA-----TAVSDKMSRVH 1176
Cdd:TIGR01612 801 IDNIK-DEDAKQNYDKSKEYIKTI--SIKEDEIFKIinEMKFMKDDFLNKVDKFINFENNCKEKidsehEQFAELTNKIK 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1177 SE-RDAELDHYRQLLSSLQDRWKAVFSQIDLRQRELEQLGRQLGYYR------ESydwlirwINDAKQRQEKIQAVTITD 1249
Cdd:TIGR01612 878 AEiSDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKicentkES-------IEKFHNKQNILKEILNKN 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1250 SKTLKEQLAQEKKLLEEVEGN-KDKVDECQKYAKAYidTIKDYEL---QLVAYKAQV-EPLASPLKKT------KLDSAS 1318
Cdd:TIGR01612 951 IDTIKESNLIEKSYKDKFDNTlIDKINELDKAFKDA--SLNDYEAknnELIKYFNDLkANLGKNKENMlyhqfdEKEKAT 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1319 DNIIQEYVTLRTKYSELMTLTSQYIKFITDsqrRLEDE-EKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHakaiaKAEK 1397
Cdd:TIGR01612 1029 NDIEQKIEDANKNIPNIEIAIHTSIYNIID---EIEKEiGKNIELLNKEILEEAEINITNFNEIKEKLKHY-----NFDD 1100
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1398 EAQELKLRMQEEVNRREDAVVDAEKQ-KHNIQlELHELKNLSEQQIMDKSKQVDD--ALQSRVKIEEEIRLIRLQLE--- 1471
Cdd:TIGR01612 1101 FGKEENIKYADEINKIKDDIKNLDQKiDHHIK-ALEEIKKKSENYIDEIKAQINDleDVADKAISNDDPEEIEKKIEniv 1179
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1472 TTVKQKSTAESELKQLRDRAAEAEKlRKAAQEEAEKLRKQVNEETQKkrMAEEELKRKAEAEKEAAKQKQKALEDLENLK 1551
Cdd:TIGR01612 1180 TKIDKKKNIYDEIKKLLNEIAEIEK-DKTSLEEVKGINLSYGKNLGK--LFLEKIDEEKKKSEHMIKAMEAYIEDLDEIK 1256
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1552 RQAEEAERQVkQAEIEKERQIQVAHVAAQKSAAAELQSKHMSfvEKTSKL-EESLKQEHGavLQLQHEAAALKKQQEDAE 1630
Cdd:TIGR01612 1257 EKSPEIENEM-GIEMDIKAEMETFNISHDDDKDHHIISKKHD--ENISDIrEKSLKIIED--FSEESDINDIKKELQKNL 1331
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1631 RAREEAEKELEKWRQK-ANEALRLRLQaeeeaHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAEN-ELERQRK 1708
Cdd:TIGR01612 1332 LDAQKHNSDINLYLNEiANIYNILKLN-----KIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDiNLEECKS 1406
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1709 VAESTAQ--------QKLTAEQELI-----RLRADFDNAEQQRsllEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDV 1775
Cdd:TIGR01612 1407 KIESTLDdkdideciKKIKELKNHIlseesNIDTYFKNADENN---ENVLLLFKNIEMADNKSQHILKIKKDNATNDHDF 1483
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1776 LI-QLKSKAEKETMSNSERSKQLLEVEATKM------RDLAEEASKLRAIAEEAKhqrqvaeeeAARQRAEAERILKEkl 1848
Cdd:TIGR01612 1484 NInELKEHIDKSKGCKDEADKNAKAIEKNKElfeqykKDVTELLNKYSALAIKNK---------FAKTKKDSEIIIKE-- 1552
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1849 aaISDA-TRLKTEAEIA-LKEKEAENERLRrqAEDEAyqrkALEDQANQHKQQIEEKIVLLkKSSEAEMERQRAIVDDTL 1926
Cdd:TIGR01612 1553 --IKDAhKKFILEAEKSeQKIKEIKKEKFR--IEDDA----AKNDKSNKAAIDIQLSLENF-ENKFLKISDIKKKINDCL 1623
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222988 1927 KQRRVVEEEIRILKLN-----FEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKL 1984
Cdd:TIGR01612 1624 KETESIEKKISSFSIDsqdteLKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKI 1686
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1641-1854 |
2.10e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1641 EKWRQKANEALRLRLQAEEEAH--------KKSLAQEDAEKQKEEAEREAKKRAK-AEDSALKQKEMAENELERQRKVAE 1711
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEqerlkqleKERLAAQEQKKQAEEAAKQAALKQKqAEEAAAKAAAAAKAKAEAEAKRAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1712 STAQQkltAEQElirlradfdnaeqqrslledelyrlKNEVVAAQQQRKQLEDELAKVRSEMdvliqlKSKAEKEtmsns 1791
Cdd:PRK09510 158 AAAKK---AAAE-------------------------AKKKAEAEAAKKAAAEAKKKAEAEA------AAKAAAE----- 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222988 1792 erSKQLLEVEATKMrdlAEEASKLRAIAEEAKhqrqVAEEEAARQRAEAERILKEKLAAISDA 1854
Cdd:PRK09510 199 --AKKKAEAEAKKK---AAAEAKKKAAAEAKA----AAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2290-2485 |
2.10e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2290 AARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLE 2369
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2370 AERKRQ-----LEIIAESEKLK------LQVSQLSEAQAK-------AQEEAKKFKKQADSIASRLHETELATQEKmtvV 2431
Cdd:COG3883 94 ALYRSGgsvsyLDVLLGSESFSdfldrlSALSKIADADADlleelkaDKAELEAKKAELEAKLAELEALKAELEAA---K 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1927222988 2432 EKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIE 2485
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2517-2612 |
2.18e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2517 ESQFEEEVKKAKALKDEQERQKQQMEDEKKkLQATmDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLRE 2596
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEAL-LEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107
|
90
....*....|....*.
gi 1927222988 2597 KLQQLEEAQKDQPDKE 2612
Cdd:PRK12704 108 REEELEKKEKELEQKQ 123
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
150-263 |
2.37e-04 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 43.64 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 150 DIQINGQSEDMTAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLV-DMGRVYRQTNLENLEQAFGVA 228
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQ---NKLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1927222988 229 ERDLGVTRLLDPEDVDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2132-2610 |
2.43e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2132 QEDAERLRKEAEFEAakRAQAENAALKQKqqaDAEMAKHKklaeQTLKQKFQVEQELTKVKL---KLDETDKQKSVLDEE 2208
Cdd:pfam10174 178 EEDWERTRRIAEAEM--QLGHLEVLLDQK---EKENIHLR----EELHRRNQLQPDPAKTKAlqtVIEMKDTKISSLERN 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2209 LQRLKDEVD----DAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDntqkflakeadnMKKLaedaarls 2284
Cdd:pfam10174 249 IRDLEDEVQmlktNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESE------------LLAL-------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2285 veaqeaarlrQIAEDDLNQQRALADK---MLKEKMQAI-QEASRLRAEAEMLQrqkdLAQEQAQKLLEDKQLMQQRLDEE 2360
Cdd:pfam10174 309 ----------QTKLETLTNQNSDCKQhieVLKESLTAKeQRAAILQTEVDALR----LRLEEKESFLNKKTKQLQDLTEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2361 teeyqKSLEAERKRQLEIIAESEKLKLQVsqLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVArlT 2440
Cdd:pfam10174 375 -----KSTLAGEIRDLKDMLDVKERKINV--LQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEA--L 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2441 SSKEaddlrKAIADLEKEKSRLKKE-AEDLQNKSKEMADAQQK--QIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLE 2517
Cdd:pfam10174 446 SEKE-----RIIERLKEQREREDRErLEELESLKKENKDLKEKvsALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2518 S-QFEEEVKKAKALKDEQERQK-QQME------------------------DEKKKLQATMDAALNKQKEAEKEMHNKQK 2571
Cdd:pfam10174 521 SlEIAVEQKKEECSKLENQLKKaHNAEeavrtnpeindrirlleqevarykEESGKAQAEVERLLGILREVENEKNDKDK 600
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1927222988 2572 EMKELERKRLEQ--------ERILAEENQKLREKLQQLEEAQKDQPD 2610
Cdd:pfam10174 601 KIAELESLTLRQmkeqnkkvANIKHGQQEMKKKGAQLLEEARRREDN 647
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
2066-2374 |
2.53e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.45 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2066 LAQQKEDtiMQTKLKEEYEKakklaKQAEAAKEKA--EREAALLRQQAEEAERQKAAAEQEAAnqaKAQEDAERLRKEAE 2143
Cdd:pfam00038 23 LEQQNKL--LETKISELRQK-----KGAEPSRLYSlyEKEIEDLRRQLDTLTVERARLQLELD---NLRLAAEDFRQKYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2144 FEAAKRAQAENAALKQKQQADAEMAkhkklaeqtlkQKFQVEqelTKVKLKLDETDKQKSVLDEELQRLKD--------- 2214
Cdd:pfam00038 93 DELNLRTSAENDLVGLRKDLDEATL-----------ARVDLE---AKIESLKEELAFLKKNHEEEVRELQAqvsdtqvnv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2215 EVDDAVKQ---------RGQVEEELLKVKVQMEELLKLKLrieEENQRLIKKDKDNTQKflAKEadNMKKLAEDAARLSV 2285
Cdd:pfam00038 159 EMDAARKLdltsalaeiRAQYEEIAAKNREEAEEWYQSKL---EELQQAAARNGDALRS--AKE--EITELRRTIQSLEI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2286 E-----AQEAARLRQIAEddLNQQRALADKMLKEKMQAIQEAsrlraeaemLQRQKdlaQEQAQKLLEDKQLM--QQRLD 2358
Cdd:pfam00038 232 ElqslkKQKASLERQLAE--TEERYELQLADYQELISELEAE---------LQETR---QEMARQLREYQELLnvKLALD 297
|
330
....*....|....*.
gi 1927222988 2359 EETEEYQKSLEAERKR 2374
Cdd:pfam00038 298 IEIATYRKLLEGEECR 313
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2459-2606 |
2.61e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2459 KSRLKKEAEDLQNKSKEMADAQQKQIEHEKtvlQQTFLSEKEmllkkeklieeEKKRLESQFEEEVKKAKALKDEQERQK 2538
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIK---KEALLEAKE-----------EIHKLRNEFEKELRERRNELQKLEKRL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2539 QQMEDEKKKLQATMDaalNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQKLrEKLQQL--EEAQK 2606
Cdd:PRK12704 92 LQKEENLDRKLELLE---KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLtaEEAKE 157
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2241-2415 |
2.62e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2241 LKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQ 2320
Cdd:PRK00409 497 LGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2321 EA-SRLRAEAEMLQRQKDLAQEQAQKLLEDKQL--MQQRLDEETEEYQKSLEAERKRQ--------------------LE 2377
Cdd:PRK00409 577 QAiKEAKKEADEIIKELRQLQKGGYASVKAHELieARKRLNKANEKKEKKKKKQKEKQeelkvgdevkylslgqkgevLS 656
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1927222988 2378 IIAESE--------KLKLQVSQLSEAQAKAQEEAKKFKKQADSIAS 2415
Cdd:PRK00409 657 IPDDKEaivqagimKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRT 702
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1647-1983 |
2.77e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 47.21 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1647 ANEALRLRLQAEEEAH-KKSLAQEDAEKQKEEAEREA----KKRAKAEDSALKQKEMAENELERQRkvaESTAQQKLTAE 1721
Cdd:pfam15964 333 AYEQVKQAVQMTEEANfEKTKALIQCEQLKSELERQKerleKELASQQEKRAQEKEALRKEMKKER---EELGATMLALS 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1722 QELIRLRADFDNAEQQRSlledelyRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQL----KSKAEKETMSNSERSKQL 1797
Cdd:pfam15964 410 QNVAQLEAQVEKVTREKN-------SLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQtkmkKDEAEKEHREYRTKTGRQ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1798 LEVEatkmrdlAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERIlkeklaaisdaTRLKTEAEIALKEKEAENERLRR 1877
Cdd:pfam15964 483 LEIK-------DQEIEKLGLELSESKQRLEQAQQDAARAREECLKL-----------TELLGESEHQLHLTRLEKESIQQ 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1878 QAEDEAyqrKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASsgkldlelel 1957
Cdd:pfam15964 545 SFSNEA---KAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEIT---------- 611
|
330 340
....*....|....*....|....*.
gi 1927222988 1958 NKLKNIAEETQQSKLRAEEEAEKLRK 1983
Cdd:pfam15964 612 QKSRSEVEQLSQEKEYLQDRLEKLQK 637
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1351-1460 |
2.88e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1351 RRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHA-KAIAKAEKEAQELKLRMQEEvnRREDAVVDAEKQKHNIQL 1429
Cdd:PRK00409 537 EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAqQAIKEAKKEADEIIKELRQL--QKGGYASVKAHELIEARK 614
|
90 100 110
....*....|....*....|....*....|...
gi 1927222988 1430 ELHElKNLSEQQIMDKSKQVDDALQS--RVKIE 1460
Cdd:PRK00409 615 RLNK-ANEKKEKKKKKQKEKQEELKVgdEVKYL 646
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3387-3420 |
2.96e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.96e-04
10 20 30
....*....|....*....|....*....|....
gi 1927222988 3387 LLEAQAATGFMVDPVKKQCLSVDEAVKSGLVGPE 3420
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1174-1589 |
2.97e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1174 RVHSER----DAELDHYRQLLSSLQDRwkavfsQIDLRqRELEQLGRQLGY----YRESYDWLIRWINdAKQRQEKIQAV 1245
Cdd:COG3096 281 RELSERalelRRELFGARRQLAEEQYR------LVEMA-RELEELSARESDleqdYQAASDHLNLVQT-ALRQQEKIERY 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1246 TiTDSKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDyelQLVAYKaqveplasplkkTKLDSASDNIIQEY 1325
Cdd:COG3096 353 Q-EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKS---QLADYQ------------QALDVQQTRAIQYQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1326 VTLRT--KYSELMTLTSQYIKFITDSQRRLEDEEKAA-EKLKAEEQKkMAMMQA---ELDKQKQLAEVHAKAIAKAE--K 1397
Cdd:COG3096 417 QAVQAleKARALCGLPDLTPENAEDYLAAFRAKEQQAtEEVLELEQK-LSVADAarrQFEKAYELVCKIAGEVERSQawQ 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1398 EAQELKLRMQEEVNRREdavvdaekQKHNIQLELHELKNLSEQQ------IMDKSKQVDDALQSRVKIEE-----EIRLI 1466
Cdd:COG3096 496 TARELLRRYRSQQALAQ--------RLQQLRAQLAELEQRLRQQqnaerlLEEFCQRIGQQLDAAEELEEllaelEAQLE 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1467 RL--QLETTVKQKSTAESELKQLRDRAAEAEKLRKA---AQEEAEKLRKQVNEETQKKRMAEEELKRKaeaekeaakqkq 1541
Cdd:COG3096 568 ELeeQAAEAVEQRSELRQQLEQLRARIKELAARAPAwlaAQDALERLREQSGEALADSQEVTAAMQQL------------ 635
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1927222988 1542 kaledLENLkRQAEEAERQVKQAEIEKERQIQVAHvAAQKSAAAELQS 1589
Cdd:COG3096 636 -----LERE-REATVERDELAARKQALESQIERLS-QPGGAEDPRLLA 676
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1381-1572 |
3.07e-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: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1381 QKQLAEVHAKaIAKAEKEAQELKLR-----MQEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQ---QIMDKSKQVDDA 1452
Cdd:COG3206 181 EEQLPELRKE-LEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAlraQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1453 LQSRVKIEEEIRLIRLQLE-TTVKQKSTAES-ELKQLRdraAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKA 1530
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAElAELSARYTPNHpDVIALR---AQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQL 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1927222988 1531 EAEKEAAKQKQKALEDLENLKRQAEEAER-------QVKQAEIEKERQI 1572
Cdd:COG3206 337 AQLEARLAELPELEAELRRLEREVEVARElyesllqRLEEARLAEALTV 385
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3093-3129 |
3.14e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.14e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1927222988 3093 KLLSAERAVTGYKDPYTGKTVSLFQAMKKDLIPKEQG 3129
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2298-2606 |
3.16e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2298 EDDLNQQRALADKMLKEKMQAIQEasrLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSleaeRKRQLE 2377
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDE---LNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL----KEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2378 IIAESEKLKLQVSQLSEAQAKAQ---EEAKKFKKQADSIASRLHETELATQEKMTVVEKLEV--ARLTSSKEADDLRKAI 2452
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNkagGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKEleKELEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2453 ADLEKEKSRLKKEAEDLQNKSKEMADAQQKqiehektvlqqtflsekemllkkeklieeekkrLESQFEEEVKKAKALKD 2532
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQE---------------------------------LHEEMIELYKEADELRK 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1927222988 2533 EQERQKQQMEDEKKKLqatmDAALNKQKEAEKEMHNKQKEMKELERKRLEQERilAEENQKLREKLQQLEEAQK 2606
Cdd:COG1340 210 EADELHKEIVEAQEKA----DELHEEIIELQKELRELRKELKKLRKKQRALKR--EKEKEELEEKAEEIFEKLK 277
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1478-1720 |
3.21e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 46.51 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1478 STAESELKQLRDRAAEAEKLRkAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEaekeaakqkqkalEDLENLKRQAEEA 1557
Cdd:PRK07735 1 MDPEKDLEDLKKEAARRAKEE-ARKRLVAKHGAEISKLEEENREKEKALPKNDD-------------MTIEEAKRRAAAA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1558 ERqVKQAEIEKERQIQVAHV------AAQKSAAAELQSKHMSFVEKT------SKLEESLKQEHGAVLQLQHEAAALKKQ 1625
Cdd:PRK07735 67 AK-AKAAALAKQKREGTEEVteeekaKAKAKAAAAAKAKAAALAKQKregteeVTEEEKAAAKAKAAAAAKAKAAALAKQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1626 QEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSL-AQEDAEKQKEEAEREAKKR----AKAEDSAL-KQKEM- 1698
Cdd:PRK07735 146 KREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAeAGEGTEEVTEEEKAKAKAKaaaaAKAKAAALaKQKASq 225
|
250 260
....*....|....*....|....*.
gi 1927222988 1699 ----AENELERQRKVAESTAQQKLTA 1720
Cdd:PRK07735 226 gngdSGDEDAKAKAIAAAKAKAAAAA 251
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2267-2485 |
3.22e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2267 AKEADNMKKLAEDAArlsvEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKL 2346
Cdd:TIGR02794 64 KKEQERQKKLEQQAE----EAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2347 LEDKQLmqqrldeetEEYQKSLEAERKRQLEiiAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQE 2426
Cdd:TIGR02794 140 AERKAK---------EEAAKQAEEEAKAKAA--AEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAE 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1927222988 2427 kmtvveklevarltSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIE 2485
Cdd:TIGR02794 209 --------------AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGAR 253
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2320-2579 |
3.36e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.86 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2320 QEASRLRAeaemlQRQKDLAQEQAQKLLEDKQlmqQRLDEEteeyqkslEAERKRQLEIIAESEKLKLQvsqlsEAQAKA 2399
Cdd:PRK05035 433 QAKAEIRA-----IEQEKKKAEEAKARFEARQ---ARLERE--------KAAREARHKKAAEARAAKDK-----DAVAAA 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2400 QEEAKKFKKQADSIASRLHE-----TELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSK 2474
Cdd:PRK05035 492 LARVKAKKAAATQPIVIKAGarpdnSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEA 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2475 EMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDE---KKKLQAT 2551
Cdd:PRK05035 572 EEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVdprKAAVAAA 651
|
250 260
....*....|....*....|....*...
gi 1927222988 2552 MDAAlnKQKEAEKEMHNKQKEMKELERK 2579
Cdd:PRK05035 652 IARA--KARKAAQQQANAEPEEAEDPKK 677
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2046-2489 |
3.46e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.94 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2046 LMAQQAAQKCSAAEQQVQSvlaqqKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKaeREAALLRQQAEE-AERQKAAAEQE 2124
Cdd:pfam05667 208 LLERNAAELAAAQEWEEEW-----NSQGLASRLTPEEYRKRKRTKLLKRIAEQL--RSAALAGTEATSgASRSAQDLAEL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2125 AANQAKAQEDAERLRKEAEFEAAKRAQAENAAlkqkqQADAEMAKHKKLAEQTLKQkfQVEQELtkvklkldetdkqksv 2204
Cdd:pfam05667 281 LSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEA-----PAATSSPPTKVETEEELQQ--QREEEL---------------- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2205 ldEELQRLKDEVDDAVKqrgQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKF-LAKEAD-NMKKLAEDaar 2282
Cdd:pfam05667 338 --EELQEQLEDLESSIQ---ELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLdLLPDAEeNIAKLQAL--- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2283 lsVEAQeAARLRQIAED-------DLNQQRALADKMLKEKMqaiqEASRLRAEAEMLQRQ-KDLAQEQAQKLLEDKQLMQ 2354
Cdd:pfam05667 410 --VDAS-AQRLVELAGQwekhrvpLIEEYRALKEAKSNKED----ESQRKLEEIKELREKiKEVAEEAKQKEELYKQLVA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2355 Q--RLDEETeeyqkSLEAERKRQLEIIAESEKLKlqvsqlsEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMtvve 2432
Cdd:pfam05667 483 EyeRLPKDV-----SRSAYTRRILEIVKNIKKQK-------EEITKILSDTKSLQKEINSLTGKLDRTFTVTDELV---- 546
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2433 klevarLTSSKEADDLRKA---IADLEKEKSRLKKEAEDLQNKSKEMADAQQkQIEHEKT 2489
Cdd:pfam05667 547 ------FKDAKKDESVRKAykyLAALHENCEQLIQTVEETGTIMREIRDLEE-QIETESG 599
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2076-2180 |
3.60e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 43.58 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2076 QTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEaerqkaaaeqeaaNQAKAQEDAERLRKEAefeaakRAQAENA 2155
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQE-------------IIEEARKEAEKIKEEI------LAEAKEE 92
|
90 100
....*....|....*....|....*
gi 1927222988 2156 ALKQKQQADAEMAKHKKLAEQTLKQ 2180
Cdd:cd06503 93 AERILEQAKAEIEQEKEKALAELRK 117
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2078-2232 |
3.72e-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: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2078 KLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAeRQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAAL 2157
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-EARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 2158 KQKQQADAEMAKHKKLAEqtlkqkfQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKqrgQVEEELLK 2232
Cdd:COG1579 114 ELMERIEELEEELAELEA-------ELAELEAELEEKKAELDEELAELEAELEELEAEREELAA---KIPPELLA 178
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1405-1590 |
4.02e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1405 RMQEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQlettvkQKSTAESEL 1484
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALK------QKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1485 KQLRDRAAEAEKLRKAAQEEAeklrKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQA 1564
Cdd:PRK09510 140 KAAAAAKAKAEAEAKRAAAAA----KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEA 215
|
170 180
....*....|....*....|....*...
gi 1927222988 1565 E--IEKERQIQVAHVAAQKSAAAELQSK 1590
Cdd:PRK09510 216 KkkAAAEAKAAAAKAAAEAKAAAEKAAA 243
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
2288-2498 |
4.54e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 45.20 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2288 QEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEY-QK 2366
Cdd:pfam17045 56 KEIGLLRQQLEELEKGKQELVAKYEQQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFrQK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2367 SLEAERKRQLeiiaesekLKLQVSQLsEAQAKAQEEakkfkkQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEA- 2445
Cdd:pfam17045 136 SLEWEQQRLQ--------YQQQVASL-EAQRKALAE------QSSLIQSAAYQVQLEGRKQCLEASQSEIQRLRSKLERa 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1927222988 2446 -----------DDLRKAIADLEKEKSRLKKEAEDLQNKSKeMADAQQKQIEHEKTVLQQTFLSE 2498
Cdd:pfam17045 201 qdslcaqelelERLRMRVSELGDSNRKLLEEQQRLLEELR-MSQRQLQVLQNELMELKATLQSQ 263
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2026-2257 |
4.76e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.68 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2026 KAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQsvlAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAA 2105
Cdd:pfam13868 111 QEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE---EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2106 LLRQQAEEAERQKAAAEQEAANqaKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKqkfqvE 2185
Cdd:pfam13868 188 RLRAQQEKAQDEKAERDELRAK--LYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAERE-----E 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2186 QELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQ---------RGQVEEELLKVKVQMEELLKLKLRIEEENQRLIK 2256
Cdd:pfam13868 261 EEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKqieereeqrAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
.
gi 1927222988 2257 K 2257
Cdd:pfam13868 341 E 341
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3958-3992 |
4.89e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 4.89e-04
10 20 30
....*....|....*....|....*....|....*
gi 1927222988 3958 LLEAQAATGYVIDPIKNLKLTVSEAVRMGIVGPEF 3992
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2768-2798 |
5.13e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.13e-04
10 20 30
....*....|....*....|....*....|.
gi 1927222988 2768 LSAERAVVGYKDPYTGGKISVFEAMKKGLIE 2798
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2145-2290 |
5.80e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 45.76 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2145 EAAKRAQAENAALKQKQQADAEMAKHKKLAEQTL-KQKFQVEQELTKVKLKLDETDKQKSVLDEELQR-LKDEVDDAVKQ 2222
Cdd:pfam05262 210 EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNAdKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAEnQKREIEKAQIE 289
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 2223 RGQVEEELLKVKVQMEELLKLKLRieEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEA 2290
Cdd:pfam05262 290 IKKNDEEALKAKDHKAFDLKQESK--ASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2074-2292 |
5.87e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2074 IMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALlrqqaeeaerqkaaaeqeaanqaKAQEDAERLRKEAEFEAAKRaqae 2153
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALL-----------------------EAKEEIHKLRNEFEKELRER---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2154 NAALKQKqqadaemakhkklaEQTLKQKfqvEQELTKvklKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEellKV 2233
Cdd:PRK12704 81 RNELQKL--------------EKRLLQK---EENLDR---KLELLEKREEELEKKEKELEQKQQELEKKEEELEE---LI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2234 KVQMEELLKL-KLRIEEENQRLIKKDKDNTQkflaKEADNMKKLAEDAARLsvEAQEAAR 2292
Cdd:PRK12704 138 EEQLQELERIsGLTAEEAKEILLEKVEEEAR----HEAAVLIKEIEEEAKE--EADKKAK 191
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2281-2608 |
6.03e-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: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2281 ARLSVEAQEAARLRQIAE--DDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQR-L 2357
Cdd:pfam07888 67 DREQWERQRRELESRVAElkEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRvL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2358 DEETE-----EYQKSLEAERKRQlEIIAESEKLKLQVSQL-SEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVV 2431
Cdd:pfam07888 147 ERETElermkERAKKAGAQRKEE-EAERKQLQAKLQQTEEeLRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2432 EKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDL-QNKSKEMADAQQKQIEHEKTVLQqtfLSEKEMLLKkeklie 2510
Cdd:pfam07888 226 HRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMaAQRDRTQAELHQARLQAAQLTLQ---LADASLALR------ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2511 eekkrlesqfEEEVKKAKalkdEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEE 2590
Cdd:pfam07888 297 ----------EGRARWAQ----ERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSES 362
|
330
....*....|....*...
gi 1927222988 2591 NQKLREKLQQLEEAQKDQ 2608
Cdd:pfam07888 363 RRELQELKASLRVAQKEK 380
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2488-2602 |
6.11e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 45.36 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2488 KTVLQQtFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQE------RQKQQMEDEKKKLQATMDAALNKQKE 2561
Cdd:pfam02841 175 EEVLQE-FLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQEllrekqKEEEQMMEAQERSYQEHVKQLIEKME 253
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1927222988 2562 AEKEMHNKQKEMKeLERKRLEQERILAE----ENQKLREKLQQLE 2602
Cdd:pfam02841 254 AEREQLLAEQERM-LEHKLQEQEELLKEgfktEAESLQKEIQDLK 297
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1645-1937 |
6.35e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.61 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1645 QKANEALRLRLQAEEEAHKkslaQEDAEKQKEEAEREAKKRAKAEDSALKQKEmaenelerQRKVAESTAQQkltaeqel 1724
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKK----EQERQKKLEQQAEEAEKQRAAEQARQKELE--------QRAAAEKAAKQ-------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1725 irlradfdnAEQQRSlledelyrlknevvAAQQQRKQLEDELAKVRSEmdvliqLKSKAEKEtmsnseRSKQLLEVEATK 1804
Cdd:TIGR02794 107 ---------AEQAAK--------------QAEEKQKQAEEAKAKQAAE------AKAKAEAE------AERKAKEEAAKQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1805 mrdlAEEASKLRAIAE---EAKHQRQVAEEEaARQRAEAERILK-EKLAAISDATRLKTEAEIALKEKEAENERLRRQAE 1880
Cdd:TIGR02794 152 ----AEEEAKAKAAAEakkKAEEAKKKAEAE-AKAKAEAEAKAKaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAE 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222988 1881 DEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIR 1937
Cdd:TIGR02794 227 RKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQNLYDDPSFR 283
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1644-1945 |
6.47e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1644 RQKANEAlRLRLQAEEEAHKKSLAQEDAEKQKEEAER----EAKKRAKAEDSALKQkEMAENELERQRKVAESTAQQK-- 1717
Cdd:pfam02029 12 RRRAREE-RRRQKEEEEPSGQVTESVEPNEHNSYEEDselkPSGQGGLDEEEAFLD-RTAKREERRQKRLQEALERQKef 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1718 ---LTAEQELIRLRADfDNAEQQRSLLEDELYRlknevvaaqQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERS 1794
Cdd:pfam02029 90 dptIADEKESVAERKE-NNEEEENSSWEKEEKR---------DSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1795 KQL-LEVEATKMRDLAEEASKLRAIAEEAK----------HQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEI 1863
Cdd:pfam02029 160 EDKsEEAEEVPTENFAKEEVKDEKIKKEKKvkyeskvfldQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1864 ALKEKEAEN--ERLRRQ---AEDEAYQRKaledqaNQHKQQIEEKIVLLKKSSEaemERQRAIVDDtlKQRRVVEEEIRI 1938
Cdd:pfam02029 240 AEVFLEAEQklEELRRRrqeKESEEFEKL------RQKQQEAELELEELKKKRE---ERRKLLEEE--EQRRKQEEAERK 308
|
....*..
gi 1927222988 1939 LKLNFEK 1945
Cdd:pfam02029 309 LREEEEK 315
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2292-2612 |
6.53e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 46.16 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2292 RLRQIAEDDLNQQRALADKMLKEKMQAIQE---ASRLRAEAEMLQRQKDLAqEQAQKLLEDKQLMQQRLDEETEEYQ--- 2365
Cdd:NF033838 92 KLSDIKTEYLYELNVLKEKSEAELTSKTKKeldAAFEQFKKDTLEPGKKVA-EATKKVEEAEKKAKDQKEEDRRNYPtnt 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2366 -KSLEAErkrqleiIAESEkLKLQVSQLSEAQAKAQE----------EAKKFKKQADsiASRLHETElatQEKMTVVEKL 2434
Cdd:NF033838 171 yKTLELE-------IAESD-VEVKKAELELVKEEAKEprdeekikqaKAKVESKKAE--ATRLEKIK---TDREKAEEEA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2435 EVARLTSSKEADDLRKAIADLEKEKSRLKKEA---EDLQNKSKEMADAQQKQIeHEKTVLQQTFLSEKEMLLKkekliee 2511
Cdd:NF033838 238 KRRADAKLKEAVEKNVATSEQDKPKRRAKRGVlgePATPDKKENDAKSSDSSV-GEETLPSPSLKPEKKVAEA------- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2512 ekkrlESQFEEEVKKAKALKDEQER-------------------QKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKE 2572
Cdd:NF033838 310 -----EKKVEEAKKKAKDQKEEDRRnyptntyktleleiaesdvKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAE 384
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1927222988 2573 MKELE-----RKRLEQE--RILAEENQKLREKLQQLEEAQKDQPDKE 2612
Cdd:NF033838 385 ATRLEkiktdRKKAEEEakRKAAEEDKVKEKPAEQPQPAPAPQPEKP 431
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1611-1842 |
6.98e-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: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1611 AVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAED 1690
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1691 SALKQKEMAENELERQRKVAESTAQQK-----------LTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQR 1759
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1760 KQLEDELAKVRSEMDVLIQLKSKAEKEtmsnSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAE 1839
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKL----LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 1927222988 1840 AER 1842
Cdd:COG4942 250 ALK 252
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1488-1716 |
7.17e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.63 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1488 RDRAAEAEKLRKAAQEEAEKLrKQVNEETQKKRMAEEELKRKAEAEKEAAKQkqkalEDLENLKRQAEEaERQVKQAEIE 1567
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERE-TEIAIAQANREAEEAELEQEREIETARIAE-----AEAELAKKKAEE-RREAETARAE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1568 KERQIQVAHVAAQKSAAAELqskhmsfvektskleESLKQEHGAVLQlqhEAAALKKQQEdaerareeaekeLEKWRQKA 1647
Cdd:COG2268 264 AEAAYEIAEANAEREVQRQL---------------EIAEREREIELQ---EKEAEREEAE------------LEADVRKP 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1648 NEALRLRLQAEEEAHKkslaqeDAEKQKEEAEREAkKRAKAE-DSALKQKEMAENELERQRKVAESTAQQ 1716
Cdd:COG2268 314 AEAEKQAAEAEAEAEA------EAIRAKGLAEAEG-KRALAEaWNKLGDAAILLMLIEKLPEIAEAAAKP 376
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1379-1599 |
7.38e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1379 DKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQKHNIQLELHELknlsEQQIMDKSKQVDDAlqsRVK 1458
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEER---REE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1459 IEEEIRLIRLQ------LETTVKQKSTAE-----SELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELK 1527
Cdd:COG3883 88 LGERARALYRSggsvsyLDVLLGSESFSDfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 1528 RKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTS 1599
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1659-2115 |
7.53e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1659 EEAHKKSLAQED----AEKQKEEAE----------REAKKRAKAEDSALKQKEMAE--------------NELERQRKVA 1710
Cdd:pfam05557 44 DRESDRNQELQKrirlLEKREAEAEealreqaelnRLKKKYLEALNKKLNEKESQLadarevisclknelSELRRQIQRA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1711 ESTAQQKLTAEQELIR----LRADFDNAEQQRSLLEDELYRLKnevvAAQQQRKQLEDELAKvrSEMDVLIQLKSKAEKE 1786
Cdd:pfam05557 124 ELELQSTNSELEELQErldlLKAKASEAEQLRQNLEKQQSSLA----EAEQRIKELEFEIQS--QEQDSEIVKNSKSELA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1787 TMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAK---HQRQVAEEEAARQRAEAERILKE-----KLAAISDATRLK 1858
Cdd:pfam05557 198 RIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKrklEREEKYREEAATLELEKEKLEQElqswvKLAQDTGLNLRS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1859 TEA-----------EIALKEkeaENERLRRQAEDEAYQRKALEDQANQHKQQIEEkivlLKKsseaEMERQRAIVDDTLK 1927
Cdd:pfam05557 278 PEDlsrrieqlqqrEIVLKE---ENSSLTSSARQLEKARRELEQELAQYLKKIED----LNK----KLKRHKALVRRLQR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1928 QRRVVEEEIRILK---------LNFEKASSGKLDLELELNKL------KNIAEETQQSKLRAEEEAEKLRKLALEEEKRR 1992
Cdd:pfam05557 347 RVLLLTKERDGYRailesydkeLTMSNYSPQLLERIEEAEDMtqkmqaHNEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1993 REAEEKVKKIAAAEEEAARQRQaaqdELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKED 2072
Cdd:pfam05557 427 LRQQESLADPSYSKEEVDSLRR----KLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQR 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1927222988 2073 TIMQTKLKEEYEKAKKLAKQAEAAKEK-----------AEREAALLRQQAEEAE 2115
Cdd:pfam05557 503 KNQLEKLQAEIERLKRLLKKLEDDLEQvlrlpettstmNFKEVLDLRKELESAE 556
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1867-2159 |
7.74e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1867 EKEAENERLRRQAEDEAYQRKALE------DQANQHKQQIEEKIVLLKKSSEAEMERQRAIVDDTLK-----QRRVVEEE 1935
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEpsgqvtESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKreerrQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1936 IRiLKLNFEKASSGKLDLELELNKL-----KNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAA 2010
Cdd:pfam02029 84 ER-QKEFDPTIADEKESVAERKENNeeeenSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2011 RQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQ--AAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKA-- 2086
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRghPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAev 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 2087 -----KKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQ 2159
Cdd:pfam02029 243 fleaeQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKE 320
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1654-1844 |
8.40e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1654 RLQAEEEAHKKSL-AQEDAEKQKEEAEREAKKRakaedsalkqkemaENELERQrkvaESTAQQKltaEQELirlradfd 1732
Cdd:PRK12704 48 KKEAEAIKKEALLeAKEEIHKLRNEFEKELRER--------------RNELQKL----EKRLLQK---EENL-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1733 naEQQRSLLEDElyrlKNEVVAAQQQRKQLEDELAKVRSEMDVLIQlKSKAEKETMSN--SERSKQLL--EVEAtKMRdl 1808
Cdd:PRK12704 99 --DRKLELLEKR----EEELEKKEKELEQKQQELEKKEEELEELIE-EQLQELERISGltAEEAKEILleKVEE-EAR-- 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 1927222988 1809 AEEASKLRAIAEEAKhqrqvaeEEAARqraEAERIL 1844
Cdd:PRK12704 169 HEAAVLIKEIEEEAK-------EEADK---KAKEIL 194
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1600-1887 |
8.68e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 45.03 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1600 KLEESLKQEHGAVLQLQHEAAALKKQQEDaerareeaekeLEKWRQKANEALRLRLQAEEEAHKKSLAQEdaekQKEEAE 1679
Cdd:pfam15558 19 EEQRMRELQQQAALAWEELRRRDQKRQET-----------LERERRLLLQQSQEQWQAEKEQRKARLGRE----ERRRAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1680 REAKKRAKAEDSALKQKEMAEN----ELERQRKVAESTAQ---QKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEV 1752
Cdd:pfam15558 84 RREKQVIEKESRWREQAEDQENqrqeKLERARQEAEQRKQcqeQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKER 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1753 vaAQQQRKQLEDELAKVRSE-MDVLIQLKSKAEKETMSNS---------ERSKQLLEVEATKMRDLA--EEASKLRA--I 1818
Cdd:pfam15558 164 --EEQKKVQENNLSELLNHQaRKVLVDCQAKAEELLRRLSleqslqrsqENYEQLVEERHRELREKAqkEEEQFQRAkwR 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222988 1819 AEEAKHQRQ------VAEEEAARQRAE--AERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRK 1887
Cdd:pfam15558 242 AEEKEEERQehkealAELADRKIQQARqvAHKTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKK 318
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2174-2391 |
8.69e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.21 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2174 AEQTLKQKFQVEQELTKVKLKLDETDKQKsvldEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKL---KLRIEEE 2250
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDASK----QRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEilaSLSLEEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2251 NQRLIKKDKD--NTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQ-EASRLRA 2327
Cdd:pfam12795 84 EQRLLQTSAQlqELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELAALKA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 2328 EAEMLQRQ---KDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLE-IIAESEKLKLQVSQ 2391
Cdd:pfam12795 164 QIDMLEQEllsNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQEAEqAVAQTEQLAEEAAG 231
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2388-2578 |
8.91e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2388 QVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKE-KSRLKKEA 2466
Cdd:PRK09510 63 QYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQaEEAAAKAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2467 EDLQNKSKE---MADAQQKQIEHEKTVlqqtflseKEMLLKKEKLIEEEKKRLEsqfEEEVKKAKAL---KDEQERQKQQ 2540
Cdd:PRK09510 143 AAAKAKAEAeakRAAAAAKKAAAEAKK--------KAEAEAAKKAAAEAKKKAE---AEAAAKAAAEakkKAEAEAKKKA 211
|
170 180 190
....*....|....*....|....*....|....*...
gi 1927222988 2541 MEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELER 2578
Cdd:PRK09510 212 AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEK 249
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2094-2537 |
8.98e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.28 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2094 EAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAER---LRKEAEFEAAKRAQAENAALKQKQQADAEMAKH 2170
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQviaLRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2171 KKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEE 2250
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2251 NQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAE 2330
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2331 MLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQA 2410
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2411 DSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTV 2490
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1927222988 2491 LQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQ 2537
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASA 528
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2185-2593 |
9.01e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2185 EQELTKVKLKLDETDKQKSVLDEELQRLKDEVDdaVKQRgqvEEELLKVKVQ-MEELLKLKLRIEEENQRLIK---KDKD 2260
Cdd:pfam10174 358 ESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLD--VKER---KINVLQKKIEnLQEQLRDKDKQLAGLKERVKslqTDSS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2261 NTQKFLA--KEADNMKKLAEDAARLSVEAQEAARLRQIaeDDLNQQralaDKMLKEKMQAIQE--ASRLRAEAEMLQRQK 2336
Cdd:pfam10174 433 NTDTALTtlEEALSEKERIIERLKEQREREDRERLEEL--ESLKKE----NKDLKEKVSALQPelTEKESSLIDLKEHAS 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2337 DLAQEQAQKLLEDKQL---MQQRLDEETE---EYQKSLEAERKRQLeiiaeSEKLKLQVSQLSEAQAKAQEEAKKFKKQA 2410
Cdd:pfam10174 507 SLASSGLKKDSKLKSLeiaVEQKKEECSKlenQLKKAHNAEEAVRT-----NPEINDRIRLLEQEVARYKEESGKAQAEV 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2411 DSIASRLHETElatqekmtvveklevarltssKEADDLRKAIADLEKEKSRLKKEaedlqnKSKEMADAQQKQIEHEKTV 2490
Cdd:pfam10174 582 ERLLGILREVE---------------------NEKNDKDKKIAELESLTLRQMKE------QNKKVANIKHGQQEMKKKG 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2491 LQqtflsekEMLLKKEKLIEEEKKRLESQFEEevkkakaLKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQ 2570
Cdd:pfam10174 635 AQ-------LLEEARRREDNLADNSQQLQLEE-------LMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERR 700
|
410 420
....*....|....*....|....
gi 1927222988 2571 KEMKE-LERKrleQERILAEENQK 2593
Cdd:pfam10174 701 KQLEEiLEMK---QEALLAAISEK 721
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1972-2377 |
9.47e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1972 LRAEEEAEKLRKLALEEEKRRREAEEKVKKiaaaeeeaarqrqaaqdELDRLKKKAEEArkqkdDADKEAEKQILMAQQA 2051
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAA-----------------EQYRLVEMAREL-----AELNEAESDLEQDYQA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2052 AqkcSAAEQQVQSVLAQQKEDTIMQTKLKeeyEKAKKLAKQAEAAKEKAEreaallrqQAEEAERQKAAaeqeaanqakA 2131
Cdd:PRK04863 333 A---SDHLNLVQTALRQQEKIERYQADLE---ELEERLEEQNEVVEEADE--------QQEENEARAEA----------A 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2132 QEDAERLRKE-AEFEAA-----KRA----QAENAALKQKQQ---ADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDET 2198
Cdd:PRK04863 389 EEEVDELKSQlADYQQAldvqqTRAiqyqQAVQALERAKQLcglPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2199 DKQKSVLDEELQ---RLKDEVD--DAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKkdKDNTQKFLAKEADNM 2273
Cdd:PRK04863 469 QAAHSQFEQAYQlvrKIAGEVSrsEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQ--QQRAERLLAEFCKRL 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2274 KKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEA-EMLQRQKDLAQ--EQAQKLLEDK 2350
Cdd:PRK04863 547 GKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARApAWLAAQDALARlrEQSGEEFEDS 626
|
410 420 430
....*....|....*....|....*....|..
gi 1927222988 2351 Q----LMQQRLDEETE-EYQKSLEAERKRQLE 2377
Cdd:PRK04863 627 QdvteYMQQLLERERElTVERDELAARKQALD 658
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2088-2301 |
9.63e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2088 KLAKQAEAAKEKAEREAALLRQQAEEAERQKAaaeqeaanqaKAQEDAERLRKEAEFEAAKRAQAENAA-LKQKQQADAE 2166
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQA----------AEQERLKQLEKERLAAQEQKKQAEEAAkQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2167 MAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQksvlDEELQRLKDEVDDAVKQrgqveEELLKVKVQMEELLKLKLR 2246
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKK----AEAEAAKKAAAEAKKKA-----EAEAAAKAAAEAKKKAEAE 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 2247 IEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQIAE-DDL 2301
Cdd:PRK09510 207 AKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEvDDL 262
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1429-1787 |
9.91e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1429 LELHELKNLSEQQIMDKSKQVDdalqSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAE------------- 1495
Cdd:COG5185 184 LTLGLLKGISELKKAEPSGTVN----SIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEdlaqtsdkleklv 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1496 ----KLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQ 1571
Cdd:COG5185 260 eqntDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQ 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1572 IQVAHVAAQKSAAAELQSKHMSFVEKTSKLEEslkqehgaVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEAL 1651
Cdd:COG5185 340 NLTAEIEQGQESLTENLEAIKEEIENIVGEVE--------LSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1652 rlrlqaeeEAHKKSlaqedAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELI--RLRA 1729
Cdd:COG5185 412 --------EDTLKA-----ADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEInrSVRS 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 1730 DFDNAEQQRSLLEDELYRLKNEVvaaQQQRKQLEDELAKVRSEMDVLIQLKSKAEKET 1787
Cdd:COG5185 479 KKEDLNEELTQIESRVSTLKATL---EKLRAKLERQLEGVRSKLDQVAESLKDFMRAR 533
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
40-143 |
1.01e-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: 42.05 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 40 DERDRVQkktFTKWVNK---------HLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETL-------PREKGRM--RFHK 101
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIdervlnkPPRKNKPlnNFQM 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1927222988 102 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 143
Cdd:cd21294 81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
2159-2592 |
1.06e-03 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 45.24 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2159 QKQQADAEMAKHKKLAEQTLKQKF------QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLK 2232
Cdd:pfam09730 8 KKVAADGESREESLLQESASKEAYyaqrilELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDEIKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2233 VKVQMEELLKLKLRIEEENQRLIKKD---KDNTQKFLAKEADnMKKLAEDAARLSVEAQEAARLRQIAEddlnqqralad 2309
Cdd:pfam09730 88 YKVREARLLQDYSELEEENISLQKQVsvlKQNQVEFEGLKHE-ITRKEEETELLNSQLEEAIRLREIAE----------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2310 KMLKEKMQAIQEASRLRAEAemlqrQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESE----KL 2385
Cdd:pfam09730 156 RQLDEALETLKTEREQKNSL-----RKELSHYMTLNDFDYVSHLSISLDGLKFSEDEGAGTEPNNDGEAMDGGEngggGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2386 KLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETEL---------ATQEKMTVVEKLEvarlTSSKEADDLRKAIADLE 2456
Cdd:pfam09730 231 KNSGLDNRTSTPRKSEVFPPAPSLVSDLLSELNISEIqklkqqliqVEREKVSLLSTLQ----ESQKQLEQAKGALSEQQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2457 KEKSRLKKEAEDLQN----KSKEMADAQQKQ-IEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFeeevkkaKALK 2531
Cdd:pfam09730 307 EKVNRLTENLEAMRGlqasKERQDALDSEKDrDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREEL-------KALK 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222988 2532 DEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELErKRLEQERILAEENQ 2592
Cdd:pfam09730 380 ARYNTLEERYKEEKTRWEAEAQDLAEKIRQLEKASHQDQERIAHLE-KELGKTRKVAGESE 439
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
41-149 |
1.07e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 41.90 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 41 ERDRVQKKTFTKWVNKhlIKSQRQVTDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 111
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1927222988 112 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2313-2565 |
1.07e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.32 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2313 KEKMQAiqEASRLRAEAemlqRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEaeRKRQLEIIAESEKLKLQVSQL 2392
Cdd:PRK05035 443 QEKKKA--EEAKARFEA----RQARLEREKAAREARHKKAAEARAAKDKDAVAAALA--RVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2393 SEAQAKAQEEAKKFKKQADsiASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNK 2472
Cdd:PRK05035 515 DNSAVIAAREARKAQARAR--QAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAK 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2473 SKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEE--------EVKKAKALKDEQER---QKQQM 2541
Cdd:PRK05035 593 KAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDprkaavaaAIARAKARKAAQQQanaEPEEA 672
|
250 260
....*....|....*....|....*.
gi 1927222988 2542 EDEKKklqATMDAALN--KQKEAEKE 2565
Cdd:PRK05035 673 EDPKK---AAVAAAIAraKAKKAAQQ 695
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1667-1851 |
1.09e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 44.20 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1667 AQEDAEKQKEEAEREAKKRAKAEDS-ALKQKEMAENELERQR---------KVAESTAQQKLTAEQELIRLRADFDNAEQ 1736
Cdd:pfam12037 1 GGPGSDKDPKKSNDKPRTAYSGFDPeALERAAKAARELESSPhakkalelmKKQEQTRQAELQAKIKEYEAAQEQLKIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1737 QRsLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAE-----------KETMSNSERSKQLLEVEA--- 1802
Cdd:pfam12037 81 QR-VEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEEllrkqeesvakQEAMRIQAQRRQTEEHEAelr 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1927222988 1803 --TKMRDLAEEAsklRAIAEEAKHQRQVAEEEaARQRAEAERilKEKLAAI 1851
Cdd:pfam12037 160 reTERAKAEAEA---EARAKEERENEDLNLEQ-LREKANEER--ETVLESI 204
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2239-2403 |
1.11e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.99 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2239 ELLKLKLRIEEENQRLIKKDKDNTQKfLAKEADNMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQA 2318
Cdd:pfam05262 199 DMTDLKERESQEDAKRAQQLKEELDK-KQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2319 IQeasrlRAEAEMLQRQKDLAQEQAQKLLEDK--QLMQQRLDEETEEYQKSLEAERKRqLEIIAESEKLKLQVsqlsEAQ 2396
Cdd:pfam05262 278 NQ-----KREIEKAQIEIKKNDEEALKAKDHKafDLKQESKASEKEAEDKELEAQKKR-EPVAEDLQKTKPQV----EAQ 347
|
....*..
gi 1927222988 2397 AKAQEEA 2403
Cdd:pfam05262 348 PTSLNED 354
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2290-2608 |
1.11e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2290 AARLRQIAEDDLNQQRALADK--MLKEKMQAIQEASRL---RAEAEMLQ-RQKDLAQEQaQKLLEDKQLMQQ--RLDEET 2361
Cdd:COG3096 271 ADYMRHANERRELSERALELRreLFGARRQLAEEQYRLvemARELEELSaRESDLEQDY-QAASDHLNLVQTalRQQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2362 EEYQKSLEAERKRqLEIIAEseklklQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTvveklevarlts 2441
Cdd:COG3096 350 ERYQEDLEELTER-LEEQEE------VVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQT------------ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2442 skEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMA--DAQQKQIEHEKTVLQQTfLSEKEMLLkkeklieeekkrleSQ 2519
Cdd:COG3096 411 --RAIQYQQAVQALEKARALCGLPDLTPENAEDYLAafRAKEQQATEEVLELEQK-LSVADAAR--------------RQ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2520 FEEEVKKAKALKDEQERQ------KQQMED--EKKKLQATMDAALNKQKEAEKEMHNKQKEMKELER--KRLEQ------ 2583
Cdd:COG3096 474 FEKAYELVCKIAGEVERSqawqtaRELLRRyrSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfcQRIGQqldaae 553
|
330 340
....*....|....*....|....*..
gi 1927222988 2584 --ERILAEENQKLREKLQQLEEAQKDQ 2608
Cdd:COG3096 554 elEELLAELEAQLEELEEQAAEAVEQR 580
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2199-2415 |
1.14e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2199 DKQKSVLDEELQRLKDEvddavkqRGQVEEELLKVKVQMEELLKLklrieeENQRLIKKDKDNTQKFLAKEADNMKKLAE 2278
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKE-------QQQAEELQQKQAAEQERLKQL------EKERLAAQEQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2279 DAARlsvEAQEAARLRqiAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMlqrQKDLAQEQAQKLledkqlmqqrld 2358
Cdd:PRK09510 136 EAAA---KAAAAAKAK--AEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAEAAAKA------------ 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222988 2359 eeTEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIAS 2415
Cdd:PRK09510 196 --AAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKA 250
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2365-2485 |
1.15e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2365 QKSLEAERKRQlEIIAESEKLKLQVSQlsEAQAKAQEEAKKFKKQADSiASRLHETELATQEKmtvveKLEVARLTSSKE 2444
Cdd:PRK12704 31 AKIKEAEEEAK-RILEEAKKEAEAIKK--EALLEAKEEIHKLRNEFEK-ELRERRNELQKLEK-----RLLQKEENLDRK 101
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1927222988 2445 ADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIE 2485
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| 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 ... |
1830-1929 |
1.17e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 41.91 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1830 EEEAARQRAEAERILKEKLAAISdatrlktEAEIALKEKEAENERLRRQAEDEAYQ-RKALEDQANQHKQQIEEkivllk 1908
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAALA-------EAEQQLKEARAEAQEIIENAKKRAEKlKEEIVAAAEAEAERIIE------ 98
|
90 100
....*....|....*....|.
gi 1927222988 1909 kSSEAEMERQRAIVDDTLKQR 1929
Cdd:pfam00430 99 -QAAAEIEQEKDRALAELRQQ 118
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1037-1688 |
1.23e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1037 KVQVELEGLKKDLNKVSAK----TKEVLASPQQTASAPVLRSELdlTVEKMDHTHMLSSVYLEKLKTVEMVIRNTQGAEG 1112
Cdd:pfam01576 437 KLQSELESVSSLLNEAEGKniklSKDVSSLESQLQDTQELLQEE--TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1113 VLKQYEDCLREVHTVPNDVKE----VETYRTKLKKMRAEAEGEQPVFDSLEAELKKATAVSDKMSRVHSERDAELDHYRQ 1188
Cdd:pfam01576 515 VERQLSTLQAQLSDMKKKLEEdagtLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQ 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1189 LLSSLQDRWKAvFSQIDLRQRELEqlgrqlGYYRESYDWLirwinDAKQRQEKIQAVTITdsktlkeqlaqekKLLEEVE 1268
Cdd:pfam01576 595 LVSNLEKKQKK-FDQMLAEEKAIS------ARYAEERDRA-----EAEAREKETRALSLA-------------RALEEAL 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1269 GNKDKVDECQKYAKAYIDtikdyelQLVAYKAQVEPLASPLKKTKldSASDNIIQEyvtLRTKYSElmtltsqyikfitd 1348
Cdd:pfam01576 650 EAKEELERTNKQLRAEME-------DLVSSKDDVGKNVHELERSK--RALEQQVEE---MKTQLEE-------------- 703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1349 sqrrLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKA-EKEAQELKLRMQEEVNRREDAVvdAEKQKhnI 1427
Cdd:pfam01576 704 ----LEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQlVKQVRELEAELEDERKQRAQAV--AAKKK--L 775
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1428 QLELHELknlsEQQIMDKSKQVDDALQSRVKIE----------EEIRLIRLQLETTVKQKS----TAESELKQLRDRAAE 1493
Cdd:pfam01576 776 ELDLKEL----EAQIDAANKGREEAVKQLKKLQaqmkdlqrelEEARASRDEILAQSKESEkklkNLEAELLQLQEDLAA 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1494 AEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQ--AEIEKERq 1571
Cdd:pfam01576 852 SERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQltTELAAER- 930
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1572 iqvAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEH-GAVLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEA 1650
Cdd:pfam01576 931 ---STSQKSESARQQLERQNKELKAKLQEMEGTVKSKFkSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEV 1007
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1927222988 1651 LrlrLQAEEEAHKKSLAQEDAEK----------QKEEAEREAkKRAKA 1688
Cdd:pfam01576 1008 L---LQVEDERRHADQYKDQAEKgnsrmkqlkrQLEEAEEEA-SRANA 1051
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
45-147 |
1.23e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 41.90 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 45 VQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKHRQVKLV 120
Cdd:cd21337 20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
|
90 100
....*....|....*....|....*..
gi 1927222988 121 NIRNDDIADGNPKLTLGLIWTIILHFQ 147
Cdd:cd21337 100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1438-1963 |
1.27e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1438 SEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLrKQVNEETQ 1517
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDL-SMELEKNN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1518 KKRMAEEELKRkaeAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAeiekERQIQVAHVAAQKsaAAELQSKHMSFVEK 1597
Cdd:PRK01156 274 YYKELEERHMK---IINDPVYKNRNYINDYFKYKNDIENKKQILSNI----DAEINKYHAIIKK--LSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1598 TSKLEEslkqehgavlqLQHEAAALKKQQEDAERAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEE 1677
Cdd:PRK01156 345 KSRYDD-----------LNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1678 AEREAKK-RAKAEDSALKQKEMAENELERQRKVAESTAQQKLT------AEQELIRLRADFDNaeqQRSLLEDELYRLKN 1750
Cdd:PRK01156 414 INVKLQDiSSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPvcgttlGEEKSNHIINHYNE---KKSRLEEKIREIEI 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1751 EVVAAQQQRKQLE--------DELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEE- 1821
Cdd:PRK01156 491 EVKDIDEKIVDLKkrkeylesEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSw 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1822 --AKHQRQVAEEEAARQRAEaerilkEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEA--YQRKALEDQANQ-H 1896
Cdd:PRK01156 571 lnALAVISLIDIETNRSRSN------EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEAnnLNNKYNEIQENKiL 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1897 KQQIEEKIVLLKKSSEAEMERQ--------------------RAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELE 1956
Cdd:PRK01156 645 IEKLRGKIDNYKKQIAEIDSIIpdlkeitsrindiednlkksRKALDDAKANRARLESTIEILRTRINELSDRINDINET 724
|
....*..
gi 1927222988 1957 LNKLKNI 1963
Cdd:PRK01156 725 LESMKKI 731
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1820-2279 |
1.27e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.13 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1820 EEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERlrrQAEDEAYQRKALEDQAnqhKQQ 1899
Cdd:pfam09731 52 GEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEK---EATKDAAEAKAQLPKS---EQE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1900 IEEKIVLLKKSSEAEMER-QRAIVDDTLKQRRVVEEEIRILKLNFEKAssgkldlelelnkLKNIAEETQQSKLRAEEEA 1978
Cdd:pfam09731 126 KEKALEEVLKEAISKAESaTAVAKEAKDDAIQAVKAHTDSLKEASDTA-------------EISREKATDSALQKAEALA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1979 EKLRKLAleeekrRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAA 2058
Cdd:pfam09731 193 EKLKEVI------NLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2059 EQQVQSVLaqqKEDTIMQT--------KLKEEYEKA-KKLAKQ--------AEAAKEKAEREAALLRQQAEEAERQKaaa 2121
Cdd:pfam09731 267 FPDIIPVL---KEDNLLSNddlnsliaHAHREIDQLsKKLAELkkreekhiERALEKQKEELDKLAEELSARLEEVR--- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2122 eqeaaNQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQElTKVklkLDETDKQ 2201
Cdd:pfam09731 341 -----AADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIK-EKV---EEERAGR 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 2202 KSVLDEELQRLKdEVDDAVKQRGQVEEELLKVKvqmeellKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAED 2279
Cdd:pfam09731 412 LLKLNELLANLK-GLEKATSSHSEVEDENRKAQ-------QLWLAVEALRSTLEDGSADSRPRPLVRELKALKELASD 481
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1673-1903 |
1.34e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.21 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1673 KQKEEAEREAKKRAKAEDSALKQKEMAEN-----ELERQRKVAE-STAQQKLTAEQELirlrADFDNAEQQRSLLEDELY 1746
Cdd:NF012221 1541 SQQADAVSKHAKQDDAAQNALADKERAEAdrqrlEQEKQQQLAAiSGSQSQLESTDQN----ALETNGQAQRDAILEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1747 RLKNEVVAAQQQRKQLEDE-------------------LAKVRSEMDvliQLKSKAEKETmsnsERSKQLLEVEATKMRD 1807
Cdd:NF012221 1617 AVTKELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLD---DAKKISGKQL----ADAKQRHVDNQQKVKD 1689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1808 laeEASKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRK 1887
Cdd:NF012221 1690 ---AVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ 1766
|
250
....*....|....*.
gi 1927222988 1888 AledQANQHKQQIEEK 1903
Cdd:NF012221 1767 A---DAKGAKQDESDK 1779
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2423-2607 |
1.35e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.90 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2423 ATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEml 2502
Cdd:pfam15964 333 AYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQ-- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2503 lkkeklieeEKKRLESQFEEEVKKAKALKDEQERQKQQM---EDEKKKLQATMDAALNKQK----EAEKEMHN-KQKEMK 2574
Cdd:pfam15964 411 ---------NVAQLEAQVEKVTREKNSLVSQLEEAQKQLasqEMDVTKVCGEMRYQLNQTKmkkdEAEKEHREyRTKTGR 481
|
170 180 190
....*....|....*....|....*....|...
gi 1927222988 2575 ELERKRLEQERILAEenqkLREKLQQLEEAQKD 2607
Cdd:pfam15964 482 QLEIKDQEIEKLGLE----LSESKQRLEQAQQD 510
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
183-260 |
1.40e-03 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 40.75 E-value: 1.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 183 DNFTTSWRDGKLFNAVIHKHYPRLVDMGRVYRQTNLENLEQAFGVAERdLGVTRLLDPEDVDVPHPDEKSIITYVSSL 260
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1456-1919 |
1.41e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.68 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1456 RVKIEE-EIRLIRLQLETTVKQKSTAESelKQLRDraaEAEKLRKAAqEEAEKLRKQVneETQKKRmaeeelkrkaeaek 1534
Cdd:pfam05622 86 RIKCEElEKEVLELQHRNEELTSLAEEA--QALKD---EMDILRESS-DKVKKLEATV--ETYKKK-------------- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1535 eaakqkqkaLEDLENLKRQ--------AEEAERQVKQAEIEKERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLK 1606
Cdd:pfam05622 144 ---------LEDLGDLRRQvklleernAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1607 QEHGAVLQLQHEAAALKKQQEDAerareeaekelekwrQKANEALRLrlqAEEEAHKKSLAQEDAEKQKEEAEREAKKRA 1686
Cdd:pfam05622 215 KLEEKLEALQKEKERLIIERDTL---------------RETNEELRC---AQLQQAELSQADALLSPSSDPGDNLAAEIM 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1687 KAEdsaLKQK-EMAENELERQRKVAESTAQQKLTAEQELIrlradfDNAEQQRSLLEDELyRLKNE-VVAAQQQRKQLED 1764
Cdd:pfam05622 277 PAE---IREKlIRLQHENKMLRLGQEGSYRERLTELQQLL------EDANRRKNELETQN-RLANQrILELQQQVEELQK 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1765 ELAKVRSEMDVLIQLKSKAE----KETMSNSERSK---QLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQR 1837
Cdd:pfam05622 347 ALQEQGSKAEDSSLLKQKLEehleKLHEAQSELQKkkeQIEELEPKQDSNLAQKIDELQEALRKKDEDMKAMEERYKKYV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1838 AEAERILK-----EKLAAISDATRLKT-----EAEIALKEKEAENERLRRQAEDE----AYQRKALedqaNQHKQQIEEK 1903
Cdd:pfam05622 427 EKAKSVIKtldpkQNPASPPEIQALKNqllekDKKIEHLERDFEKSKLQREQEEKlivtAWYNMGM----ALHRKAIEER 502
|
490
....*....|....*.
gi 1927222988 1904 IVLLKKSSEAEMERQR 1919
Cdd:pfam05622 503 LAGLSSPGQSFLARQR 518
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2019-2480 |
1.41e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.63 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2019 ELDRLKKKAEEARKQKDDADKEAEKQIL----MAQQAAQKCS-AAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKK----L 2089
Cdd:pfam05701 78 LIEELKLNLERAQTEEAQAKQDSELAKLrveeMEQGIADEASvAAKAQLEVAKARHAAAVAELKSVKEELESLRKeyasL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2090 AKQAEAAKEKAErEAALLRQQAEeaerqkaaaeqeaanqaKAQED--AERLRKEAEFEAAKRAQAEnaalKQKQQADAEM 2167
Cdd:pfam05701 158 VSERDIAIKRAE-EAVSASKEIE-----------------KTVEEltIELIATKESLESAHAAHLE----AEEHRIGAAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2168 AK-HKKLA-EQTLKQkfqVEQELTKVKLKLDETDKQKSVLD---EELQRLKDEVDDAVKqrGQVEEELLKVKVqmeellk 2242
Cdd:pfam05701 216 AReQDKLNwEKELKQ---AEEELQRLNQQLLSAKDLKSKLEtasALLLDLKAELAAYME--SKLKEEADGEGN------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2243 lklriEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAqeaARLRqiaeDDLNQQRA-LADKMLKEKMQAIQE 2321
Cdd:pfam05701 284 -----EKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAA---ASLR----SELEKEKAeLASLRQREGMASIAV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2322 ASrLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEyqksleaerkrqleiiAESEKLKLQVSQlsEAQAKAQE 2401
Cdd:pfam05701 352 SS-LEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQE----------------AEEAKSLAQAAR--EELRKAKE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2402 EAKKFKKQADSIASRLH----ETELA-TQEKMTVV-----EKLEVARLTSSKEaDDLRKAIADLEK--EKSRLKKEAEDL 2469
Cdd:pfam05701 413 EAEQAKAAASTVESRLEavlkEIEAAkASEKLALAaikalQESESSAESTNQE-DSPRGVTLSLEEyyELSKRAHEAEEL 491
|
490
....*....|.
gi 1927222988 2470 QNKSKEMADAQ 2480
Cdd:pfam05701 492 ANKRVAEAVSQ 502
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4272-4305 |
1.43e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.43e-03
10 20 30
....*....|....*....|....*....|....
gi 1927222988 4272 EETGPIAGILDIDTLEKVSITEAIHRNLVDNISG 4305
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1798-2449 |
1.46e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1798 LEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEE-EAARQRAEAERILKEKLAAISDATRLKTeAEIALKEKEAENERLR 1876
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIELLEPiRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1877 RQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSS-------EAEMERQRAIVDDTLKQRRVVEEEIRILKLnfekassg 1949
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgdrleqlEREIERLERELEERERRRARLEALLAALGL-------- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1950 klDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAaaeeeaarqrqaaqDELDRLKK---- 2025
Cdd:COG4913 374 --PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE--------------AEIASLERrksn 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2026 ---KAEEARKQKDDADKEAEKQI-----LMaqQAAQKCSAAEQQVQSVLAQQKEDTIM-------------QTKLKEE-- 2082
Cdd:COG4913 438 ipaRLLALRDALAEALGLDEAELpfvgeLI--EVRPEEERWRGAIERVLGGFALTLLVppehyaaalrwvnRLHLRGRlv 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2083 YEKAKKLAKQAEAAKEKAEREA---------------ALLRQQ--------AEEAER------------QKAAAEQEAAN 2127
Cdd:COG4913 516 YERVRTGLPDPERPRLDPDSLAgkldfkphpfrawleAELGRRfdyvcvdsPEELRRhpraitragqvkGNGTRHEKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2128 QAKAQE-----DAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAE--QTLKQKFQVEQELTKVKLKLDETDK 2200
Cdd:COG4913 596 RRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2201 QKSVLDE---ELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNmkkLA 2277
Cdd:COG4913 676 ELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2278 EDAARLSVEAQEAARLRQIAE--DDLNQQRALADKMLKEKMQAIQ-----EASRLRAEAE-------MLQRQK--DLAqE 2341
Cdd:COG4913 753 ERFAAALGDAVERELRENLEEriDALRARLNRAEEELERAMRAFNrewpaETADLDADLEslpeylaLLDRLEedGLP-E 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2342 QAQKLledKQLMQQRLDEETEEYQKSLEAER---KRQLEIIAES---------EKLKLqvsqlsEAQAKAQEEAKKFKKQ 2409
Cdd:COG4913 832 YEERF---KELLNENSIEFVADLLSKLRRAIreiKERIDPLNDSlkripfgpgRYLRL------EARPRPDPEVREFRQE 902
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1927222988 2410 A-DSIASRLHETELATQEKMTVVEKLeVARLTSSKEADDLR 2449
Cdd:COG4913 903 LrAVTSGASLFDEELSEARFAALKRL-IERLRSEEEESDRR 942
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1484-1620 |
1.47e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1484 LKQLRDRAAEAEKLRKAAQEEAEKLRKQV------------NEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLK 1551
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAAlleakelllrerNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1552 RQAEEAERQVKQAEIE-KERQIQVAHVAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEAA 1620
Cdd:PRK12705 105 NQLEEREKALSARELElEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEA 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1232-1424 |
1.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1232 INDAKQRQEKIQAVTITDSKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLASPLKK 1311
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1312 TK---------LDSASdniIQEYVTLRTKYSELMTLTSQYIKFITDSQRRLEDEEKAAEKLKAE---EQKKMAMMQAELD 1379
Cdd:COG3883 98 SGgsvsyldvlLGSES---FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEleaLKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1927222988 1380 KQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVVDAEKQK 1424
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2075-2420 |
1.52e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.90 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2075 MQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKaaaeqeaanqakaqedaERLRKEAEFEAAKRAQAEN 2154
Cdd:pfam15964 326 AQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQK-----------------ERLEKELASQQEKRAQEKE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2155 AALKqkqqadaEMAKHKKLAEQTLkqkFQVEQELTKVKLKLDETDKQKSVLDEELQrlkdevdDAVKQRGQVEEELLKVK 2234
Cdd:pfam15964 389 ALRK-------EMKKEREELGATM---LALSQNVAQLEAQVEKVTREKNSLVSQLE-------EAQKQLASQEMDVTKVC 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2235 VQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKK----LAEDAARLSVEAQEAARLRQ----IAEDDLNQQRA 2306
Cdd:pfam15964 452 GEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKlgleLSESKQRLEQAQQDAARAREeclkLTELLGESEHQ 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2307 LadKMLKEKMQAIQEASRLRAEAEMLQrqkdlAQEQAQKLLEDKQLMQQRLDE-ETEEY-----QKSLEAERKRQLEIIA 2380
Cdd:pfam15964 532 L--HLTRLEKESIQQSFSNEAKAQALQ-----AQQREQELTQKMQQMEAQHDKtVNEQYslltsQNTFIAKLKEECCTLA 604
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1927222988 2381 E-----SEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIAS------RLHET 2420
Cdd:pfam15964 605 KkleeiTQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEqcvqhgRMHER 655
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2085-2278 |
1.62e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.47 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2085 KAKKLAKQAEAAKEKAEREAALLRQQAE-EAERQKAAaeqeaanqakAQEDAERLRKEAEFEAAKRAQaenaalKQKQQA 2163
Cdd:PRK00106 25 KMKSAKEAAELTLLNAEQEAVNLRGKAErDAEHIKKT----------AKRESKALKKELLLEAKEEAR------KYREEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2164 DAEMakhkKLAEQTLKQkfqVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQ-MEELLK 2242
Cdd:PRK00106 89 EQEF----KSERQELKQ---IESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQkKAELER 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1927222988 2243 LKLRIEEENQRLIKKDkdnTQKFLAKEADNMKKLAE 2278
Cdd:PRK00106 162 VAALSQAEAREIILAE---TENKLTHEIATRIREAE 194
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2281-2471 |
1.89e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2281 ARLSVEAQE-AARLRQIAED-DLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDL-AQEQAQKLLEDKQLMQQRL 2357
Cdd:PRK05035 460 ARLEREKAArEARHKKAAEArAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAViAAREARKAQARARQAEKQA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2358 DEETEEYQKSLEAERKR--------QLEIIAESEKLKLQVSQLSEAQAKAQeeAKKFKKQADSIASRlhETELATQEKMT 2429
Cdd:PRK05035 540 AAAADPKKAAVAAAIARakakkaaqQAANAEAEEEVDPKKAAVAAAIARAK--AKKAAQQAASAEPE--EQVAEVDPKKA 615
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1927222988 2430 VVE---------KLEVARLTSSKEADDLRKAI--ADLEKEKSRLKKEAEDLQN 2471
Cdd:PRK05035 616 AVAaaiarakakKAEQQANAEPEEPVDPRKAAvaAAIARAKARKAAQQQANAE 668
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1333-1525 |
1.91e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.83 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1333 SELMTLTSQYIKFITDS---QRRLEDEEKAAE---KLKAEEQKKMAMM---QAELDKQKQLA-----EVHAKAIaKAEKE 1398
Cdd:NF012221 1538 SESSQQADAVSKHAKQDdaaQNALADKERAEAdrqRLEQEKQQQLAAIsgsQSQLESTDQNAletngQAQRDAI-LEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1399 A--QELKLRMQEEVNRREDAVVDAEKQKH-----------NIQLELHELKNLSEQQIMDKSKQVDDALQsrvKIEEEIRl 1465
Cdd:NF012221 1617 AvtKELTTLAQGLDALDSQATYAGESGDQwrnpfagglldRVQEQLDDAKKISGKQLADAKQRHVDNQQ---KVKDAVA- 1692
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1927222988 1466 irlQLETTVKQKSTAESELKQ-LRDRAAEAEKLRKAA---QEEAEKLRKQVNEETQKKRMAEEE 1525
Cdd:NF012221 1693 ---KSEAGVAQGEQNQANAEQdIDDAKADAEKRKDDAlakQNEAQQAESDANAAANDAQSRGEQ 1753
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
32-140 |
1.92e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 44.55 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 32 LKAMDGRKDERDRVqkktFTKWVNKHLIKSQrqVTDLYEDLRDGHNLISLLEVLSGE---TLPREKGR-------MRFHK 101
Cdd:COG5069 370 IEEFDAEGEFEARV----FTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKA 443
|
90 100 110
....*....|....*....|....*....|....*....
gi 1927222988 102 LQNVQIALDFLKHRQVKLVNIRNDDIADGNpKLTLGLIW 140
Cdd:COG5069 444 FENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVW 481
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1158-1344 |
1.98e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1158 LEAELKKATAVSDKMSRVHSERDAELDHYRQLLSSLQDRWKAVFSQIDLR--QRELEQLGRQLGYYRESYDWLIRwindA 1235
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAsaEREIAELEAELERLDASSDDLAA----L 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1236 KQRQEKIQAVTITDSKTLKEQLAQEKKLLEEVEGNKDKVDECQKYAKAYIDTIKDYELQLVAykaqvEPLASPLKKTKLD 1315
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE-----ERFAAALGDAVER 765
|
170 180 190
....*....|....*....|....*....|...
gi 1927222988 1316 SASDNIIQEYVTLRTK----YSELMTLTSQYIK 1344
Cdd:COG4913 766 ELRENLEERIDALRARlnraEEELERAMRAFNR 798
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1736-2149 |
2.06e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.25 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1736 QQRSLLEDELYRLKNEV-------VAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSkQLLEVEATKM-RD 1807
Cdd:pfam05701 35 ERRKLVELELEKVQEEIpeykkqsEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDS-ELAKLRVEEMeQG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1808 LAEEAS-KLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKE-KEAEnerlrRQAEDEAYQ 1885
Cdd:pfam05701 114 IADEASvAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSAsKEIE-----KTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1886 ----RKALEDQANQHKQQIEEKIvllkkssEAEMERQRaivdDTLKQRR---VVEEEIRilKLNFEKASSGKLDLELELN 1958
Cdd:pfam05701 189 liatKESLESAHAAHLEAEEHRI-------GAALAREQ----DKLNWEKelkQAEEELQ--RLNQQLLSAKDLKSKLETA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1959 KLKniaeetqQSKLRAEEEAEKLRKLaleeekrrreaeekvKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDAD 2038
Cdd:pfam05701 256 SAL-------LLDLKAELAAYMESKL---------------KEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2039 KEAEkqiLMAQQAAQKCSAAEQQvQSVLA--QQKED--TIMQTKLKEEYEKAKK----LAKQAEAAKEKAEREAALLRQQ 2110
Cdd:pfam05701 314 DEVN---CLRVAAASLRSELEKE-KAELAslRQREGmaSIAVSSLEAELNRTKSeialVQAKEKEAREKMVELPKQLQQA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1927222988 2111 AEEAERQKAAAEQEAANQAKAQEDAERLRK-----EAEFEAAKR 2149
Cdd:pfam05701 390 AQEAEEAKSLAQAAREELRKAKEEAEQAKAaastvESRLEAVLK 433
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2274-2573 |
2.06e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2274 KKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLM 2353
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2354 QQRLD---EETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETE-----LATQ 2425
Cdd:COG4372 100 QEELEslqEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEqelqaLSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2426 EKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKK 2505
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 2506 EKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEM 2573
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2332-2608 |
2.11e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.29 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2332 LQRQKDLAQEQAQKLLEDKQLMQQRLDEeTEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQAD 2411
Cdd:pfam05622 19 LDQQVSLLQEEKNSLQQENKKLQERLDQ-LESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2412 SIASRLHETELATQEKMTVVEKLEVARLTSSKeaddlrkaIADLEKEKSRLKKEAEDLQNKSKEMadaqqKQIEHEKTV- 2490
Cdd:pfam05622 98 ELQHRNEELTSLAEEAQALKDEMDILRESSDK--------VKKLEATVETYKKKLEDLGDLRRQV-----KLLEERNAEy 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2491 LQQTFlsekemllkkeklieeekkrlesQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMdaalNKQKEAEKEMHNKQ 2570
Cdd:pfam05622 165 MQRTL-----------------------QLEEELKKANALRGQLETYKRQVQELHGKLSEES----KKADKLEFEYKKLE 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 1927222988 2571 KEMKELERkrlEQERILAEENQkLREKLQQLEEAQKDQ 2608
Cdd:pfam05622 218 EKLEALQK---EKERLIIERDT-LRETNEELRCAQLQQ 251
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2272-2482 |
2.22e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.82 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2272 NMKKLAEDAARlsvEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQE-----------ASRLRAEAEMLQRQKDLAQ 2340
Cdd:PRK07735 6 DLEDLKKEAAR---RAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDdmtieeakrraAAAAKAKAAALAKQKREGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2341 EQAQKllEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHET 2420
Cdd:PRK07735 83 EEVTE--EEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEET 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1927222988 2421 ELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQK 2482
Cdd:PRK07735 161 DKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQK 222
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2212-2611 |
2.23e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2212 LKDEVDDAVKQRGQVEEELLKVKVQMEELLK---LKLRIEEENQRLIKKDKD-NTQKFLAKEADNMKKLAEDAARLSVEA 2287
Cdd:pfam12128 198 VKSMIVAILEDDGVVPPKSRLNRQQVEHWIRdiqAIAGIMKIRPEFTKLQQEfNTLESAELRLSHLHFGYKSDETLIASR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2288 QEAarlRQIAEDDLNQQRALADKMLKEKMQAI-QEASRLRAEAEMLQRQKDLAQEQAQklledkqlmqQRLDEETEEYQK 2366
Cdd:pfam12128 278 QEE---RQETSAELNQLLRTLDDQWKEKRDELnGELSAADAAVAKDRSELEALEDQHG----------AFLDADIETAAA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2367 SLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHEtelatqekmtvveklevaRLTSSKEAD 2446
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKD------------------KLAKIREAR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2447 DLRKAIA--DLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKR--LESQFEE 2522
Cdd:pfam12128 407 DRQLAVAedDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAReeQEAANAE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2523 ------EVKKAKALKDEQER---------QKQQMEDEKKKLQ-----ATMDAALNKQKEAEKEMHNKQKEMKELERK--- 2579
Cdd:pfam12128 487 verlqsELRQARKRRDQASEalrqasrrlEERQSALDELELQlfpqaGTLLHFLRKEAPDWEQSIGKVISPELLHRTdld 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1927222988 2580 -----------------RLEQERILAEE----NQKLREKLQQLEEAQKDQPDK 2611
Cdd:pfam12128 567 pevwdgsvggelnlygvKLDLKRIDVPEwaasEEELRERLDKAEEALQSAREK 619
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1350-1568 |
2.24e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.68 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1350 QRRLEDEEKAAEKLKAEEQKKMAMMQ-AELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEVNRREDAVvdAEKQKhniq 1428
Cdd:TIGR02794 71 KKLEQQAEEAEKQRAAEQARQKELEQrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAE--AERKA---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1429 lelhelknlseqqimdkskqvddALQSRVKIEEEirliRLQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEE---- 1504
Cdd:TIGR02794 145 -----------------------KEEAAKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakak 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 1505 AEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDL--ENLKRQAEEAERQVKQAEIEK 1568
Cdd:TIGR02794 198 AEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLasGSNAEKQGGARGAAAGSEVDK 263
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2286-2468 |
2.33e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.84 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2286 EAQEAARLRQIAEDDLNQQRALADKmlkekmqAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQ 2365
Cdd:pfam05262 207 ESQEDAKRAQQLKEELDKKQIDADK-------AQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2366 KSlEAERKRQleiiaeseklklqvsqlsEAQaKAQEEAKKFKKQADSIASRlhetELATQEKMTVVEKLEvARLTSSKEA 2445
Cdd:pfam05262 280 KR-EIEKAQI------------------EIK-KNDEEALKAKDHKAFDLKQ----ESKASEKEAEDKELE-AQKKREPVA 334
|
170 180
....*....|....*....|...
gi 1927222988 2446 DDLRKAIADLEKEKSRLKKEAED 2468
Cdd:pfam05262 335 EDLQKTKPQVEAQPTSLNEDAID 357
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2347-2586 |
2.36e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 43.86 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2347 LEDKQLMQQRLD---EETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELA 2423
Cdd:pfam05701 34 VERRKLVELELEkvqEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2424 TQEKMTVVEK--LEVAR---------LTSSK-EADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMadaqQKQIEH---EK 2488
Cdd:pfam05701 114 IADEASVAAKaqLEVAKarhaaavaeLKSVKeELESLRKEYASLVSERDIAIKRAEEAVSASKEI----EKTVEEltiEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2489 TVLQQTFLS---------EKEMLLKKEKLIEEEKKRLE-SQFEEEVKK-------AKALKDEQERQKQQMEDEKKKLQAT 2551
Cdd:pfam05701 190 IATKESLESahaahleaeEHRIGAALAREQDKLNWEKElKQAEEELQRlnqqllsAKDLKSKLETASALLLDLKAELAAY 269
|
250 260 270
....*....|....*....|....*....|....*...
gi 1927222988 2552 MDAALNK---QKEAEKEMHNKQKEMKELERKRLEQERI 2586
Cdd:pfam05701 270 MESKLKEeadGEGNEKKTSTSIQAALASAKKELEEVKA 307
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2309-2629 |
2.38e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.98 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2309 DKMLKEKMQAIQEASRLRAEAE-----MLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESE 2383
Cdd:pfam09731 84 EEKKQVKIPRQSGVSSEVAEEEkeatkDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2384 KLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSrlk 2463
Cdd:pfam09731 164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQS--- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2464 kEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEE------------EKKRLESQFEEEVKKAKALK 2531
Cdd:pfam09731 241 -LAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSliahahreidqlSKKLAELKKREEKHIERALE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2532 DEQERQKQQMEDEKKKLQATMDAALNK-QKEAEKEMHNKQKEMKELERKRLEQERILAEEnqKLREKLQQLEEAQKDQPD 2610
Cdd:pfam09731 320 KQKEELDKLAEELSARLEEVRAADEAQlRLEFEREREEIRESYEEKLRTELERQAEAHEE--HLKDVLVEQEIELQREFL 397
|
330
....*....|....*....
gi 1927222988 2611 KEVIhvTMVETTKNVYNGQ 2629
Cdd:pfam09731 398 QDIK--EKVEEERAGRLLK 414
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1913-2472 |
2.40e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1913 AEMERQRAIVDDTLKQRRVVEEeIRILKLNFEKASSGKLDLELELNKLKniAEETQQSKLRAEEEAEKLRKlaleeekrr 1992
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRA--------- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1993 reaeekvkKIAAAEEEAArqrqAAQDELDRLKKKAEEARKQKDDAD----KEAEKQILMAQQAAQKCSAAEQQVQSVLAQ 2068
Cdd:COG4913 303 --------ELARLEAELE----RLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2069 QKEdtimqtKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKaaaeqeaanqAKAQEDAERLRKE------- 2141
Cdd:COG4913 371 LGL------PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL----------RDLRRELRELEAEiaslerr 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2142 -----AEFEAAKRAQAENAALKQKQ-------------QADAEMA----------------KHKKLA----EQT-LKQKF 2182
Cdd:COG4913 435 ksnipARLLALRDALAEALGLDEAElpfvgelievrpeEERWRGAiervlggfaltllvppEHYAAAlrwvNRLhLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2183 QVEQELTKVKLKLDETDKQKSVLDE---ELQRLKDEVDDAVKQRGQV-----EEELLKVK--VQMEELLKLKLRIEEEN- 2251
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDSLAGKldfKPHPFRAWLEAELGRRFDYvcvdsPEELRRHPraITRAGQVKGNGTRHEKDd 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2252 QRLIKKD----KDNTQKFLAKEADnmkkLAEDAARLSVEAQEAARLRQIAEDDLNQQRALadkmlkekmQAIQEASRLRA 2327
Cdd:COG4913 595 RRRIRSRyvlgFDNRAKLAALEAE----LAELEEELAEAEERLEALEAELDALQERREAL---------QRLAEYSWDEI 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2328 EAEMLQRQKDLAQEQAQKLLEDKQLMQQrLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAkkfk 2407
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---- 736
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 2408 KQADSIASRLHETELATQEKMTVVEKLEvarltsSKEADDLRKAIADLEKEKSRLKKEAEDLQNK 2472
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVE------RELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2075-2348 |
2.44e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.82 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2075 MQTKLKEEYEKAKKLAKQAEAAKEKAEReaALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAEN 2154
Cdd:PRK07735 7 LEDLKKEAARRAKEEARKRLVAKHGAEI--SKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2155 A-----ALKQKQQADAEMAKHKKLAEQTLKQKFQV-EQELTKVKLKLDETDKQKSvldEELQRLKDEVDDAVKQRGQVEE 2228
Cdd:PRK07735 85 VteeekAKAKAKAAAAAKAKAAALAKQKREGTEEVtEEEKAAAKAKAAAAAKAKA---AALAKQKREGTEEVTEEEEETD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2229 ELL-------KVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKflAKEADNMKKLAEDAARlsveaQEAARLRQIAEDDL 2301
Cdd:PRK07735 162 KEKakakaaaAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAK--AKAAAAAKAKAAALAK-----QKASQGNGDSGDED 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1927222988 2302 NQQRALAdkMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLE 2348
Cdd:PRK07735 235 AKAKAIA--AAKAKAAAAARAKTKGAEGKKEEEPKQEEPSVNQPYLN 279
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1551-1846 |
2.56e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.37 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1551 KRQAEEAERQVKQAeIEKERQIQVAHVAAQKSAAAELQsKHMSFVEKTSKLEESLKQEHGavLQLQHEAAALKKQQEDAE 1630
Cdd:pfam13868 43 RRLDEMMEEERERA-LEEEEEKEEERKEERKRYRQELE-EQIEEREQKRQEEYEEKLQER--EQMDEIVERIQEEDQAEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1631 RAREEAEKELEKWRQKANEALRLRLQAEEEAHKK---SLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQR 1707
Cdd:pfam13868 119 EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREedeRILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1708 KVAESTAQ-QKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDELAKVRSEMdvLIQLKSKAEKE 1786
Cdd:pfam13868 199 EKAERDELrAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFER--MLRKQAEDEEI 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 1787 TMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQR-----AEAERILKE 1846
Cdd:pfam13868 277 EQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERrerieEERQKKLKE 341
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2287-2612 |
2.60e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2287 AQEAARLRQIAEDDLNQQRALADKmlKEKMQAIQEA-SRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQ--RLDEETEE 2363
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTS--RRQLAAEQYRlVEMARELAELNEAESDLEQDYQAASDHLNLVQTalRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2364 YQKSLEaERKRQLEiiAESEKLKLQVSQLSEAQAK---AQEEAKKFKKQ-ADsiasrlhetelatqekmtVVEKLEVARl 2439
Cdd:PRK04863 353 YQADLE-ELEERLE--EQNEVVEEADEQQEENEARaeaAEEEVDELKSQlAD------------------YQQALDVQQ- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2440 tssKEADDLRKAIADLEKEKSRLKKEAEDLQNKSK--EMADAQQKQIEHEKTVLQQTfLSEKEMLLkkeklieeekkrle 2517
Cdd:PRK04863 411 ---TRAIQYQQAVQALERAKQLCGLPDLTADNAEDwlEEFQAKEQEATEELLSLEQK-LSVAQAAH-------------- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2518 SQFEEEVKKAKALKDEQERqkqqmEDEKKKLQATMDAALNKQKEAEKE--MHNKQKEMKELERKRLEQERILAEENQKLR 2595
Cdd:PRK04863 473 SQFEQAYQLVRKIAGEVSR-----SEAWDVARELLRRLREQRHLAEQLqqLRMRLSELEQRLRQQQRAERLLAEFCKRLG 547
|
330
....*....|....*..
gi 1927222988 2596 EKLQQLEEAQKDQPDKE 2612
Cdd:PRK04863 548 KNLDDEDELEQLQEELE 564
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1794-1980 |
2.77e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1794 SKQLLEVEATKMRDLAEEASKLRAIAEEAKHQrqvAEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENE 1873
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLE---AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1874 RLRRQAEDEAYQRKALEDQANQHKQQIEEKIvllkKSSEAEMERQRAIVDDTLKQR--RVVEEEIRIlklnfEKASsgkl 1951
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELI----EEQLQELERISGLTAEEAKEIllEKVEEEARH-----EAAV---- 173
|
170 180
....*....|....*....|....*....
gi 1927222988 1952 dlelelnKLKNIAEEtqqsklrAEEEAEK 1980
Cdd:PRK12704 174 -------LIKEIEEE-------AKEEADK 188
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1963-2309 |
2.82e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1963 IAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAE 2042
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2043 KQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAE 2122
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2123 QEAANQAKAQEDAERLRKEAEFEAAKRAQAENAalKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQK 2202
Cdd:COG4372 164 EELAALEQELQALSEAEAEQALDELLKEANRNA--EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2203 SVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAAR 2282
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
330 340
....*....|....*....|....*..
gi 1927222988 2283 LSVEAQEAARLRQIAEDDLNQQRALAD 2309
Cdd:COG4372 322 LELAKKLELALAILLAELADLLQLLLV 348
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1499-2246 |
2.86e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1499 KAAQEEAEKLRKQV------NEETQKKRMAEEELKRKAEAEKEAAK-QKQKALEDLENlkrQAEEAERQVKQAEIEKERq 1571
Cdd:COG4913 238 ERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLwFAQRRLELLEA---ELEELRAELARLEAELER- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1572 iqvaHVAAQKSAAAELQSkhmsfvektskLEESLKQEHGAVLQlqheaaALKKQqedaerareeaekeLEKWRQKANEAL 1651
Cdd:COG4913 314 ----LEARLDALREELDE-----------LEAQIRGNGGDRLE------QLERE--------------IERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1652 RLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKvaestaqqklTAEQELIRLRADF 1731
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR----------DLRRELRELEAEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1732 DNAEQQRSLLEDELyrlknevvaaQQQRKQLEDELAKVRSEMDV---LIQLKSKAEKETMS--------------NSERS 1794
Cdd:COG4913 429 ASLERRKSNIPARL----------LALRDALAEALGLDEAELPFvgeLIEVRPEEERWRGAiervlggfaltllvPPEHY 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1795 KQLLE-VEATKMRdlaeeaskLRAIAEEAKHQRQVAEEEAARQRAEAERI----------LKEKLAAISDATRLKTEAEI 1863
Cdd:COG4913 499 AAALRwVNRLHLR--------GRLVYERVRTGLPDPERPRLDPDSLAGKLdfkphpfrawLEAELGRRFDYVCVDSPEEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1864 A-----------LKEKEAENERLRRQAEDEAY--------QRKALEDQAnqhkQQIEEKIVLLkkssEAEMERQRAIVDD 1924
Cdd:COG4913 571 RrhpraitragqVKGNGTRHEKDDRRRIRSRYvlgfdnraKLAALEAEL----AELEEELAEA----EERLEALEAELDA 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1925 TLKQRRVVEeeiRILKLNFEKASSGKLDLELElnklkniaeetqqsklRAEEEAEKLRKlaleeekrrreaeekvkkiaa 2004
Cdd:COG4913 643 LQERREALQ---RLAEYSWDEIDVASAEREIA----------------ELEAELERLDA--------------------- 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2005 aeeeaarqrqaAQDELDRLKKKAEEARKQKDDADKEAEkqilmaqQAAQKCSAAEQQVQSVLAQQKEdtimqtkLKEEYE 2084
Cdd:COG4913 683 -----------SSDDLAALEEQLEELEAELEELEEELD-------ELKGEIGRLEKELEQAEEELDE-------LQDRLE 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2085 KAKKLAKQAEAAkekaerEAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAE--FEAAKRAQAENAALKQKQQ 2162
Cdd:COG4913 738 AAEDLARLELRA------LLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELEraMRAFNREWPAETADLDADL 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2163 ADAE--MAKHKKLAEQTL---KQKFQveqeltkvKLKLDETDKQKSVLdeeLQRLKDEVDDAVKQRGQVEEELLKVKVQM 2237
Cdd:COG4913 812 ESLPeyLALLDRLEEDGLpeyEERFK--------ELLNENSIEFVADL---LSKLRRAIREIKERIDPLNDSLKRIPFGP 880
|
....*....
gi 1927222988 2238 EELLKLKLR 2246
Cdd:COG4913 881 GRYLRLEAR 889
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2517-2611 |
2.87e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2517 ESQFEEEVKKAKAL---KDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAEENQK 2593
Cdd:PRK12704 46 EAKKEAEAIKKEALleaKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE 125
|
90
....*....|....*...
gi 1927222988 2594 LREKLQQLEEAQKDQPDK 2611
Cdd:PRK12704 126 LEKKEEELEELIEEQLQE 143
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1350-1571 |
2.89e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.37 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1350 QRRLEDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKLRMQEEV---NRREDAVVDAEKQKHN 1426
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKlqeREQMDEIVERIQEEDQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1427 IQLELHELKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLRDRAA-EAEKLRKAAQEEA 1505
Cdd:pfam13868 116 AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEkEREIARLRAQQEK 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 1506 EKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKERQ 1571
Cdd:pfam13868 196 AQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEE 261
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2075-2423 |
2.89e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2075 MQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAEN 2154
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2155 AALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVK 2234
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2235 VQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEAARLRQ--IAEDDLNQQRALADKML 2312
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALldALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2313 KEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQL 2392
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
330 340 350
....*....|....*....|....*....|.
gi 1927222988 2393 SEAQAKAQEEAKKFKKQADSIASRLHETELA 2423
Cdd:COG4372 338 ELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2334-2661 |
2.97e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2334 RQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSI 2413
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2414 ASRLHETELATQEKMTVVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQ-QKQIEHEKTVLQ 2492
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALDELLKEAN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2493 QTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKE 2572
Cdd:COG4372 194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2573 MKELERKRLEQERILAEENQKLREKLQQLEEAQKDQPDKEVIHVTMVETTKNVYNGQNVGDVVDSAEKKPDPLAFNGIRE 2652
Cdd:COG4372 274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDN 353
|
....*....
gi 1927222988 2653 KVPASRLHD 2661
Cdd:COG4372 354 DVLELLSKG 362
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
950-1523 |
2.98e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.27 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 950 DDRMQIEEDYTKSTQHFDSLIRSMEKglmvVRHKGQqdetlckNYLSEIKdlrLRIEDCEAGTVARIRRPVEKEPLKECV 1029
Cdd:TIGR01612 1111 DEINKIKDDIKNLDQKIDHHIKALEE----IKKKSE-------NYIDEIK---AQINDLEDVADKAISNDDPEEIEKKIE 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1030 QKTTEQKKVQVELEGLKKDLNKVSAKTKEvlaspqQTASAPVLRSeldltveKMDHTHMLSSVYLEKLKtvemviRNTQG 1109
Cdd:TIGR01612 1177 NIVTKIDKKKNIYDEIKKLLNEIAEIEKD------KTSLEEVKGI-------NLSYGKNLGKLFLEKID------EEKKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1110 AEGVLKQYEDCLREVHTVPNDVKEVETYRTKLKKMRAEAEgeqpVFDSLEAELKKATAVSDKMSRVHSE-RDAEL----D 1184
Cdd:TIGR01612 1238 SEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEME----TFNISHDDDKDHHIISKKHDENISDiREKSLkiieD 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1185 HYRQllSSLQDRWKAVFSQIDLRQRELEQLGRQLGYYRESYDWLI-----RWINDAKQRQEKIQavtiTDSKTLKEQLAQ 1259
Cdd:TIGR01612 1314 FSEE--SDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKlnkikKIIDEVKEYTKEIE----ENNKNIKDELDK 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1260 EKKLLEEVEGNKDkVDECQKYAKAYIDTiKDYELQLVAYKAQVEPLASplKKTKLDSASDNIIQ--EYVTLRTKYSELMT 1337
Cdd:TIGR01612 1388 SEKLIKKIKDDIN-LEECKSKIESTLDD-KDIDECIKKIKELKNHILS--EESNIDTYFKNADEnnENVLLLFKNIEMAD 1463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1338 LTSQYI-------------------KFITDSQRRLEDE----EKAAEKLKA--EEQKKMAM----------MQAELDKQK 1382
Cdd:TIGR01612 1464 NKSQHIlkikkdnatndhdfninelKEHIDKSKGCKDEadknAKAIEKNKElfEQYKKDVTellnkysalaIKNKFAKTK 1543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1383 --------QLAEVHAKAIAKAEKEAQELKlRMQEEVNRREDAVVDAEKQKH---NIQLELHELKNlSEQQIMDKSKQVDD 1451
Cdd:TIGR01612 1544 kdseiiikEIKDAHKKFILEAEKSEQKIK-EIKKEKFRIEDDAAKNDKSNKaaiDIQLSLENFEN-KFLKISDIKKKIND 1621
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1927222988 1452 ALQSRVKIEEEIRLIRL-----QLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAE 1523
Cdd:TIGR01612 1622 CLKETESIEKKISSFSIdsqdtELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYE 1698
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
810-854 |
3.15e-03 |
|
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212702 [Multi-domain] Cd Length: 54 Bit Score: 38.41 E-value: 3.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1927222988 810 IQAVCDFK---QQEITVHKGDECALLNNSQPFKWKVLNRSGHEAVVPS 854
Cdd:cd11768 2 VVALYDFQpiePGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
972-1511 |
3.25e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 972 SMEKGLMVVRHKGQQDETLCKNYLSEIKDL--RLRIEDCEAgtvARIRRPVEKEPLKECVQKTTEQKKVQVELEGLKKDL 1049
Cdd:pfam15921 296 SIQSQLEIIQEQARNQNSMYMRQLSDLESTvsQLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERDQFSQES 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1050 NKVSAKTKEVLASpqqtasapVLRSELDLTVEKMDHTHML-----SSVYLEKLKTvEMVIRN--TQGAEGVLKQYE-DCL 1121
Cdd:pfam15921 373 GNLDDQLQKLLAD--------LHKREKELSLEKEQNKRLWdrdtgNSITIDHLRR-ELDDRNmeVQRLEALLKAMKsECQ 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1122 REVHTVPNDVKEVETYRTKLKKMRAEAEGEQPVFDSLEAELKKATAVSDKMSRVHSERDAELDHYRQLLSSLQDRWKAVF 1201
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLR 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1202 SQIDLRQRELEQLgrqlgyyresydwlirwindaKQRQEKIQAVTiTDSKTLKEQLAQEKKLLE----------EVEGNK 1271
Cdd:pfam15921 524 SRVDLKLQELQHL---------------------KNEGDHLRNVQ-TECEALKLQMAEKDKVIEilrqqienmtQLVGQH 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1272 DKVDECQKYAKAYIDT-IKDYELQLVAYK-------AQVEPLAS-----PLKKTKLDSASD-------NIIQEYVTL--- 1328
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKeINDRRLELQEFKilkdkkdAKIRELEArvsdlELEKVKLVNAGSerlravkDIKQERDQLlne 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1329 -RTKYSELMTLTSQYIKFITDSQRRLEDEEKAAEKLKAEeqkkMAMMQAELDKQKQLaevhAKAIAKAEKEAQELKLRMQ 1407
Cdd:pfam15921 662 vKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ----LKSAQSELEQTRNT----LKSMEGSDGHAMKVAMGMQ 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1408 EEVNRR--------------EDAVVDAEKQKHNIQLELHELknlseqqimdkSKQVDDALQSRVKIEEEIRLIRLQlETT 1473
Cdd:pfam15921 734 KQITAKrgqidalqskiqflEEAMTNANKEKHFLKEEKNKL-----------SQELSTVATEKNKMAGELEVLRSQ-ERR 801
|
570 580 590
....*....|....*....|....*....|....*....
gi 1927222988 1474 VKQK-STAESELKQLRDRAAEAEKLRKAAQEEAEKLRKQ 1511
Cdd:pfam15921 802 LKEKvANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2370-2600 |
3.32e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2370 AERKRQLEI----IAESEK-LKLQVSQLSE--AQAKAQEeakkfkkQADSIASR-LHETelatQEKMTVVEKlEVARLTS 2441
Cdd:PRK11637 43 SDNRDQLKSiqqdIAAKEKsVRQQQQQRASllAQLKKQE-------EAISQASRkLRET----QNTLNQLNK-QIDELNA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2442 SkeaddlrkaIADLEKEKSRLKK----------------------EAEDLQNKSKEMA------DAQQKQIEHektvLQQ 2493
Cdd:PRK11637 111 S---------IAKLEQQQAAQERllaaqldaafrqgehtglqlilSGEESQRGERILAyfgylnQARQETIAE----LKQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2494 TflsEKEMLLKkeklieeekkrlESQFEEEVKKAKALKDEQERQKQQME---DEKKKLQATMDAALNKQKEAEKEMHNKQ 2570
Cdd:PRK11637 178 T---REELAAQ------------KAELEEKQSQQKTLLYEQQAQQQKLEqarNERKKTLTGLESSLQKDQQQLSELRANE 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 1927222988 2571 KEMK------ELERK-RLEQErilAEENQKLREKLQQ 2600
Cdd:PRK11637 243 SRLRdsiaraEREAKaRAERE---AREAARVRDKQKQ 276
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2026-2178 |
3.39e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.36 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2026 KAEEARKQKDDADKEAEKQIlmaqqaaqkcSAAEQQVQSVLAQQKEdtiMQTKLKEEYEKAKKLAKQAEAAKEKAEREAA 2105
Cdd:pfam04012 19 KAEDPEKMLEQAIRDMQSEL----------VKARQALAQTIARQKQ---LERRLEQQTEQAKKLEEKAQAALTKGNEELA 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222988 2106 llRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAEnaALKQKQQADAEMAKHKKLAEQTL 2178
Cdd:pfam04012 86 --REALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLK--AKKNLLKARLKAAKAQEAVQTSL 154
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2239-2404 |
3.45e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.85 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2239 ELLKLKLRIEEENQRlikkdkdntQKFLAKEADNMKKLAEDAARlsVEAQEAARLRQIaeddlnqqraladkmlkeKMQA 2318
Cdd:PTZ00491 684 ERQKMHDKAKAEEQR---------TKLLELQAESAAVESSGQSR--AEALAEAEARLI------------------EAEA 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2319 IQEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQlmQQRLDEeteeyqksLEAERKRQLEIIaESEKLKLQVSQLS----E 2394
Cdd:PTZ00491 735 EVEQAELRAKALRIEAEAELEKLRKRQELELEY--EQAQNE--------LEIAKAKELADI-EATKFERIVEALGretlI 803
|
170
....*....|
gi 1927222988 2395 AQAKAQEEAK 2404
Cdd:PTZ00491 804 AIARAGPELQ 813
|
|
| SH3_Eps8 |
cd11764 |
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ... |
819-854 |
3.65e-03 |
|
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar proteins; This group is composed of Eps8 and Eps8-like proteins including Eps8-like 1-3, among others. These proteins contain N-terminal Phosphotyrosine-binding (PTB), central SH3, and C-terminal effector domains. Eps8 binds either Abi1 (also called E3b1) or Rab5 GTPase activating protein RN-tre through its SH3 domain. With Abi1 and Sos1, it becomes part of a trimeric complex that is required to activate Rac. Together with RN-tre, it inhibits the internalization of EGFR. The SH3 domains of Eps8 and similar proteins recognize peptides containing a PxxDY motif, instead of the classical PxxP motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212698 [Multi-domain] Cd Length: 54 Bit Score: 38.40 E-value: 3.65e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1927222988 819 QEITVHKGDECALLNNSQPFkWKVLNRSGHEAVVPS 854
Cdd:cd11764 14 KELSVLKGEYLEVLDDSRQW-WKVRNSRGQVGYVPH 48
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4382-4419 |
3.67e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.67e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1927222988 4382 QRFLEIQYLTGGLIEPDVEGRVSLDESIRKGTIDARTA 4419
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
996-1558 |
3.70e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 996 SEIKDLRLRIEDCEAgtvariRRPVEKEPLKECVQKTTEQKKVQVELEGLKKDLNKVSAkTKEVLASPQQTASAPVlrSE 1075
Cdd:PRK02224 213 SELAELDEEIERYEE------QREQARETRDEADEVLEEHEERREELETLEAEIEDLRE-TIAETEREREELAEEV--RD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1076 LDLTVEKM--DHTHMLSSVYLEKL--KTVEMVIRNTQGAEgvlKQYEDCLREVHTVPNDV-KEVETYRTKLKKMRAEAEG 1150
Cdd:PRK02224 284 LRERLEELeeERDDLLAEAGLDDAdaEAVEARREELEDRD---EELRDRLEECRVAAQAHnEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1151 EQPVFDSLEAELKKA-TAVSDKMSRVhserdAELDhyrqllsslqdrwkavfSQIDLRQRELEQLGRQLGYYRESYDWLI 1229
Cdd:PRK02224 361 LREEAAELESELEEArEAVEDRREEI-----EELE-----------------EEIEELRERFGDAPVDLGNAEDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1230 RWINDAKQRQEKIQAvtitDSKTLKEQLAQEKKLLEEvegnkDKVDECQKYAK--AYIDTIKDYELQLVAYKAQVEPLAS 1307
Cdd:PRK02224 419 EERDELREREAELEA----TLRTARERVEEAEALLEA-----GKCPECGQPVEgsPHVETIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1308 PLKK--TKLDSASDNIIQE--YVTLRTKYSELMTLTSQYIKFITDSQRRLEDEEKAAEKLKAEEQKKmammQAELDKQKQ 1383
Cdd:PRK02224 490 EVEEveERLERAEDLVEAEdrIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK----REAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1384 LAEVHAKAIAKAEKEAQELKLRMqEEVNRREDAVVDAEKQKHNIQLELHELKNLSEQQimDKSKQVDDALQSRVKieeei 1463
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELN--DERRERLAEKRERKR----- 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1464 rlirlQLETTVKqkstaESELKQLRDRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRkAEAEKEAAKQKQKA 1543
Cdd:PRK02224 638 -----ELEAEFD-----EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE-LEELRERREALENR 706
|
570
....*....|....*
gi 1927222988 1544 LEDLENLKRQAEEAE 1558
Cdd:PRK02224 707 VEALEALYDEAEELE 721
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3057-3089 |
3.71e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.71e-03
10 20 30
....*....|....*....|....*....|...
gi 1927222988 3057 LEAQAGTGYVVDPVDNKKYTVDEAVKAGVVGPE 3089
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2178-2624 |
3.90e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2178 LKQKFQVEQ-ELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIK 2256
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2257 KDKDNTQkflakeadnMKKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLK----------EKMQAIQEASRLR 2326
Cdd:PRK01156 268 ELEKNNY---------YKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSnidaeinkyhAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2327 AEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLdEETEEYQKSLEAERKRQLEIIAE-SEKLKLQ-------VSQLSEAQAK 2398
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMDYNSYL-KSIESLKKKIEEYSKNIERMSAFiSEILKIQeidpdaiKKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2399 AQEEAKKFKKQADSIASrLHETELATQEKMTVVEKLEVARLTSSKEADD-LRKAIADLEKEKSRLKKEAEDLQNKSKEMA 2477
Cdd:PRK01156 418 LQDISSKVSSLNQRIRA-LRENLDELSRNMEMLNGQSVCPVCGTTLGEEkSNHIINHYNEKKSRLEEKIREIEIEVKDID 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2478 DAQQKQI---------EHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKL 2548
Cdd:PRK01156 497 EKIVDLKkrkeyleseEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAV 576
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 2549 QATMDAALNKQK--EAEKEMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEEAQKDQPDKEVIHVTMVETTKN 2624
Cdd:PRK01156 577 ISLIDIETNRSRsnEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDN 654
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1409-1749 |
3.92e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1409 EVNRREDAVVDAEKQKHNIQLELHELKNLSEQQIMDKSKQVDDALQSRVKIEEEIRLIRLQLETTVKQKSTAESELKQLR 1488
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1489 DRAAEAEKLRKAAQEEAEKLRKQVNEETQKKRMAEEELKRkaeaekeaakqkqkaLEDLENL----KRQAEEAERQVKQA 1564
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEER---------------EEDERILeylkEKAEREEEREAERE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1565 EIEKERQIQVAHVAAQKSAAAELQSkhmsfvektskleeslkqehgavlqlQHEAAALKKQQEDAERAREEAEKELEKWR 1644
Cdd:pfam13868 177 EIEEEKEREIARLRAQQEKAQDEKA--------------------------ERDELRAKLYQEEQERKERQKEREEAEKK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1645 QKANEALRLRLQAEEEAHKKSLAqedAEKQKEEAEREAKKRAKAEDsalKQKEMAENELERQRKVAESTAQQKLTAEQEL 1724
Cdd:pfam13868 231 ARQRQELQQAREEQIELKERRLA---EEAEREEEEFERMLRKQAED---EEIEQEEAEKRRMKRLEHRRELEKQIEEREE 304
|
330 340
....*....|....*....|....*
gi 1927222988 1725 IRLRADFDNAEQQRSLLEDELYRLK 1749
Cdd:pfam13868 305 QRAAEREEELEEGERLREEEAERRE 329
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2440-2562 |
3.95e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2440 TSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEmllkKEKLIEEEKKRLESQ 2519
Cdd:COG0542 408 SKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKE----LIEEIQELKEELEQR 483
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 2520 FEEEVKKAKALKDEQERQKQQ----------------------------MEDEKKKLQaTMDAALNK----QKEA 2562
Cdd:COG0542 484 YGKIPELEKELAELEEELAELapllreevteediaevvsrwtgipvgklLEGEREKLL-NLEEELHErvigQDEA 557
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1597-1730 |
4.00e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1597 KTSKLEESLKQEHGAVLQLQHEAAALKKQQEDAERAREEaekeLEKWRQKANEALRLRLQAEEEAHKKSlAQED---AEK 1673
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDN----ADKQRDEVRQKQQEAKNLPKPADTSS-PKEDkqvAEN 278
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 1674 QKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQK-LTAEQELIRLRAD 1730
Cdd:pfam05262 279 QKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKeLEAQKKREPVAED 336
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2529-2608 |
4.07e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2529 ALKDEQERQKQQMEDEKKKLQatmdaaLNKQKEAEKEMHNKQKEMKELER-KRLEQERILAEENQKLREKLQQLEEAQKD 2607
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEE------QRKKKEQQQAEELQQKQAAEQERlKQLEKERLAAQEQKKQAEEAAKQAALKQK 132
|
.
gi 1927222988 2608 Q 2608
Cdd:PRK09510 133 Q 133
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1748-2089 |
4.26e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1748 LKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETmsnsERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQ 1827
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1828 VAEEEAARQRAEAERILKEKLAAISDATRLK---TEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQHKQQIEEKI 1904
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEaqiAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1905 VLLKKSSEAEMERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKL 1984
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1985 ALEEEKRRREAEEKVKKIAAAEEEAARQRQAAQDELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQS 2064
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
330 340
....*....|....*....|....*
gi 1927222988 2065 VLAQQKEDTIMQTKLKEEYEKAKKL 2089
Cdd:COG4372 345 LLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1657-1904 |
4.41e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1657 AEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELirlrADFDNAEQ 1736
Cdd:PRK07735 18 AKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEV----TEEEKAKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1737 QRSLLEDELYR---LKNEVVAAQQQRKQLEDELAKVRSEMDVLIQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEAS 1813
Cdd:PRK07735 94 KAKAAAAAKAKaaaLAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1814 KLRAIA---EEAKHQRQ----VAEEEAARQRAEAERILKEKLAAI-----------SDATRLKTEAEIALKEKEAENERL 1875
Cdd:PRK07735 174 KAKAAAlakQKAAEAGEgteeVTEEEKAKAKAKAAAAAKAKAAALakqkasqgngdSGDEDAKAKAIAAAKAKAAAAARA 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 1927222988 1876 RRQA-----EDEAYQRKALEDQA--NQHKQQIEEKI 1904
Cdd:PRK07735 254 KTKGaegkkEEEPKQEEPSVNQPylNKYVEVIKEKL 289
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2300-2472 |
4.45e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2300 DLNQQRALAD--KMLKEKMQAIQEASRLRAEAEMLQRQKDLAQ---EQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKR 2374
Cdd:COG1579 2 MPEDLRALLDlqELDSELDRLEHRLKELPAELAELEDELAALEarlEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2375 QLEIIA--ESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETElatqekmtvvEKLEVARLTSSKEADDLRKAI 2452
Cdd:COG1579 82 LGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE----------AELAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|
gi 1927222988 2453 ADLEKEKSRLKKEAEDLQNK 2472
Cdd:COG1579 152 AELEAELEELEAEREELAAK 171
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1806-1929 |
4.50e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1806 RDLAEEASKLRAIAEEAKHQRQVAEEEAARQRAEAERIlkEKLAAisdatrlktEAEIALKEKEAENERLRRQAEDEAYQ 1885
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVAL--EGLAA---------ELEEKQQELEAQLEQLQEKAAETSQE 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1927222988 1886 RKAledQANQHKQQIEEKIVLlkksSEAEmerQRAIVDDTLKQR 1929
Cdd:PRK11448 214 RKQ---KRKEITDQAAKRLEL----SEEE---TRILIDQQLRKA 247
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1645-1814 |
4.69e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1645 QKANEAlrlRLQAEEEAHKKSLAQEDAEKQKEEAEREAK---KRAKAEDSALKQKEMAE---------NELERQRKVAES 1712
Cdd:COG2268 221 REAEEA---ELEQEREIETARIAEAEAELAKKKAEERREaetARAEAEAAYEIAEANAErevqrqleiAEREREIELQEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1713 TAQQKLTAEQELIRLRADfdnAEQQRslledelyrlkneVVAAQQQRKQLEDELAKVRSEMdvlIQLKSKAEKEtMSNSE 1792
Cdd:COG2268 298 EAEREEAELEADVRKPAE---AEKQA-------------AEAEAEAEAEAIRAKGLAEAEG---KRALAEAWNK-LGDAA 357
|
170 180
....*....|....*....|..
gi 1927222988 1793 RSKQLLEveatKMRDLAEEASK 1814
Cdd:COG2268 358 ILLMLIE----KLPEIAEAAAK 375
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1142-1569 |
4.70e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1142 KKMRAEAEGEQPVFDSLEAELKKAtavsdkmsrvhSERDAELDHYRQLLSSLQDRWKAVFSQIDLRQRELEQLGRQLGYY 1221
Cdd:pfam05557 69 EALREQAELNRLKKKYLEALNKKL-----------NEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1222 RESYDWLIRWINDAKQRQEKIQAvtitDSKTLKEQLAQEKKLLEEVEGNKDKVDECqKYAKAYIDTIKDYELQLVAYKAQ 1301
Cdd:pfam05557 138 QERLDLLKAKASEAEQLRQNLEK----QQSSLAEAEQRIKELEFEIQSQEQDSEIV-KNSKSELARIPELEKELERLREH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1302 VEPLASpLKKTKLdsasdnIIQEYVTlrtkyselmtltsqyikfitDSQRRLEDEEKAAEKLKAEEQKKmAMMQAELDKQ 1381
Cdd:pfam05557 213 NKHLNE-NIENKL------LLKEEVE--------------------DLKRKLEREEKYREEAATLELEK-EKLEQELQSW 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1382 KQLAEVHAKAIAKAEKEAQELKLRMQEEVNRRED--AVVDAEKQKHNIQLELHE-----LKNLSEQQIMDKS-KQVDDAL 1453
Cdd:pfam05557 265 VKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEEnsSLTSSARQLEKARRELEQelaqyLKKIEDLNKKLKRhKALVRRL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1454 QSRVKI-EEEIRLIRLQLETTVKQKSTAESELKQLRdRAAEAEKLRKAAQEEAEKLRKQ--VNEET---QKKRMAEEELK 1527
Cdd:pfam05557 345 QRRVLLlTKERDGYRAILESYDKELTMSNYSPQLLE-RIEEAEDMTQKMQAHNEEMEAQlsVAEEElggYKQQAQTLERE 423
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1927222988 1528 RKAEAEKEAAKQKQKALEDLENLKRQAEEAERQVKQAEIEKE 1569
Cdd:pfam05557 424 LQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKN 465
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1612-1838 |
4.73e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.53 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1612 VLQLQHEAAALKKQQEDAERAREEAEKELEKWRQKAnEALRLRLQAEEEAHKKSLAQEDAEKQKEEAE--REAKKRAKAE 1689
Cdd:TIGR02794 42 LVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQA-EEAEKQRAAEQARQKELEQRAAAEKAAKQAEqaAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1690 DSALKQKEMAEN----ELERQRKVAESTAQQkltAEQElirlrADFDNAEQQRSLLEDELYRLKNEVVAAQQQRKQLEDE 1765
Cdd:TIGR02794 121 AEEAKAKQAAEAkakaEAEAERKAKEEAAKQ---AEEE-----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1927222988 1766 LAKVRSEmdvliQLKSKAEKETMSNSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQRA 1838
Cdd:TIGR02794 193 EAKAKAE-----AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2024-2180 |
4.76e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2024 KKKAEEARKQKDDADKEAEKQILMAqqAAQKCSAAEQQVQSVLAQQKEDTIMQTKlKEEYEKAKKLAKQAEAAKEKAERE 2103
Cdd:PRK07735 68 KAKAAALAKQKREGTEEVTEEEKAK--AKAKAAAAAKAKAAALAKQKREGTEEVT-EEEKAAAKAKAAAAAKAKAAALAK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2104 -----AALLRQQAEEAERQKAAAEQEAANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEmAKHKKLAEQTL 2178
Cdd:PRK07735 145 qkregTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAK-AKAAALAKQKA 223
|
..
gi 1927222988 2179 KQ 2180
Cdd:PRK07735 224 SQ 225
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2309-2596 |
4.85e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2309 DKMLKEKMQAIQEaSRLRAEAEMLQRQKDLAQEQAqkllEDKQLMQQRLDEETEEYQKSLEAERKRQLEI----IAESEK 2384
Cdd:pfam02029 61 EEAFLDRTAKREE-RRQKRLQEALERQKEFDPTIA----DEKESVAERKENNEEEENSSWEKEEKRDSRLgrykEEETEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2385 LKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVE-KLEVARLTSSKEADDLRKAIADLEKEKSRLK 2463
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKiKKEKKVKYESKVFLDQKRGHPEVKSQNGEEE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2464 KEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRL-ESQFEEEVKKAKALKDEQERQKQQME 2542
Cdd:pfam02029 216 VTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLrQKQQEAELELEELKKKREERRKLLEE 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1927222988 2543 DEKKKLQATMDaalnkQKEAEKEMHNKQKEmkELERKRLEQerilAEENQKLRE 2596
Cdd:pfam02029 296 EEQRRKQEEAE-----RKLREEEEKRRMKE--EIERRRAEA----AEKRQKLPE 338
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1678-1986 |
5.34e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1678 AEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVVAAQQ 1757
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1758 QRKQLEDELAKVRSEMDVLIQLKSKAEKEtmsnSERSKQLLEVEATKMRDLAEEASKLRAIAEEAKHQRQVAEEEAARQR 1837
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEE----AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1838 AEAERILKE-KLAAISDATRLKTEAEIALKEKEAE-NERLRRQAEDEAYQRKALEDQANQHKQQIEEKIVLLKKSSEAEM 1915
Cdd:COG4372 157 EQLESLQEElAALEQELQALSEAEAEQALDELLKEaNRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1927222988 1916 ERQRAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLAL 1986
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
46-143 |
5.45e-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: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 46 QKKTFTKWVNKHLIKSQ--RQV-------TDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 111
Cdd:cd21293 2 EKGSYVDHINRYLGDDPflKQFlpidpstNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1927222988 112 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 143
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1354-1755 |
5.81e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.82 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1354 EDEEKAAEKLKAEEQKKMAMMQAELDKQKQLAEVHAKAIAKAEKEAQELKlRMQEEVNRREDAVVDAEKQ-----KHNIQ 1428
Cdd:pfam09731 100 EVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAK-EAKDDAIQAVKAHTDSLKEasdtaEISRE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1429 LELHELKNLSEQQIMDKSKQVDDALQSrvkieeeirlirlQLETTVKQKSTAESELKQLRDRAAEAEKLRKAAQEEA--- 1505
Cdd:pfam09731 179 KATDSALQKAEALAEKLKEVINLAKQS-------------EEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAklv 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1506 EKLRKQVNEETQKKRMaeeELKRKAEAEKEAAKQKQKALEDleNLKRQAEEAERQVKQAEiekeRQIQVAHVAAQKSAAA 1585
Cdd:pfam09731 246 DQYKELVASERIVFQQ---ELVSIFPDIIPVLKEDNLLSND--DLNSLIAHAHREIDQLS----KKLAELKKREEKHIER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1586 ELQSKHMSFvektSKLEESLKQEhgavlqLQHEAAALKKQqedaerAREEAEKELEKWRQKANEALRLRLQAEEEAHKKS 1665
Cdd:pfam09731 317 ALEKQKEEL----DKLAEELSAR------LEEVRAADEAQ------LRLEFEREREEIRESYEEKLRTELERQAEAHEEH 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1666 LAQEDAEkQKEEAEREAKKRAK---AEDSALKQKEMAE-----NELERQ---RKVAESTAQ--QKLTAEQELIRLRADFD 1732
Cdd:pfam09731 381 LKDVLVE-QEIELQREFLQDIKekvEEERAGRLLKLNEllanlKGLEKAtssHSEVEDENRkaQQLWLAVEALRSTLEDG 459
|
410 420
....*....|....*....|....*...
gi 1927222988 1733 NAEQQRSLLEDELYRLK-----NEVVAA 1755
Cdd:pfam09731 460 SADSRPRPLVRELKALKelasdDEVVKA 487
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2525-2600 |
5.84e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.25 E-value: 5.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 2525 KKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMhnkQKEMKELERKRLEQERILAEENQKLREKLQQ 2600
Cdd:pfam03938 26 KKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQEL---QKKEQELQQLQQKAQQELQKKQQELLQPIQD 98
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
372-546 |
5.95e-03 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 42.67 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 372 GRLHVAILERERLLRIEFERLERLQRIvSKVQMESGLCDEQLSHLETLLQMD-------IRLLSAGKPAQHTAEVERELD 444
Cdd:COG3914 92 GRYEEALALYRRALALNPDNAEALFNL-GNLLLALGRLEEALAALRRALALNpdfaeayLNLGEALRRLGRLEEAIAALR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 445 KAV----NMIRLLFNDVQVLKD-GRHPQAEQMYRRVYRLDERLVNLRSDY-NLRLKSAVTTVKVPMQQTTQQTMKVRPEL 518
Cdd:COG3914 171 RALeldpDNAEALNNLGNALQDlGRLEEAIAAYRRALELDPDNADAHSNLlFALRQACDWEVYDRFEELLAALARGPSEL 250
|
170 180
....*....|....*....|....*...
gi 1927222988 519 DDVTLRYIQDLLAWVEENQHRideaQWG 546
Cdd:COG3914 251 SPFALLYLPDDDPAELLALAR----AWA 274
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
2078-2168 |
5.97e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 42.55 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2078 KLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAaaeqeaanqakaQEDAERLRKEAEFEAAKRAQAENAAL 2157
Cdd:PRK12472 194 TLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKA------------RADAELKRADKALAAAKTDEAKARAE 261
|
90
....*....|.
gi 1927222988 2158 KQKQQADAEMA 2168
Cdd:PRK12472 262 ERQQKAAQQAA 272
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3797-3830 |
6.00e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.08 E-value: 6.00e-03
10 20 30
....*....|....*....|....*....|....
gi 1927222988 3797 LEAQTATGGIIDPEFQFHLPADVAMQRGYINKET 3830
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2293-2485 |
6.12e-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: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2293 LRQIAE--DDLNQQRALADKmlkEKMQAIQEASRLRAEAEmlqrqkdLAQEQAQKLLEDKQLmQQRLDEETEEYQksLEA 2370
Cdd:COG2268 191 RRKIAEiiRDARIAEAEAER---ETEIAIAQANREAEEAE-------LEQEREIETARIAEA-EAELAKKKAEER--REA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2371 ERKRqleIIAEseklklqvsqlsEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEKLevarltsskEADDLRK 2450
Cdd:COG2268 258 ETAR---AEAE------------AAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAEL---------EADVRKP 313
|
170 180 190
....*....|....*....|....*....|....*
gi 1927222988 2451 AIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIE 2485
Cdd:COG2268 314 AEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2284-2466 |
6.33e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.63 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2284 SVEAQEAARLRQIAEDDLNQQRALADKMLKEKMqaiqEASRLRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEE 2363
Cdd:pfam15709 316 SEEDPSKALLEKREQEKASRDRLRAERAEMRRL----EVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2364 YQKSLEAERKRQ--------LEIIAESEKLKLQVSQ----LSEAQAKAQEEAKKfKKQADSIASRLHETELATQEK---- 2427
Cdd:pfam15709 392 RKQRLEEERQRQeeeerkqrLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAE-RAEAEKQRQKELEMQLAEEQKrlme 470
|
170 180 190
....*....|....*....|....*....|....*....
gi 1927222988 2428 MTVVEKLEVARLTSSKEADdlrkaiADLEKEKSRLKKEA 2466
Cdd:pfam15709 471 MAEEERLEYQRQKQEAEEK------ARLEAEERRQKEEE 503
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2330-2488 |
6.34e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2330 EMLQRQKDLAQEQ-AQKLLEdkqlmQQRLDEETEEyqkslEAERKRQLEIIAESEKLklQVSQLSEAQAKAQEEAKKFKK 2408
Cdd:PTZ00491 665 EAAARHQAELLEQeARGRLE-----RQKMHDKAKA-----EEQRTKLLELQAESAAV--ESSGQSRAEALAEAEARLIEA 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2409 QADsiasrlhetelatqekmtvvekLEVARLTSskEADDLRKAiADLEKEKSRLKKEAEDLQN-------KSKEMADaqq 2481
Cdd:PTZ00491 733 EAE----------------------VEQAELRA--KALRIEAE-AELEKLRKRQELELEYEQAqneleiaKAKELAD--- 784
|
....*..
gi 1927222988 2482 kqIEHEK 2488
Cdd:PTZ00491 785 --IEATK 789
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2194-2485 |
6.44e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2194 KLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKdkdntqkflakeadnM 2273
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREK---------------R 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2274 KKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQaIQEASRLRAEAEMLQRQKDLAQEqaqkllEDKQLM 2353
Cdd:COG1340 67 DELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGS-IDKLRKEIERLEWRQQTEVLSPE------EEKELV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2354 QQ--RLDEETEEYQKSLEAERKRQlEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHET-ELATQEKMTV 2430
Cdd:COG1340 140 EKikELEKELEKAKKALEKNEKLK-ELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELrKEADELHKEI 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 2431 VEKLEVARLTsSKEADDLRKAIADLEKEKSRLKKEAEDLQ-NKSKEMADAQQKQIE 2485
Cdd:COG1340 219 VEAQEKADEL-HEEIIELQKELRELRKELKKLRKKQRALKrEKEKEELEEKAEEIF 273
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1328-1518 |
6.59e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1328 LRTKYSELMTLTSQyIKFITDSQRRLEDEEKAAEKLKAeEQKKMAMMQAE-------------LDKQKQLA------EVH 1388
Cdd:PRK11637 91 LRETQNTLNQLNKQ-IDELNASIAKLEQQQAAQERLLA-AQLDAAFRQGEhtglqlilsgeesQRGERILAyfgylnQAR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1389 AKAIAKAEKEAQELKLRMQEEVnrredavvdaekQKHNIQLELhelknLSEQQimDKSKQVDDALQSRVKIEEEirlirl 1468
Cdd:PRK11637 169 QETIAELKQTREELAAQKAELE------------EKQSQQKTL-----LYEQQ--AQQQKLEQARNERKKTLTG------ 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1927222988 1469 qLETTVKQKSTAESELKQ----LRDRAAEAEKLRKAAQE----EAEKLRKQVNEETQK 1518
Cdd:PRK11637 224 -LESSLQKDQQQLSELRAnesrLRDSIARAEREAKARAErearEAARVRDKQKQAKRK 280
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2336-2608 |
6.66e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2336 KDLAQEQAQKLLEDKQLMQQRLDEEteEYQKsleaeRKRQleiiaesEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIAS 2415
Cdd:pfam05667 214 AELAAAQEWEEEWNSQGLASRLTPE--EYRK-----RKRT-------KLLKRIAEQLRSAALAGTEATSGASRSAQDLAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2416 RLHE--------TELATQEKMTVVEKLEVAR---------LTSSKEADDLRKAiadLEKEKSRLKKEAEDLQNKSKEMad 2478
Cdd:pfam05667 280 LLSSfsgssttdTGLTKGSRFTHTEKLQFTNeapaatsspPTKVETEEELQQQ---REEELEELQEQLEDLESSIQEL-- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2479 aqQKQIEHEKTVLQQTFLSEKEMllkkekliEEEKKRLESQFEEEVKKAKALKDEQErqkqQMEDEKKKLQATMDAALNK 2558
Cdd:pfam05667 355 --EKEIKKLESSIKQVEEELEEL--------KEQNEELEKQYKVKKKTLDLLPDAEE----NIAKLQALVDASAQRLVEL 420
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1927222988 2559 QKEAEK---EMHNKQKEMKELERKRLEQERILAEENQKLREKLQQLEE--AQKDQ 2608
Cdd:pfam05667 421 AGQWEKhrvPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEeaKQKEE 475
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1350-1626 |
6.66e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1350 QRRLEDEEKAAEKLkaEEQkkmAMMQAELDKQKQLAEVHAKAiakAEKEAQELK-----------------LRMQEEVNR 1412
Cdd:COG3096 350 ERYQEDLEELTERL--EEQ---EEVVEEAAEQLAEAEARLEA---AEEEVDSLKsqladyqqaldvqqtraIQYQQAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1413 REDA---VVDAEKQKHNIQLELHELKN---------LSEQQIMDKSK----QVDDALQSRVKIEEEI------RLIRLQL 1470
Cdd:COG3096 422 LEKAralCGLPDLTPENAEDYLAAFRAkeqqateevLELEQKLSVADaarrQFEKAYELVCKIAGEVersqawQTARELL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1471 ETTVKQKSTAEsELKQLRDRAAEAEKlRKAAQEEAEKLRKQVNEETQKKRMAEEELKRKAEAEKEAAKQKQKAL----ED 1546
Cdd:COG3096 502 RRYRSQQALAQ-RLQQLRAQLAELEQ-RLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAaeavEQ 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1547 LENLKRQAEEAERQVKQ----AEIEKERQIQVAHVAAQKSAAAElqskhmSFVEKTSKLEESLKQEHGAVLQLQHEAAal 1622
Cdd:COG3096 580 RSELRQQLEQLRARIKElaarAPAWLAAQDALERLREQSGEALA------DSQEVTAAMQQLLEREREATVERDELAA-- 651
|
....
gi 1927222988 1623 KKQQ 1626
Cdd:COG3096 652 RKQA 655
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2401-2614 |
6.79e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2401 EEAKKFKKQADSIASRLHETELATQEKMTVVEKLevarltsSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQ 2480
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEI-------SSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2481 Q-KQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRLESQfEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQ 2559
Cdd:PRK03918 252 GsKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2560 KEAEK---EMHNKQKEMKELERK--RLEQERILAEENQKLREKLQQLEEAQKDQPDKEVI 2614
Cdd:PRK03918 331 KELEEkeeRLEELKKKLKELEKRleELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2174-2405 |
6.87e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2174 AEQTLKQKFQVEQELTKVKLKLDETDKQKSV----------LDEELQRLKDEVDDAVKQRGQVEEEL-LKVKVQMEELLK 2242
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIKLaaqekihveiLEEQLEKLRNELLIRGATEGLCVHSLsKELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2243 LKLRIEEENQRLIK-KDKDNTQKFLAKEADNMK-KLAEDAARLSVEAQEAARLRQIaeddlnQQRALADKMlkEKMQAIQ 2320
Cdd:PLN02939 238 LKDDIQFLKAELIEvAETEERVFKLEKERSLLDaSLRELESKFIVAQEDVSKLSPL------QYDCWWEKV--ENLQDLL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2321 EASRLRAE--AEMLQRQKDLaQEQAQKL-------------LEDKQLMQQRLDEETEEYQKSlEAERKRQLEIIAESekl 2385
Cdd:PLN02939 310 DRATNQVEkaALVLDQNQDL-RDKVDKLeaslkeanvskfsSYKVELLQQKLKLLEERLQAS-DHEIHSYIQLYQES--- 384
|
250 260
....*....|....*....|
gi 1927222988 2386 klqVSQLSEAQAKAQEEAKK 2405
Cdd:PLN02939 385 ---IKEFQDTLSKLKEESKK 401
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2018-2117 |
7.04e-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: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2018 DELDRLKKKAEEARKQKDDADKEAEKQILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAK 2097
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAEA 80
|
90 100
....*....|....*....|
gi 1927222988 2098 EKAEREAALLRQQAEEAERQ 2117
Cdd:pfam07926 81 ESAKAELEESEESWEEQKKE 100
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1595-1804 |
7.26e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1595 VEKTSKLEESLKQeHGAVLQLQHEAAALKKQqedaerareeaekelekwrqkanealRLRLQAEEEAHKKSLAQEDAEKQ 1674
Cdd:PTZ00491 657 IEITTKSQEAAAR-HQAELLEQEARGRLERQ--------------------------KMHDKAKAEEQRTKLLELQAESA 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1675 KEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAEstaqqKLTAEQELirlradfdnaeqqrslledelyrlknevvA 1754
Cdd:PTZ00491 710 AVESSGQSRAEALAEAEARLIEAEAEVEQAELRAKAL-----RIEAEAEL-----------------------------E 755
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1755 AQQQRKQLEDELAKVRSEMDVliqlkskaeketmsnsERSKQLLEVEATK 1804
Cdd:PTZ00491 756 KLRKRQELELEYEQAQNELEI----------------AKAKELADIEATK 789
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1644-1870 |
7.40e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1644 RQKANEAlRLRLQA------EEEAHKKSLAQEDAEKQKEEAER---EAKKRAKAEDSALKQKEMAENELERQRKVAESTA 1714
Cdd:PRK05035 445 KKKAEEA-KARFEArqarleREKAAREARHKKAAEARAAKDKDavaAALARVKAKKAAATQPIVIKAGARPDNSAVIAAR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1715 QQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEvVAAQQQ-----RKQLEDELAKVRSEMdvliqLKSKAEKETMS 1789
Cdd:PRK05035 524 EARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAK-KAAQQAanaeaEEEVDPKKAAVAAAI-----ARAKAKKAAQQ 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1790 NSERSKQLLEVEATKMRDLAEEASKlRAIAEEAKHQR--QVAEEEAARQRAEAERI--LKEKLAAISDATRLKTEAEIAL 1865
Cdd:PRK05035 598 AASAEPEEQVAEVDPKKAAVAAAIA-RAKAKKAEQQAnaEPEEPVDPRKAAVAAAIarAKARKAAQQQANAEPEEAEDPK 676
|
....*
gi 1927222988 1866 KEKEA 1870
Cdd:PRK05035 677 KAAVA 681
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2308-2419 |
7.44e-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: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2308 ADKMLKEKMQAIQEAsrlRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQKSLEAERKRQLEiiaesEKLKL 2387
Cdd:cd16269 189 ADQALTEKEKEIEAE---RAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLK-----EQERA 260
|
90 100 110
....*....|....*....|....*....|..
gi 1927222988 2388 QVSQLSEAQAKAQEEakkFKKQADSIASRLHE 2419
Cdd:cd16269 261 LESKLKEQEALLEEG---FKEQAELLQEEIRS 289
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2154-2291 |
7.57e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2154 NAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDE-TDKQKSVLDE-ELQRLKDEVDDAVKQRGQVEEELL 2231
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyEEQLGNVRNNkEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2232 KVkvqMEELLKLKLRIEEENQRLIKKDKDNTQKfLAKEADNMKKLAEDAARLSVEAQEAA 2291
Cdd:COG1579 114 EL---MERIEELEEELAELEAELAELEAELEEK-KAELDEELAELEAELEELEAEREELA 169
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2312-2482 |
7.58e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2312 LKEKMQAIQEASRLRAEAEM-LQRQKDLAQEQAQKLLEDKQLMQ-QRLDEETEEYQKSLE--AERKRQLEiiAESEKLKL 2387
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKeAEEKLEAALLEAKELLLRERNQQrQEARREREELQREEErlVQKEEQLD--ARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2388 QVSQLSEAQakaqeeaKKFKKQADSIASRLHETELatqekmtvvEKLEVARLTSSKEADDLrkaIADLEKEksrLKKEAE 2467
Cdd:PRK12705 103 LENQLEERE-------KALSARELELEELEKQLDN---------ELYRVAGLTPEQARKLL---LKLLDAE---LEEEKA 160
|
170
....*....|....*
gi 1927222988 2468 DLQNKSKEMADAQQK 2482
Cdd:PRK12705 161 QRVKKIEEEADLEAE 175
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2222-2565 |
7.62e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2222 QRGQVEEELLKVKVQMEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSveaQEAARLRQIAEDDL 2301
Cdd:COG5185 204 VNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLR---LEKLGENAESSKRL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2302 NQQRALADKMLKEKMQAIQEasrlRAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQksLEAERKRQLEIIAE 2381
Cdd:COG5185 281 NENANNLIKQFENTKEKIAE----YTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQN--LTAEIEQGQESLTE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2382 S-EKLKLQVSQL--SEAQAKAQEEAKKFKKQADSIASRLHE--TELATQEKMtVVEKLEVARLTSSKEADDLRKAIADLE 2456
Cdd:COG5185 355 NlEAIKEEIENIvgEVELSKSSEELDSFKDTIESTKESLDEipQNQRGYAQE-ILATLEDTLKAADRQIEELQRQIEQAT 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2457 ---KEKSRLKKEA-EDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEmllkkekLIEEEKKRLESQFEEEVKKAKALKD 2532
Cdd:COG5185 434 ssnEEVSKLLNELiSELNKVMREADEESQSRLEEAYDEINRSVRSKKE-------DLNEELTQIESRVSTLKATLEKLRA 506
|
330 340 350
....*....|....*....|....*....|...
gi 1927222988 2533 EQERQKQQMEDEKKKLQATMDAALNKQKEAEKE 2565
Cdd:COG5185 507 KLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1705-1895 |
7.64e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.55 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1705 RQRKVAESTAQQKLTAEQELIRLRADFD-NAEQQRSLLEDELYRLKNEVV--AAQQQRKQLEDELAKVRSEMDVLIQLKS 1781
Cdd:PRK00106 25 KMKSAKEAAELTLLNAEQEAVNLRGKAErDAEHIKKTAKRESKALKKELLleAKEEARKYREEIEQEFKSERQELKQIES 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1782 KAEKETMSNSERSKQLLEVEatKMRDlaeeaSKLRAIAEEAKH----QRQVAEEEAaRQRAEAERI----LKEKLAAISD 1853
Cdd:PRK00106 105 RLTERATSLDRKDENLSSKE--KTLE-----SKEQSLTDKSKHiderEEQVEKLEE-QKKAELERVaalsQAEAREIILA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1927222988 1854 ATRLKTEAEIALKEKEAENE---RLRRQAED---EAYQRKALEDQANQ 1895
Cdd:PRK00106 177 ETENKLTHEIATRIREAEREvkdRSDKMAKDllaQAMQRLAGEYVTEQ 224
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
2051-2324 |
7.66e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 42.36 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2051 AAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEEYEKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAANQAK 2130
Cdd:pfam04747 56 ASLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEARRAEAEAKKRAAQEEEHKQWKAEQERIQKEQEK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2131 AQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKqksvldEELQ 2210
Cdd:pfam04747 136 KEADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTPTNTPAEPA------EQVQ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2211 RLKDEVDDAVKQRGQVEEELLKVKVQmEELLKLKLRIEEENQRLIKKDKDNTQKFLAKEADNMKKLAEDAARLSVEAQEA 2290
Cdd:pfam04747 210 EITGKKNKKNKKKSESEATAAPASVE-QVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETPVEPVVETTPP 288
|
250 260 270
....*....|....*....|....*....|....
gi 1927222988 2291 ARLRQiAEDDLNQQRALADKMLKEKMQAIQEASR 2324
Cdd:pfam04747 289 ASENQ-KKNKKDKKKSESEKVVEEPVQAEAPKSK 321
|
|
| CH_PARVB_rpt2 |
cd21338 |
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ... |
45-150 |
7.99e-03 |
|
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409187 Cd Length: 130 Bit Score: 39.57 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 45 VQKKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKHRQVKLV 120
Cdd:cd21338 21 VVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTpesfDQKVHNVSFAFELMQDGGLKKP 100
|
90 100 110
....*....|....*....|....*....|
gi 1927222988 121 NIRNDDIADGNPKLTLGLIWTIILHFQISD 150
Cdd:cd21338 101 KARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1488-1681 |
8.17e-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: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1488 RDRAAEAEKLRKaaqeEAEKLRKqvnEETQKKRMAEEELKRKAEAEKEAAKQKQKALEDLEnLKRQAEEAERQvKQAEIE 1567
Cdd:pfam15709 337 RLRAERAEMRRL----EVERKRR---EQEEQRRLQQEQLERAEKMREELELEQQRRFEEIR-LRKQRLEEERQ-RQEEEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1568 KERQIQVAhvAAQKSAAAELQSKHMSFVEKTSKLEESLKQEHGAVLQLQHEaAALKKQQEDAERAREEAEKELEKWRQKA 1647
Cdd:pfam15709 408 RKQRLQLQ--AAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKE-LEMQLAEEQKRLMEMAEEERLEYQRQKQ 484
|
170 180 190
....*....|....*....|....*....|....*...
gi 1927222988 1648 NEALRLRLQAEEEAHKKS----LAQEDAEKQKEEAERE 1681
Cdd:pfam15709 485 EAEEKARLEAEERRQKEEeaarLALEEAMKQAQEQARQ 522
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2274-2713 |
8.84e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.95 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2274 KKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQKLLE---DK 2350
Cdd:COG3064 7 EKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEaekAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2351 QLMQQRLDEETEEYQKSLEAERKRQLEIIAESEKlklqvsQLSEAQAKAQEEAK-KFKKQADSIASRLHETELATQEKMT 2429
Cdd:COG3064 87 AEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKE------KAEEAKRKAEEEAKrKAEEERKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2430 VVEKLEVARLTSSKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLI 2509
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2510 EEEKKRLESQFEEEVKKAKALKDEQERQKQQMEDEKKKLQATMDAALNKQKEAEKEMHNKQKEMKELERKRLEQERILAE 2589
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2590 ENQKLREKLQQLEEAQKDQPDKEVIHVTMVETTKNVYNGQNVGDVVDSAEKKPDPLAFNGIREKVPASRLHDLGLLPKKD 2669
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGL 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1927222988 2670 FDKLKNGKTTVQELGQTENLQKILKGKNGIAGVLTPSNQKLSIY 2713
Cdd:COG3064 401 LGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADL 444
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
2092-2186 |
8.92e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 39.60 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2092 QAEAAK--EKAEREAALLRQQAEEAERQkaaaeqEAANQAKAQEDAERLRKEAEFEAAKRAQAenaalkQKQQADAEMAK 2169
Cdd:PRK07353 45 RAEAKErlAEAEKLEAQYEQQLASARKQ------AQAVIAEAEAEADKLAAEALAEAQAEAQA------SKEKARREIEQ 112
|
90
....*....|....*..
gi 1927222988 2170 HKKLAEQTLKQkfQVEQ 2186
Cdd:PRK07353 113 QKQAALAQLEQ--QVDA 127
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2158-2344 |
8.92e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2158 KQKQQADAEMAKHKKLAEQT--LKQKFQVEQELTKV--KLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELLKV 2233
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAeeLQQKQAAEQERLKQleKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2234 KVQMEELLKLKLRIEEENQrliKKDKDNTQKFLAKEAdnmKKLAEDAARLSVEAQEAARLRQIAE---DDLNQQRALADK 2310
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAK---KKAEAEAAKKAAAEA---KKKAEAEAAAKAAAEAKKKAEAEAKkkaAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....
gi 1927222988 2311 mlKEKMQAIQEASRLRAEAEMLQRQKDLAQEQAQ 2344
Cdd:PRK09510 224 --KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| CH_PARVG_rpt2 |
cd21307 |
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ... |
47-136 |
9.02e-03 |
|
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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: 409156 [Multi-domain] Cd Length: 122 Bit Score: 39.26 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 47 KKTFTKWVNKHLIKSQRQVTDLYEDLRDGHNLISLLEVLSGETLPREKgrmrFH--------KLQNVQIALDFLKHRQVK 118
Cdd:cd21307 18 KKAILHFVNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHLSE----FFltpsstseMLHNVTLALELLKEGGLL 93
|
90
....*....|....*...
gi 1927222988 119 LVNIRNDDIADGNPKLTL 136
Cdd:cd21307 94 NFPVNPEDIVNGDSKATI 111
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
1735-1915 |
9.33e-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: 40.03 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1735 EQQRSLLEDELYRLKNEVVaaqqqRKQLEDELAKVRSEMDVLIQLKSKAEKETMsnserskqlleveatkMRDLAEEASK 1814
Cdd:pfam15346 2 EAESKLLEEETARRVEEAV-----AKRVEEELEKRKDEIEAEVERRVEEARKIM----------------EKQVLEELER 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1815 LRAIAEEAKHQRqvaEEEAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEaenerlrRQAEDEAYQRKALEDQan 1894
Cdd:pfam15346 61 EREAELEEERRK---EEEERKKREELERILEENNRKIEEAQRKEAEERLAMLEEQ-------RRMKEERQRREKEEEE-- 128
|
170 180
....*....|....*....|.
gi 1927222988 1895 qhKQQIEEKIVLLKKSSEAEM 1915
Cdd:pfam15346 129 --REKREQQKILNKKNSRPKL 147
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1661-1985 |
9.67e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1661 AHKKSLAQEDAEKQKEEAEREAKKRAKAEDSALKQKEMAENELERQRKVAESTAQQKltaeqelirlradfdnaeQQRSL 1740
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEER------------------EQKRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1741 LEDELYRLKNEVVAAQQQRKQLEDELAKvrsemdvliQLKSKAEKETMSNSERSKQLLEV--EATKMRDLAEEASKLRAI 1818
Cdd:pfam13868 91 EEYEEKLQEREQMDEIVERIQEEDQAEA---------EEKLEKQRQLREEIDEFNEEQAEwkELEKEEEREEDERILEYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1819 AEEAKHQRQVAEEEAARQRAEAERI--LKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQANQH 1896
Cdd:pfam13868 162 KEKAEREEEREAEREEIEEEKEREIarLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 1897 KQQIEEKIVLLkkssEAEMERQRAivdDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEET-QQSKLRAE 1975
Cdd:pfam13868 242 EEQIELKERRL----AEEAEREEE---EFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQrAAEREEEL 314
|
330
....*....|
gi 1927222988 1976 EEAEKLRKLA 1985
Cdd:pfam13868 315 EEGERLREEE 324
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2045-2444 |
9.83e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2045 ILMAQQAAQKCSAAEQQVQSVLAQQKEDTIMQTKLKEeyeKAKKLAKQAEAAKEKAEREAALLRQQAEEAERQKAAAEQE 2124
Cdd:COG5185 187 GLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLE---KAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2125 AANQAKAQEDAERLRKEAEFEAAKRAQAENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLD-ETDKQKS 2203
Cdd:COG5185 264 DLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETEtGIQNLTA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2204 VLDEELQRLKDEVDDAVKQRGQVEEELLKVKVQmEELLKLKLRIEEENQRLIKKDKD---NTQKFLAKEADNMKKLAEDA 2280
Cdd:COG5185 344 EIEQGQESLTENLEAIKEEIENIVGEVELSKSS-EELDSFKDTIESTKESLDEIPQNqrgYAQEILATLEDTLKAADRQI 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2281 ARL-------SVEAQEAARLRQIAEDDLNQQRALADKMLKEKMQaiqeaSRLRAEAEMLQRQKDLAQEQAQKLLEDKQLM 2353
Cdd:COG5185 423 EELqrqieqaTSSNEEVSKLLNELISELNKVMREADEESQSRLE-----EAYDEINRSVRSKKEDLNEELTQIESRVSTL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2354 QQRLDEETEEYQKSLEAERKrQLEIIAESEKLKLQVSQLSEAQAKAQEEAKKFKKQADSIASRLHETELATQEKMTVVEK 2433
Cdd:COG5185 498 KATLEKLRAKLERQLEGVRS-KLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQY 576
|
410
....*....|.
gi 1927222988 2434 LEVARLTSSKE 2444
Cdd:COG5185 577 LSTIESQQARE 587
|
|
| vATP-synt_E |
pfam01991 |
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ... |
2130-2272 |
9.83e-03 |
|
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.
Pssm-ID: 396537 [Multi-domain] Cd Length: 199 Bit Score: 40.44 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2130 KAQEDAERLRKEAEFEAAKraqaENAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETdkQKSVLDEEL 2209
Cdd:pfam01991 5 EAEEKAEEIRAKAEEEFAI----EKAELVQEAEEKIDEIYEKKEKQAEMQKKIIISNAKNEARLKVLEA--REEILDEVF 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1927222988 2210 QRLKDEVDDAVKQRGQVEEELLKVKVQ-MEELL--KLKLRIEEENQRLIKKDKDNTQKFLAKEADN 2272
Cdd:pfam01991 79 NEAEKKLAELEEDTDEYKDLLRKLIVQaLVKLGepEVIVRCRKRDEELVESALDKAAEEYKAKTKK 144
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
2362-2544 |
9.96e-03 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 41.86 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2362 EEYQKSLEAERKRQLEIIAEsEKLKLQVSQLsEAQAKAQEEAKKFKKQADSIASRLHETElatqekmtvVEKLEVARLTS 2441
Cdd:COG4487 25 KQRRAEFEKELAERLADAAK-REAALELAEA-KAKAQLQEQVAEKDAEIAELRARLEAEE---------RKKALAVAEEK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1927222988 2442 SKEADDLRKAIADLEKEKSRLKKEAEDLQNKSKEMADAQQKQIEHEKTVLQQTFLSEKEMLLKKEKLIEEEKKRL-ESQF 2520
Cdd:COG4487 94 EKELAALQEALAEKDAKLAELQAKELELLKKERELEDAKREAELTVEKERDEELDELKEKLKKEEEEKQLAEKSLkVAEY 173
|
170 180
....*....|....*....|....*...
gi 1927222988 2521 EEEVKKAK----ALKDEQERQKQQMEDE 2544
Cdd:COG4487 174 EKQLKDMQeqieELKRKKEQGSTQLQGE 201
|
|
| |
