|
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 ... |
865-972 |
5.81e-73 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 239.61 E-value: 5.81e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 865 DRVQKKTFTKWVNKHLIKraeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQVKL 944
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIK---ARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKL 77
|
90 100
....*....|....*....|....*...
gi 1678729579 945 VNIRNDDIADGNPKLTLGLIWTVILHFQ 972
Cdd:cd21188 78 VNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
862-983 |
5.13e-69 |
|
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: 228.76 E-value: 5.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 862 DERDRVQKKTFTKWVNKHLIKraeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQ 941
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK---AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQ 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1678729579 942 VKLVNIRNDDIADGNPKLTLGLIWTVILHFQISDIQINGLSE 983
Cdd:cd21235 78 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
862-980 |
4.61e-67 |
|
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: 223.71 E-value: 4.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 862 DERDRVQKKTFTKWVNKHLIKraeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQ 941
Cdd:cd21236 12 DERDKVQKKTFTKWINQHLMK---VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQ 88
|
90 100 110
....*....|....*....|....*....|....*....
gi 1678729579 942 VKLVNIRNDDIADGNPKLTLGLIWTVILHFQISDIQING 980
Cdd:cd21236 89 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTG 127
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
985-1090 |
1.30e-61 |
|
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: 207.18 E-value: 1.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 985 MSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLD 1064
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1678729579 1065 PEDVDVQHPDEKSIITYVSSLYDVMP 1090
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
986-1090 |
4.24e-60 |
|
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: 202.62 E-value: 4.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDP 1065
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1678729579 1066 EDVDVQHPDEKSIITYVSSLYDVMP 1090
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
862-982 |
1.29e-58 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 199.10 E-value: 1.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 862 DERDRVQKKTFTKWVNKHLIKraeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQ 941
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMK---VRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQ 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1678729579 942 VKLVNIRNDDIADGNPKLTLGLIWTVILHFQISDIQINGLS 982
Cdd:cd21237 78 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
986-1090 |
5.43e-55 |
|
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: 187.89 E-value: 5.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERdLGVTRLLDP 1065
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1678729579 1066 EDVDVQHPDEKSIITYVSSLYDVMP 1090
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
867-973 |
2.56e-48 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 169.10 E-value: 2.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 867 VQKKTFTKWVNKHLIKraESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQVKLVN 946
Cdd:cd21186 2 VQKKTFTKWINSQLSK--ANKPPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVN 79
|
90 100
....*....|....*....|....*..
gi 1678729579 947 IRNDDIADGNPKLTLGLIWTVILHFQI 973
Cdd:cd21186 80 ISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
984-1090 |
3.31e-48 |
|
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: 168.68 E-value: 3.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 984 DMSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERdLGVTRLL 1063
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1678729579 1064 DPEDVDVQHPDEKSIITYVSSLYDVMP 1090
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
986-1086 |
7.86e-47 |
|
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: 164.89 E-value: 7.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDP 1065
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1678729579 1066 EDVDVQHPDEKSIITYVSSLY 1086
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
986-1086 |
8.10e-47 |
|
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: 164.49 E-value: 8.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDP 1065
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1678729579 1066 EDVDVQHPDEKSIITYVSSLY 1086
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
862-969 |
4.00e-45 |
|
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: 160.23 E-value: 4.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 862 DERDRVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNVQIALDFLRHR 940
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHL---ARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQ 87
|
90 100
....*....|....*....|....*....
gi 1678729579 941 QVKLVNIRNDDIADGNPKLTLGLIWTVIL 969
Cdd:cd21246 88 RVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
863-973 |
4.31e-44 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 157.15 E-value: 4.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 863 ERDRVQKKTFTKWVNKHLIKRAESQHhVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRM--RFHKLQNVQIALDFLRHR 940
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPPMK-VEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESK 79
|
90 100 110
....*....|....*....|....*....|...
gi 1678729579 941 QVKLVNIRNDDIADGNPKLTLGLIWTVILHFQI 973
Cdd:cd21241 80 KIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
861-1086 |
8.52e-43 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 168.97 E-value: 8.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 861 EDERDRVQKKTFTKWVNKHLIKRAESQhhVTDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHKLQNVQIALDFLR 938
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGGQKE--FGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 939 HRQVKLVNIRNDDIADGNPKLTLGLIWTVILHFQISDIQingLSEDMSAKEKLLLWSQRMTGDYQN-IRCDNFSTSWRDG 1017
Cdd:COG5069 81 GKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678729579 1018 KLFNAVIHKHHPRLIDMGKVYRQSNLE--NLEQAFNVAERDLGVTRLLDPEDV-DVQHPDEKSIITYVSSLY 1086
Cdd:COG5069 158 LAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
982-1092 |
5.70e-42 |
|
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: 151.31 E-value: 5.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 982 SEDMSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTR 1061
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1678729579 1062 LLDPEDVDVQHPDEKSIITYVSSLYDVMPRM 1092
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFYHYFSKM 111
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
863-973 |
6.25e-42 |
|
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: 151.18 E-value: 6.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 863 ERDRVQKKTFTKWVNKHLIKRAeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRM--RFHKLQNVQIALDFLRHR 940
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLS-QPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKR 79
|
90 100 110
....*....|....*....|....*....|...
gi 1678729579 941 QVKLVNIRNDDIADGNPKLTLGLIWTVILHFQI 973
Cdd:cd21190 80 CIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
860-969 |
6.83e-41 |
|
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: 148.21 E-value: 6.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 860 IEDERDRVQKKTFTKWVNKHLIKraeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNVQIALDFLr 938
Cdd:cd21193 9 LQEERINIQKKTFTKWINSFLEK---ANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL- 84
|
90 100 110
....*....|....*....|....*....|.
gi 1678729579 939 HRQVKLVNIRNDDIADGNPKLTLGLIWTVIL 969
Cdd:cd21193 85 KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
839-969 |
1.28e-39 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 145.20 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 839 SSEEDWDH--SLDQPEEKTWPHFIEDERDRVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLP 916
Cdd:cd21317 1 LADDDWDNdnSSARLFERSRIKALADEREAVQKKTFTKWVNSHL---ARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 917 R-EKGRMRFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTVIL 969
Cdd:cd21317 78 KpTKGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
973-1086 |
2.38e-39 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 143.66 E-value: 2.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 973 ISDIQInglsEDMSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNV 1052
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1678729579 1053 AERDLGVTRLLDPED-VDVQHPDEKSIITYVSSLY 1086
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYY 111
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
860-969 |
7.17e-39 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409167 Cd Length: 139 Bit Score: 143.24 E-value: 7.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 860 IEDERDRVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNVQIALDFLR 938
Cdd:cd21318 31 LADEREAVQKKTFTKWVNSHL---ARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLK 107
|
90 100 110
....*....|....*....|....*....|.
gi 1678729579 939 HRQVKLVNIRNDDIADGNPKLTLGLIWTVIL 969
Cdd:cd21318 108 EQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
982-1092 |
1.42e-38 |
|
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: 141.73 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 982 SEDMSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTR 1061
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1678729579 1062 LLDPEDVDVQHPDEKSIITYVSSLYDVMPRM 1092
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKM 111
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
985-1090 |
1.58e-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: 1.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 985 MSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLD 1064
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1678729579 1065 PEDVDVQHPDEKSIITYVSSLYDVMP 1090
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
985-1086 |
4.30e-38 |
|
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: 140.00 E-value: 4.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 985 MSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLD 1064
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1678729579 1065 PEDVDVQHPDEKSIITYVSSLY 1086
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2244-3405 |
8.43e-38 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 158.07 E-value: 8.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2244 DAEKQKQNIqlelheLKNLSEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQ--------KSTAESELKQL-RE 2314
Cdd:NF041483 98 DARAQTQRI------LQEHAEHQARLQAELHTEAVQRRQQLDQELAERRQTVESHVNEnvawaeqlRARTESQARRLlDE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2315 RAAEAERLRKVAQEEAEKLHKQ----VIEETQKKRiAEKE---LQHKSEAEK---EAAKQKQKALDDLENLK-------- 2376
Cdd:NF041483 172 SRAEAEQALAAARAEAERLAEEarqrLGSEAESAR-AEAEailRRARKDAERllnAASTQAQEATDHAEQLRsstaaesd 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2377 ---KQAEEAERQVKQAEVEKERQIKVAHVAAQK--SAAAELQSKHSSFVEKTSklEESLKQEHGAVLQLQQEAAhlkkqq 2451
Cdd:NF041483 251 qarRQAAELSRAAEQRMQEAEEALREARAEAEKvvAEAKEAAAKQLASAESAN--EQRTRTAKEEIARLVGEAT------ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2452 EDAINAREEAEKELEKWRQkanEALRLRLQAEEEAhkKSLAQEDAEKQKEEAEREAKK-RAKAEESALKQKDMAEKELER 2530
Cdd:NF041483 323 KEAEALKAEAEQALADARA---EAEKLVAEAAEKA--RTVAAEDTAAQLAKAARTAEEvLTKASEDAKATTRAAAEEAER 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2531 QRKvadstaqqklTAEQELIRLRAD-FDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEmdiliqlkSKAE 2609
Cdd:NF041483 398 IRR----------EAEAEADRLRGEaADQAEQLKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAE--------AVAE 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2610 KETM---SNTEKSKQLLEAEATkmrdvAEEA-GKLRAIAEEAkhqRQVAEEEAARQRAEAerilkeklaaISEATHLKTE 2685
Cdd:NF041483 460 GERIrgeARREAVQQIEEAART-----AEELlTKAKADADEL---RSTATAESERVRTEA----------IERATTLRRQ 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2686 AEIALKEKEAENERLRRAAEDEA-YQRKALEDEANQHKKEIEEKIVQLKKSSDAEMER---------------------- 2742
Cdd:NF041483 522 AEETLERTRAEAERLRAEAEEQAeEVRAAAERAARELREETERAIAARQAEAAEELTRlhteaeerltaaeealadarae 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2743 ----QKAMVDDTLKQRRVVEEEIRILKLNFEK------------ASSGKLDLELELNKLKN-IAEETQQSKLRAEEEAEK 2805
Cdd:NF041483 602 aeriRREAAEETERLRTEAAERIRTLQAQAEQeaerlrteaaadASAARAEGENVAVRLRSeAAAEAERLKSEAQESADR 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2806 LRKLAleEEKRRREAEEKVKKITAAEEEAARQRKIAQD-----------ELERLKKKAEE----ARKQKDEADVEAEVQI 2870
Cdd:NF041483 682 VRAEA--AAAAERVGTEAAEALAAAQEEAARRRREAEEtlgsaraeadqERERAREQSEEllasARKRVEEAQAEAQRLV 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2871 VAAQQAALKCSTAEHQVqsvlAQQKEDSI--MHKKLKQEYEKakklakeaeaakekaereaalLRQQAEE-AERQKaaae 2947
Cdd:NF041483 760 EEADRRATELVSAAEQT----AQQVRDSVagLQEQAEEEIAG---------------------LRSAAEHaAERTR---- 810
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2948 qeaaiqAKAQEDAERLRKEAEFEaAKRAQAEGAALKQKQQADAEMAkhKKLAEQTLKQKFQvEQEltkvKLKLDDTDKQK 3027
Cdd:NF041483 811 ------TEAQEEADRVRSDAYAE-RERASEDANRLRREAQEETEAA--KALAERTVSEAIA-EAE----RLRSDASEYAQ 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3028 SLLDDELQRLKDEVDDAVKQRGQVEEELFKVK----VQMEELL--------KLKLRIEDENQRLLKKDKDNSQKFLAEEA 3095
Cdd:NF041483 877 RVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIgeatseaeRLTAEARAEAERLRDEARAEAERVRADAA 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3096 ENMKRLAEDAarlsveSQEAARLRQIAEDDLIQQRALADKMLKekmqaiqESSRLKAEAEM-LQRQKDLAQEQAQKLLED 3174
Cdd:NF041483 957 AQAEQLIAEA------TGEAERLRAEAAETVGSAQQHAERIRT-------EAERVKAEAAAeAERLRTEAREEADRTLDE 1023
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3175 KQlmqrrlEEETEEYQKSLEAERRRQLEIVAEAEKLklqvsqLSEAQTKAEEEAKKFKKQADKI--AARLHETEI---AT 3249
Cdd:NF041483 1024 AR------KDANKRRSEAAEQADTLITEAAAEADQL------TAKAQEEALRTTTEAEAQADTMvgAARKEAERIvaeAT 1091
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3250 KEKMTVVEKleferlnTSKEAGDL-----RDAIADLEKD---KARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQQTFL 3321
Cdd:NF041483 1092 VEGNSLVEK-------ARTDADELlvgarRDATAIRERAeelRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAE 1164
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3322 TEREMLLKKEKLIEEEKKKLESQFEEEA-KKSKALKDEQERQKQQMEEEKKKLHAtmhEAlskQKEAEKEMLSKQKEMQE 3400
Cdd:NF041483 1165 EQLAEAEAKAKELVSDANSEASKVRIAAvKKAEGLLKEAEQKKAELVREAEKIKA---EA---EAEAKRTVEEGKRELDV 1238
|
....*
gi 1678729579 3401 LEKKR 3405
Cdd:NF041483 1239 LVRRR 1243
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1721-1798 |
1.53e-37 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 136.96 E-value: 1.53e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678729579 1721 LSWQYLMRDYTQIRTWNITMLKSMKPEEYRLMMRNLELHYQDYMRDSQDSQLFGPDDRMQVEEDYTKSTQHFDGLLRS 1798
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
863-973 |
2.11e-37 |
|
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: 138.04 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 863 ERDRVQKKTFTKWVNKHLIKRAESQHhVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQV 942
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSV-VSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSI 79
|
90 100 110
....*....|....*....|....*....|.
gi 1678729579 943 KLVNIRNDDIADGNPKLTLGLIWTVILHFQI 973
Cdd:cd21242 80 KLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2306-2878 |
1.33e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 153.17 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2306 ESELKQLRERAAEAERLRKVaQEEAEKLHKQVIeeTQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQ 2385
Cdd:COG1196 199 ERQLEPLERQAEKAERYREL-KEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2386 vkQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKEL 2465
Cdd:COG1196 276 --LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2466 EKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTA 2545
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2546 EQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMD-----ILIQLKSKAEKETMSNTEKSK 2620
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAeaaarLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2621 QLLEAEATKMRDVAEEAGK-------LRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEK 2693
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVeaayeaaLEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2694 EAENERLRRAAEDEAYQRKA-------------LEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEEE 2760
Cdd:COG1196 594 RGAIGAAVDLVASDLREADAryyvlgdtllgrtLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2761 IRILKlnfekassgkldLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRKI 2840
Cdd:COG1196 674 LLEAE------------AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
570 580 590
....*....|....*....|....*....|....*...
gi 1678729579 2841 AQDELERLKKKAEEARKQKDEADVEAEVQIVAAQQAAL 2878
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
867-971 |
2.92e-36 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 134.45 E-value: 2.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 867 VQKKTFTKWVNKHLIKRAESqhhVTDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHKLQNVQIALDFLRHRQVKL 944
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLS---ITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKL 80
|
90 100
....*....|....*....|....*..
gi 1678729579 945 VNIRNDDIADGNPKLTLGLIWTVILHF 971
Cdd:cd21215 81 TNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
970-1092 |
4.24e-36 |
|
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: 135.18 E-value: 4.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 970 HFQISDIQINGLSEDMSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQA 1049
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1678729579 1050 FNVAERDLGVTRLLDPEDVDVQHPDEKSIITYVSSLYDVMPRM 1092
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFYHYFSKM 123
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
989-1090 |
6.12e-36 |
|
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: 133.71 E-value: 6.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 989 EKLLL-WSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDPED 1067
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1678729579 1068 VDVQHPDEKSIITYVSSLYDVMP 1090
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
986-1092 |
8.43e-36 |
|
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: 133.30 E-value: 8.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDP 1065
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|....*..
gi 1678729579 1066 EDVDVQHPDEKSIITYVSSLYDVMPRM 1092
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYYHYFSKM 108
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
865-969 |
1.32e-35 |
|
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: 132.51 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 865 DRVQKKTFTKWVNKHLIKRAESqhhVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNVQIALDFLRHRQVK 943
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQ---IENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVK 79
|
90 100
....*....|....*....|....*.
gi 1678729579 944 LVNIRNDDIADGNPKLTLGLIWTVIL 969
Cdd:cd21214 80 LVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2068-2897 |
5.78e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 149.14 E-value: 5.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2068 QAVSITDSKTLKEQLSQEKKLLEEIENN--KDNVDECQKYAKAYIN-------SIKDYELQLVAYN------AQADPLAS 2132
Cdd:PTZ00121 1022 QNFNIEKIEELTEYGNNDDVLKEKDIIDedIDGNHEGKAEAKAHVGqdeglkpSYKDFDFDAKEDNradeatEEAFGKAE 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2133 PLKKTKLDSASDniiqeyvtlRTRYSELMTLTSQYIKfiTETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAA 2212
Cdd:PTZ00121 1102 EAKKTETGKAEE---------ARKAEEAKKKAEDARK--AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEAR 1170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2213 HAKAIAKAEKEAQELKLMMKEEVNRREIAAVDAEKQKQNIQLELHELKNLSEQQikdKGQLVDEALQSRTKIEEEIYLIR 2292
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAK---KAEAVKKAEEAKKDAEEAKKAEE 1247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2293 IQLETTVKQKSTAESELKQLRERAAEAERLRKvaqeeAEKLHKQviEETQKKRIAEK-ELQHKSEAEKEAAKQKQKAldd 2371
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARK-----ADELKKA--EEKKKADEAKKaEEKKKADEAKKKAEEAKKA--- 1317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2372 lENLKKQAEEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKHSsfvEKTSKLEESLKQEHgavlqlQQEAAHLKKQQ 2451
Cdd:PTZ00121 1318 -DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA---EEKAEAAEKKKEEA------KKKADAAKKKA 1387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2452 EDAINArEEAEKELEKWRQKANEalrlrLQAEEEAHKKSlaqEDAEKQKEEAEREAKKRAKAEESalKQKDMAEKELERQ 2531
Cdd:PTZ00121 1388 EEKKKA-DEAKKKAEEDKKKADE-----LKKAAAAKKKA---DEAKKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEA 1456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2532 RKVADSTAQqkltaeqelirlradfdnAEQQRSllEDELYRLKNEVIAAQQQRKQLEdELAKVRSEMDILIQLKSKAEK- 2610
Cdd:PTZ00121 1457 KKAEEAKKK------------------AEEAKK--ADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEa 1515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2611 ETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAiAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIAL 2690
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKADEAKKAEEKKK-ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2691 KEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAmvddtlKQRRVVEEEIRILKlnfek 2770
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA------EELKKAEEENKIKA----- 1663
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2771 assgkldlelELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRKIAQDE----LE 2846
Cdd:PTZ00121 1664 ----------AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAE 1733
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 2847 RLKKKAEEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKED 2897
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
985-1083 |
6.23e-35 |
|
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: 130.62 E-value: 6.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 985 MSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLD 1064
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1678729579 1065 PEDVDVQHPDEKSIITYVS 1083
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2275-2808 |
7.68e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 147.39 E-value: 7.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2275 DEALQSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHK 2354
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2355 SEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAevEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEH 2434
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEA--EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2435 GAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAE 2514
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2515 ESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRS-----------------LLEDELYRLKNEV 2577
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLagavavligveaayeaaLEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2578 IAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAE-- 2655
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAArl 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2656 EEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKs 2735
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE- 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2736 SDAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKAssgkLDLELELNKLKNIAEETQQSK---------------LRAE 2800
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEEL----LEEEALEELPEPPDLEELERElerlereiealgpvnLLAI 787
|
....*...
gi 1678729579 2801 EEAEKLRK 2808
Cdd:COG1196 788 EEYEELEE 795
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
862-973 |
1.50e-34 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 130.04 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 862 DERDRVQKKTFTKWVNKHLIKRAesQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQ 941
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFG--KPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNN 78
|
90 100 110
....*....|....*....|....*....|..
gi 1678729579 942 VKLVNIRNDDIADGNPKLTLGLIWTVILHFQI 973
Cdd:cd21231 79 VDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
989-1091 |
5.55e-32 |
|
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: 122.73 E-value: 5.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 989 EKLLL-WSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSN-LENLEQAFNVAERDLGVTRLLDPE 1066
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1678729579 1067 DVDVQHPDEKSIITYVSSLYDVMPR 1091
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
842-969 |
1.24e-31 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 123.23 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 842 EDWDHSLDQPE--EKTWPHFIEDERDRVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR-E 918
Cdd:cd21316 26 DEWDNENSSARlfERSRIKALADEREAVQKKTFTKWVNSHL---ARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpT 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 919 KGRMRFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTVIL 969
Cdd:cd21316 103 KGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
989-1090 |
1.35e-31 |
|
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: 121.22 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 989 EKLLL-WSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDPED 1067
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1678729579 1068 VDVQHPDEKSIITYVSSLYDVMP 1090
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2334-2896 |
2.64e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 136.22 E-value: 2.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2334 HKQVIEETQKK-------------RIAEKELQHKS-EAEKEAAKQKQK------------ALDDLENLKKQAEEAERQVK 2387
Cdd:COG1196 170 YKERKEEAERKleateenlerledILGELERQLEPlERQAEKAERYRElkeelkeleaelLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2388 QAEVEKERQIkvAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEK 2467
Cdd:COG1196 250 ELEAELEELE--AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2468 WRQKANEALRLRLQAEEEahkkslaQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRkvadstaQQKLTAEQ 2547
Cdd:COG1196 328 LEEELEELEEELEELEEE-------LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-------EELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2548 ELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEAEA 2627
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2628 TKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHL----KTEAEIALKEKEAENERLRRA 2703
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVligvEAAYEAALEAALAAALQNIVV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2704 AEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELN 2783
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2784 KLKNIAEETQQSKLRAEEEAEKLRklaleeeKRRREAEEKVKKITAAEEEAARQRKIAQDELERLKKKAEEARKQKDEAD 2863
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGS-------AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
570 580 590
....*....|....*....|....*....|...
gi 1678729579 2864 VEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKE 2896
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
867-973 |
2.93e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 120.47 E-value: 2.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 867 VQKKTFTKWVNKHLIKRAESqhhVTDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHKLQNVQIALDFLRHRQVKL 944
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMS---VEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKL 80
|
90 100
....*....|....*....|....*....
gi 1678729579 945 VNIRNDDIADGNPKLTLGLIWTVILHFQI 973
Cdd:cd21227 81 VNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2607-3469 |
3.94e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 136.42 E-value: 3.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2607 KAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAI--AEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKT 2684
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKkkAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2685 EAEIALKEKEAEN-ERLRRAAEdeayQRKALEDEANQHKKEIE-----EKIVQLKKSSDAEMERQKAMVDDTLKQRRVVE 2758
Cdd:PTZ00121 1165 KAEEARKAEDAKKaEAARKAEE----VRKAEELRKAEDARKAEaarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2759 EEIRIlklnfEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQR 2838
Cdd:PTZ00121 1241 EAKKA-----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2839 KIaqdelERLKKKAEEARKQKDEADVEAEvqivaaqqaalkcstaehqvqsvlAQQKEDSIMHKKLKQeyekakklakea 2918
Cdd:PTZ00121 1316 KA-----DEAKKKAEEAKKKADAAKKKAE------------------------EAKKAAEAAKAEAEA------------ 1354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2919 eaakekaereaallrqQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEfEAAKRAQAEGAALKQKQQAD--AEMAKHK 2996
Cdd:PTZ00121 1355 ----------------AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKADEAKKKAEEDKKKADelKKAAAAK 1417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2997 KLAEQtLKQKFQVEQELTKVKLKLDDTDKQkslldDELQRLKDEVDDAvkqrgqveEELFKVKVQMEELLKLKLRIEDEN 3076
Cdd:PTZ00121 1418 KKADE-AKKKAEEKKKADEAKKKAEEAKKA-----DEAKKKAEEAKKA--------EEAKKKAEEAKKADEAKKKAEEAK 1483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3077 QRLLKKDKDNSQKFLAEEAenmkRLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKMlkEKMQAIQESSRLKAEAEM 3156
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEA----KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA--KKAEEKKKADELKKAEEL 1557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3157 LQRQKDLAQEQAQKLLEDKQLMQRRLEE-------ETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSeaqtKAEEEAK 3229
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEakkaeeaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK----KAEEEKK 1633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3230 KFKKQADKIAArlheteiatkekmtvvEKLEFERLNTSKEAGDLRdaiadlekdKARLKKEAEELQNKSKEMadaqQKQI 3309
Cdd:PTZ00121 1634 KVEQLKKKEAE----------------EKKKAEELKKAEEENKIK---------AAEEAKKAEEDKKKAEEA----KKAE 1684
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3310 EHEKTLLQQTFLTEREmllkkekliEEEKKKLESQFEEEAKKSKALKDEQERQKQQMEEEKKKlhatMHEALSKQKEAEK 3389
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEE---------AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKK 1751
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3390 EMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQLEEAQKEQHTVPDKElicvtTVDTTKKVYNGQNAGNAVDSAEKK 3469
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD-----IFDNFANIIEGGKEGNLVINDSKE 1826
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2148-2727 |
1.19e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 133.91 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2148 QEYVTLRTRYSEL-MTLTSQYIKFITETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQE 2226
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2227 LKLMMKEEVNRREIAAVDAEKQKQNIQLELHELKNLSEQQIKDKGQLvDEALQSRTKIEEEIYLIRIQLETTVKQKSTAE 2306
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL-EELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2307 SELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLkkQAEEAERQV 2386
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE--EEALEEAAE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2387 KQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELE 2466
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2467 KWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAE 2546
Cdd:COG1196 530 IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2547 QELIRLRADFDNAEQQRSLLEDELyrlkneviAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKEtmsnTEKSKQLLEAE 2626
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLE--------AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS----RRELLAALLEA 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2627 ATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAED 2706
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
570 580
....*....|....*....|.
gi 1678729579 2707 EAYQRKALEDEANQHKKEIEE 2727
Cdd:COG1196 758 EPPDLEELERELERLEREIEA 778
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
867-973 |
1.44e-30 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 118.57 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 867 VQKKTFTKWVNKHLIKRAESQhhVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQVKLVN 946
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKPP--IKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVN 79
|
90 100
....*....|....*....|....*..
gi 1678729579 947 IRNDDIADGNPKLTLGLIWTVILHFQI 973
Cdd:cd21232 80 IGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
973-1086 |
2.61e-30 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 118.01 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 973 ISDIQinglSEDMSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNV 1052
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1678729579 1053 AERDLGVTRLLDPEDV-DVQHPDEKSIITYVSSLY 1086
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYF 111
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
863-975 |
2.82e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 117.68 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 863 ERDRVQKKTFTKWVNKHLiKRAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPRE--KGRMRFHKLQNVQIALDFLRHR 940
Cdd:cd21191 1 ERENVQKRTFTRWINLHL-EKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDS 79
|
90 100 110
....*....|....*....|....*....|....*
gi 1678729579 941 QVKLVNIRNDDIADGNPKLTLGLIWTVILHFQISD 975
Cdd:cd21191 80 NVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
985-1083 |
4.52e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 116.86 E-value: 4.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 985 MSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLD 1064
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1678729579 1065 PEDVDVQHPDEKSIITYVS 1083
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2317-3294 |
7.40e-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: 131.72 E-value: 7.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2317 AEAERLRKVAQEEA--EKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQkqkalddLENLKKQAEEAER--QVKQAEVE 2392
Cdd:TIGR02168 152 AKPEERRAIFEEAAgiSKYKERRKETERKLERTRENLDRLEDILNELERQ-------LKSLERQAEKAERykELKAELRE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2393 KERQI-------KVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKEL 2465
Cdd:TIGR02168 225 LELALlvlrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2466 EKWRQKANEALRLRLQAEEEahkkslaQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTA 2545
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQ-------LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2546 EQELIRLRADFDNAEQQRSLLEDELYRLKNEViaaqqqrKQLEDELAKVRSEmdiliqlkskaeketmsnteKSKQLLEA 2625
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARL-------ERLEDRRERLQQE--------------------IEELLKKL 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2626 EATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIAlkekeaenERLRRAAE 2705
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL--------ERLQENLE 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2706 DEAYQRKALEDEANQhkkeieekivqlkkssdaemerqKAMVDDTLKQRRVVEEEirilklnFEKAssgkLDLELELNkL 2785
Cdd:TIGR02168 503 GFSEGVKALLKNQSG-----------------------LSGILGVLSELISVDEG-------YEAA----IEAALGGR-L 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2786 KNIAEETQQSklrAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRKIAQDELERLKKKAEEARK-------- 2857
Cdd:TIGR02168 548 QAVVVENLNA---AKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllgg 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2858 -----------------QKDEADVEAEVQIVAAQQAALKCSTAEHQvqSVLAQQKEdsimHKKLKQEYEKAKKLAKEAEA 2920
Cdd:TIGR02168 625 vlvvddldnalelakklRPGYRIVTLDGDLVRPGGVITGGSAKTNS--SILERRRE----IEELEEKIEELEEKIAELEK 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2921 AKEKAEREAALLRQQAEEAERQKAAAEQEAAIqakAQEDAERLRKEAEFEAAKRAQAEGA---ALKQKQQADAEMAKHKK 2997
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISA---LRKDLARLEAEVEQLEERIAQLSKElteLEAEIEELEERLEEAEE 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2998 LAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKlklRIEDENQ 3077
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE---QIEELSE 852
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3078 RLLKkdkdnSQKFLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEML 3157
Cdd:TIGR02168 853 DIES-----LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3158 QRQKDLAQEQAQKLLEdkqlmqrRLeeeTEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTK-------AEEEAKK 3230
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQE-------RL---SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEE 997
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 3231 FKKqadkiaarlheteiatkekmtvveklEFERLNTSKEagDLRDAIADLEKDKARLKKEAEEL 3294
Cdd:TIGR02168 998 LKE--------------------------RYDFLTAQKE--DLTEAKETLEEAIEEIDREARER 1033
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2172-3065 |
1.39e-29 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 131.10 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2172 TETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELK-------LMMKEEVNRREI---A 2241
Cdd:NF041483 312 EEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKaartaeeVLTKASEDAKATtraA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2242 AVDAEKQKQNIQLELHELKNLSEQQIKD-KGQLVDEALQSRTK---IEEEIYLIRIQLEtTVKQKSTAESE--------- 2308
Cdd:NF041483 392 AEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKtveLQEEARRLRGEAE-QLRAEAVAEGErirgearre 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2309 -LKQLRERA-----------AEAERLRKVAQEEAEKLHKQVIEE-TQKKRIAEKELQHkseAEKEAAKQKQKALDDLENL 2375
Cdd:NF041483 471 aVQQIEEAArtaeelltkakADADELRSTATAESERVRTEAIERaTTLRRQAEETLER---TRAEAERLRAEAEEQAEEV 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2376 KKQAEEAERQVKQaevEKERQIKvahvAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQ---- 2451
Cdd:NF041483 548 RAAAERAARELRE---ETERAIA----ARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLrtea 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2452 -EDAINAREEAEKELEKWRQKA------------NEALRLRLQAEEEAHK-KSLAQEDAEKQKEE----AER----EAKK 2509
Cdd:NF041483 621 aERIRTLQAQAEQEAERLRTEAaadasaaraegeNVAVRLRSEAAAEAERlKSEAQESADRVRAEaaaaAERvgteAAEA 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2510 RAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELI---RLRADFDNAEQQRsLLEDELYRLKNEVIAAQQQRKQ 2586
Cdd:NF041483 701 LAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasaRKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQ 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2587 LEDELAKVRSEMDILIQ-LKSKAEKEtmsnTEKSKQLLEAEATKMRDVAeEAGKLRAiAEEAKHQRQVAEEEAARQRAEA 2665
Cdd:NF041483 780 VRDSVAGLQEQAEEEIAgLRSAAEHA----AERTRTEAQEEADRVRSDA-YAERERA-SEDANRLRREAQEETEAAKALA 853
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2666 ERILKEklaAISEATHLKTEA-EIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQK 2744
Cdd:NF041483 854 ERTVSE---AIAEAERLRSDAsEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAAAQADRLIGEATSEAERLT 930
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2745 AMVDDTLKQRR--VVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEET----QQSKLRAEEEAEKLRklaleeekrrr 2818
Cdd:NF041483 931 AEARAEAERLRdeARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETvgsaQQHAERIRTEAERVK----------- 999
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2819 eaeekvkkiTAAEEEAARQRKIAQDELERL--------KKKAEEARKQKD----EADVEAEVQIVAAQQAALKCST-AEH 2885
Cdd:NF041483 1000 ---------AEAAAEAERLRTEAREEADRTldearkdaNKRRSEAAEQADtlitEAAAEADQLTAKAQEEALRTTTeAEA 1070
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2886 QVQSVL--AQQKEDSIMHKKLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAeRQKAAAEQEAAIQAKAQEDAERL 2963
Cdd:NF041483 1071 QADTMVgaARKEAERIVAEATVEGNSLVEKARTDADELLVGARRDATAIRERAEEL-RDRITGEIEELHERARRESAEQM 1149
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2964 RKEAE-----FEAAKRAQAEGAALKQKQQADAEMAKHK------KLAEQTLKQKFQVEQELTKvklkldDTDKQKSLLDD 3032
Cdd:NF041483 1150 KSAGErcdalVKAAEEQLAEAEAKAKELVSDANSEASKvriaavKKAEGLLKEAEQKKAELVR------EAEKIKAEAEA 1223
|
970 980 990
....*....|....*....|....*....|....*..
gi 1678729579 3033 ELQRL----KDEVDDAVKQRGQVEEELFKVKVQMEEL 3065
Cdd:NF041483 1224 EAKRTveegKRELDVLVRRREDINAEISRVQDVLEAL 1260
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
866-974 |
5.19e-29 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 114.47 E-value: 5.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 866 RVQKKTFTKWVNKHLIKRAEsqhHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGR--MRFHKLQNVQIALDFLRHRQ-V 942
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANK---HIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgI 90
|
90 100 110
....*....|....*....|....*....|..
gi 1678729579 943 KLVNIRNDDIADGNPKLTLGLIWTVILHFQIS 974
Cdd:cd21311 91 KIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
973-1086 |
5.59e-29 |
|
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: 114.41 E-value: 5.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 973 ISDIQInglsEDMSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNV 1052
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1678729579 1053 AERDLGVTRLLDPED-VDVQHPDEKSIITYVSSLY 1086
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFY 111
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
971-1086 |
8.33e-29 |
|
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: 114.03 E-value: 8.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 971 FQISDIQInglsEDMSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAF 1050
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1678729579 1051 NVAERDLGVTRLLDPED-VDVQHPDEKSIITYVSSLY 1086
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFY 114
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
866-971 |
3.51e-28 |
|
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: 111.42 E-value: 3.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 866 RVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHKLQNVQIALDFLRHRQV 942
Cdd:cd21183 3 RIQANTFTRWCNEHL---KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHI 79
|
90 100
....*....|....*....|....*....
gi 1678729579 943 KLVNIRNDDIADGNPKLTLGLIWTVILHF 971
Cdd:cd21183 80 KLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
991-1086 |
5.99e-27 |
|
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: 107.82 E-value: 5.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 991 LLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDPED-VD 1069
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1678729579 1070 VQHPDEKSIITYVSSLY 1086
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2148-2863 |
4.01e-26 |
|
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: 119.39 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2148 QEYVTLRTRYSEL-MTLTSQYIKFITETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQE 2226
Cdd:TIGR02168 213 ERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2227 LKlmmkeevnrREIAAVDAEKQKQNIQLELhelknlSEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAE 2306
Cdd:TIGR02168 293 LA---------NEISRLEQQKQILRERLAN------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2307 SELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQV 2386
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2387 KQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHgavlQLQQEAAHLKKQQE------DAINAREE 2460
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA----QLQARLDSLERLQEnlegfsEGVKALLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2461 AEKEL--------------EKWRQKANEALRLRLQA----EEEAHKK---SLAQEDAEK------------QKEEAEREA 2507
Cdd:TIGR02168 514 NQSGLsgilgvlselisvdEGYEAAIEAALGGRLQAvvveNLNAAKKaiaFLKQNELGRvtflpldsikgtEIQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2508 KKRAKAEESALKQKDMAEKELER-------QRKVADS----TAQQKLTAEQELI------RLRADF-------------- 2556
Cdd:TIGR02168 594 LKNIEGFLGVAKDLVKFDPKLRKalsyllgGVLVVDDldnaLELAKKLRPGYRIvtldgdLVRPGGvitggsaktnssil 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2557 ------DNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEAEATKM 2630
Cdd:TIGR02168 674 errreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2631 RDVAEEAGKLRAIA---EEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEiALKEKEAEN-ERLRRAAED 2706
Cdd:TIGR02168 754 KELTELEAEIEELEerlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT-LLNEEAANLrERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2707 EAYQRKALEDEANQhKKEIEEKIVQLKKS---SDAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELN 2783
Cdd:TIGR02168 833 IAATERRLEDLEEQ-IEELSEDIESLAAEieeLEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2784 KLKNIAEETQQSKLRAEEEAEKLR--------KLALEEEKRRREAEEKVKKITAAEEEAARQ-----RKIAQ-------- 2842
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEvridnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRRlkrleNKIKElgpvnlaa 991
|
810 820
....*....|....*....|..
gi 1678729579 2843 -DELERLKKKAEEARKQKDEAD 2863
Cdd:TIGR02168 992 iEEYEELKERYDFLTAQKEDLT 1013
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
848-973 |
5.84e-26 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 106.00 E-value: 5.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 848 LDQPEEKTWPHFIEDERDRVQKKTFTKWVNkHLIKRAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHK 926
Cdd:cd21247 1 MDTEYEKGHIRKLQEQRMTMQKKTFTKWMN-NVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHF 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1678729579 927 LQNVQIALDFLRHR-QVKLVNIRNddIADGNPKLTLGLIWTVILHFQI 973
Cdd:cd21247 80 LENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
985-1091 |
1.11e-25 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 104.29 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 985 MSAKEKLLLWSQRMTGDY-QNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVY--RQSNLENLEQAFNVAERDLGVTR 1061
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1678729579 1062 -LLDPEDVDvqHPDEKSIITYVSSLYDVMPR 1091
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2443-3389 |
1.25e-25 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 118.00 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2443 EAAHLKKQQEDAINAREEAEKELEKWRQKANEALR------------LRLQAEEEAHKkslAQEDAEKQKEEAEREAKKr 2510
Cdd:NF041483 23 EMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRslasrpaydgadIGYQAEQLLRN---AQIQADQLRADAERELRD- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2511 AKAEESALKQkDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDN--------AEQQRSLLEDELYRLKNEviaaqq 2582
Cdd:NF041483 99 ARAQTQRILQ-EHAEHQARLQAELHTEAVQRRQQLDQELAERRQTVEShvnenvawAEQLRARTESQARRLLDE------ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2583 QRKQLEDELAKVRSEMDiliQLKSKAEKETMSNTEKSKQllEAEATKMRDVAEEAGKLRAIAEEAK----HQRQ-----V 2653
Cdd:NF041483 172 SRAEAEQALAAARAEAE---RLAEEARQRLGSEAESARA--EAEAILRRARKDAERLLNAASTQAQeatdHAEQlrsstA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2654 AEEEAARQRA-EAERILKEKLAaiseathlktEAEIALKEKEAENERLRRAAEDEAYQRKALEDEAN-QHKKEIEEKIVQ 2731
Cdd:NF041483 247 AESDQARRQAaELSRAAEQRMQ----------EAEEALREARAEAEKVVAEAKEAAAKQLASAESANeQRTRTAKEEIAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2732 LKKSSDAEMERQKAMVDDTLKQRRVVEEeiRILKLNFEKA-SSGKLDLELELNKLKNIAEE--------TQQSKLRAEEE 2802
Cdd:NF041483 317 LVGEATKEAEALKAEAEQALADARAEAE--KLVAEAAEKArTVAAEDTAAQLAKAARTAEEvltkasedAKATTRAAAEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2803 AEKLRKlaleeekrrreaeekvkkitAAEEEAARQRKIAQDELERLKKKA---------------EEARKQKDEAD---- 2863
Cdd:NF041483 395 AERIRR--------------------EAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGEAEqlra 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2864 --------VEAEVQIVAAQQAALKCSTAEhqvqSVLAQQKEDSimhKKLKQeyekakKLAKEAEAAKEKAEREAALLRQQ 2935
Cdd:NF041483 455 eavaegerIRGEARREAVQQIEEAARTAE----ELLTKAKADA---DELRS------TATAESERVRTEAIERATTLRRQ 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2936 AEEA-ERQKaaaEQEAAIQAKAQEDAERLRKEAEFEAAK-RAQAEGAALKQKQQADAEMAKHKKLAEQTLKqkfQVEQEL 3013
Cdd:NF041483 522 AEETlERTR---AEAERLRAEAEEQAEEVRAAAERAARElREETERAIAARQAEAAEELTRLHTEAEERLT---AAEEAL 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3014 TKVKlklDDTDKQKSLLDDELQRLKDEVDDAVKQ-RGQVEEELFKVKVQME----------ELLKLKLRIE--DENQRLL 3080
Cdd:NF041483 596 ADAR---AEAERIRREAAEETERLRTEAAERIRTlQAQAEQEAERLRTEAAadasaaraegENVAVRLRSEaaAEAERLK 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3081 KKDKDNSQKFLAEEAENMKRLAEDAAR-LSVESQEAARLRQIAEDDLIQQRALADkmlkekmqaiQESSRlkaeaemlqr 3159
Cdd:NF041483 673 SEAQESADRVRAEAAAAAERVGTEAAEaLAAAQEEAARRRREAEETLGSARAEAD----------QERER---------- 732
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3160 qkdlAQEQAQKLLEDKqlmQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQV-SQLSEAQTKAEEE----------- 3227
Cdd:NF041483 733 ----AREQSEELLASA---RKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVrDSVAGLQEQAEEEiaglrsaaeha 805
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3228 AKKFKKQADKIAARLHETEIATKEKM------------------------TVVEKL-EFERL--NTSKEAGDLR----DA 3276
Cdd:NF041483 806 AERTRTEAQEEADRVRSDAYAERERAsedanrlrreaqeeteaakalaerTVSEAIaEAERLrsDASEYAQRVRteasDT 885
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3277 IADLEKDKARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQQTFLTEremllkkeklIEEEKKKLESQFEEEAKKSKALK 3356
Cdd:NF041483 886 LASAEQDAARTRADAREDANRIRSDAAAQADRLIGEATSEAERLTAE----------ARAEAERLRDEARAEAERVRADA 955
|
1050 1060 1070
....*....|....*....|....*....|....*
gi 1678729579 3357 DEQ-ERQKQQMEEEKKKLHATMHEAL-SKQKEAEK 3389
Cdd:NF041483 956 AAQaEQLIAEATGEAERLRAEAAETVgSAQQHAER 990
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2494-3440 |
1.77e-25 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 117.38 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2494 EDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRaDFDNAEQQRSLLEDELYRL 2573
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALE-YYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2574 KNEVIaaQQQRKQLEDELAKVRSEMDILIQlKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQV 2653
Cdd:pfam02463 231 YLKLN--EERIDLLQELLRDEQEEIESSKQ-EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2654 AEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAyqrkALEDEANQHKKEIEEKIVQLK 2733
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE----KLQEKLEQLEEELLAKKKLES 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2734 KSSDAEMERQKamvddtlKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKlRKLALEE 2813
Cdd:pfam02463 384 ERLSSAAKLKE-------EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE-EKEELEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2814 EKRRREAEEKVKKITAAEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEAEVQIVAaqqaalkcstaehqvqsVLAQ 2893
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA-----------------LIKD 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2894 QKEDSIMHKKLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAK 2973
Cdd:pfam02463 519 GVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2974 RAQAEGAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEE 3053
Cdd:pfam02463 599 IDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEI 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3054 ELFKVKVQMEELlKLKLRIEDENQRLLKKDKDNSQKFLAEEAENMKrlaedAARLSVESQEAARLRQIAEDDLIQQRALA 3133
Cdd:pfam02463 679 QELQEKAESELA-KEEILRRQLEIKKKEQREKEELKKLKLEAEELL-----ADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3134 DKMLKEKMQAIQEssrlkaEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQ 3213
Cdd:pfam02463 753 EKSRLKKEEKEEE------KSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3214 VSQLSEAQTKAEEEAKKFKKQADKIAARLHET--EIATKEKMTVVEKLEFERLntskEAGDLRDAIADLEKDKARLKKEA 3291
Cdd:pfam02463 827 EEKIKEEELEELALELKEEQKLEKLAEEELERleEEITKEELLQELLLKEEEL----EEQKLKDELESKEEKEKEEKKEL 902
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3292 EELQNKSKEMADAQQK--QIEHEKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQK--QQME 3367
Cdd:pfam02463 903 EEESQKLNLLEEKENEieERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNlmAIEE 982
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 3368 EEKKKLHATMHEALSKQKEAEKEMLSKQKEMQELEKKRLEQEIILAdENQKLREKLQQLEEAQKEQHTVPDKE 3440
Cdd:pfam02463 983 FEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVS-INKGWNKVFFYLELGGSAELRLEDPD 1054
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
973-1086 |
1.98e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 104.42 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 973 ISDIQInglsEDMSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNV 1052
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1678729579 1053 AERDLGVTRLLDPED-VDVQHPDEKSIITYVSSLY 1086
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFY 111
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2175-3112 |
5.26e-25 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 115.84 E-value: 5.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2175 QRRLEDEEKAA----KKLKAEEQKKMAEMQAELDKQ---KQLAAAHAKAIAKAEKEAQE-LKLMMKEEVNRREIAAVDAE 2246
Cdd:pfam02463 153 ERRLEIEEEAAgsrlKRKKKEALKKLIEETENLAELiidLEELKLQELKLKEQAKKALEyYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2247 KQKQNIQLELHELKNLSEQQIKDKGQLVDealqsrtKIEEEIYLIRIQLETTVKQKSTAESELKQLRERAAEAERLRKVA 2326
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIE-------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2327 QEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKqkaldDLENLKKQAEEAERQVKQAEVEKERQIKVAHVAAQK 2406
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL-----KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2407 SAAAELQSKHSSFVEKTSKLEESLKQehgavlqlQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEEEA 2486
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKE--------AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2487 HKKSLAQEdaEKQKEEAEREAKKRAKAEESALKQKDmaEKELERQRKVADSTAQQKltAEQELIRLRADFDNAEQQRSLL 2566
Cdd:pfam02463 453 LEKQELKL--LKDELELKKSEDLLKETQLVKLQEQL--ELLLSRQKLEERSQKESK--ARSGLKVLLALIKDGVGGRIIS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2567 EDELYRLKnEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEE 2646
Cdd:pfam02463 527 AHGRLGDL-GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2647 AKHQRQVAEEEAARQRAeaerilkeKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIE 2726
Cdd:pfam02463 606 AQLDKATLEADEDDKRA--------KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2727 EKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKldLELELNKLKNIAEETQQSKLRAEEEAEKL 2806
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR--VQEAQDKINEELKLLKQKIDEEEEEEEKS 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2807 RKLALEEEKRRREAEEKVKKItAAEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEAEVQivaaQQAALKCSTAEHQ 2886
Cdd:pfam02463 756 RLKKEEKEEEKSELSLKEKEL-AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL----EEEQLLIEQEEKI 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2887 VQSVLAQQKEDSIMHKKLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKE 2966
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLN 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2967 AEFEAAKRAQAEGAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLkdevDDAVK 3046
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE----EFEEK 986
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678729579 3047 QRGQVEEELFKVKVQMEELLKLKLRIEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDAARLSVES 3112
Cdd:pfam02463 987 EERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLED 1052
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2458-3393 |
6.13e-25 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 115.45 E-value: 6.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2458 REEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQkdmaEKELERQRKVAds 2537
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY----LKLNEERIDLL-- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2538 taQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQ-QRKQLEDELAKVRSEMDILIQLKSKAEKETmSNT 2616
Cdd:pfam02463 243 --QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEeELKLLAKEEEELKSELLKLERRKVDDEEKL-KES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2617 EKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAE 2696
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2697 NERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKamvddtlkqrrVVEEEIRILKLNFEKASSGKL 2776
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT-----------EEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2777 DLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRKIAqdeLERLKKKAEEAR 2856
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD---LGVAVENYKVAI 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2857 KQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKEDSIMHKKLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQA 2936
Cdd:pfam02463 546 STAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2937 EEAERQKAAAEQEAAIQAK----------AQEDAERLRKEAEFEAAKRAQAEGAALKQKQQADAEMAKHKKLAEQTLKQK 3006
Cdd:pfam02463 626 EGILKDTELTKLKESAKAKesglrkgvslEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3007 FQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKvQMEELLKLKLRIEDENQRLLKKDKDN 3086
Cdd:pfam02463 706 QREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK-KEEKEEEKSELSLKEKELAEEREKTE 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3087 SQKFLAEEAENMKRLAEDAARLsvESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQE 3166
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRAL--EEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEE 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3167 QAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQleivaEAEKLKLQVSQLSEAQTKAEEEAKkfkkqadkiaarLHETE 3246
Cdd:pfam02463 863 ITKEELLQELLLKEEELEEQKLKDELESKEEKEK-----EEKKELEEESQKLNLLEEKENEIE------------ERIKE 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3247 IATKEKM--TVVEKLEFERLNTSKEAGDLRDaiaDLEKDKARLKKEAEELQNKsKEMADAQQKQIEhektllqqtfltER 3324
Cdd:pfam02463 926 EAEILLKyeEEPEELLLEEADEKEKEENNKE---EEEERNKRLLLAKEELGKV-NLMAIEEFEEKE------------ER 989
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678729579 3325 EMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMLS 3393
Cdd:pfam02463 990 YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFS 1058
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2640-3441 |
1.58e-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: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2640 LRAIAEEA------KHQRQVAEEEAARQRAEAERI------LKEKLaaiseaTHLKTEAEIALKEKEAENErLRRAAEDE 2707
Cdd:TIGR02168 157 RRAIFEEAagiskyKERRKETERKLERTRENLDRLedilneLERQL------KSLERQAEKAERYKELKAE-LRELELAL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2708 AYQR-KALEDEANQHKKEIEEKiVQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLK 2786
Cdd:TIGR02168 230 LVLRlEELREELEELQEELKEA-EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2787 NIAEETQQSKLRAEEEAEKLRKlaleeekrrreaeekvKKITAAEEEAARQRKIAQD--ELERLKKKAEEARKQKdeadV 2864
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELES----------------KLDELAEELAELEEKLEELkeELESLEAELEELEAEL----E 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2865 EAEVQIVAAQQAALKCSTAEHQV-QSVLAQQKEDSIMHKKLKQeyekakKLAKEAEAAKEKAEREAALLRQQAEEAERQK 2943
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLeLQIASLNNEIERLEARLER------LEDRRERLQQEIEELLKKLEEAELKELQAEL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2944 AAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQAEGAALKQKQQADAEMAKHKKLAEQtLKQKFQVEQELTKVKLKLDDT 3023
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN-LEGFSEGVKALLKNQSGLSGI 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3024 DKQKS---------------LLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLLKKDKDNSQ 3088
Cdd:TIGR02168 522 LGVLSelisvdegyeaaieaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFL 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3089 KFLAEEAENMKRLA----------------EDAARLSVESQEAARLrQIAEDDLIQQRALADKMLKEKMQAI----QESS 3148
Cdd:TIGR02168 602 GVAKDLVKFDPKLRkalsyllggvlvvddlDNALELAKKLRPGYRI-VTLDGDLVRPGGVITGGSAKTNSSIlerrREIE 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3149 RLKAEAEMLQRQKDLAQEQAQKLLEDkqlmQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEA 3228
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3229 KKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMADAQQKQ 3308
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3309 IEHEKTLLQQtfLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAE 3388
Cdd:TIGR02168 837 ERRLEDLEEQ--IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 3389 KEMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQLEEAQKEQHTVPDKEL 3441
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE 967
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2079-2865 |
2.74e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 113.61 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2079 KEQLSQEKKLLEEIENNKDNVDECQKYAKAYINSIKDYE--------LQLVAYNAQADPLASPLKKTKldsasdniiQEY 2150
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRelelallvLRLEELREELEELQEELKEAE---------EEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2151 VTLRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELKLM 2230
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2231 mKEEVNRREIAAVDAEKQKQNIQLELHELKNL---SEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAES 2307
Cdd:TIGR02168 336 -AEELAELEEKLEELKEELESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2308 ELKQLRERAAEAERlrkvAQEEAEKlhkqvieetqkkriaeKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVK 2387
Cdd:TIGR02168 415 RRERLQQEIEELLK----KLEEAEL----------------KELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2388 QAEVEKERQikVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQqeaahlkkqqeDAINAREEAEKELEK 2467
Cdd:TIGR02168 475 QALDAAERE--LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLS-----------ELISVDEGYEAAIEA 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2468 wrqkaneALRLRLQA----EEEAHKK---SLAQEDAEK------------QKEEAEREAKKRAKAEESALKQKDMAEKEL 2528
Cdd:TIGR02168 542 -------ALGGRLQAvvveNLNAAKKaiaFLKQNELGRvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2529 ER-------QRKVADS----TAQQKLTAEQELI------RLRADF------DNAEQQRSLLEDELYRLKNEVIAAQQQRK 2585
Cdd:TIGR02168 615 RKalsyllgGVLVVDDldnaLELAKKLRPGYRIvtldgdLVRPGGvitggsAKTNSSILERRREIEELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2586 QLEDELAKVRSEMDILIQLKSKAEKETmsnTEKSKQLLEAEAtkmrdvaeeagklRAIAEEAKHQRqvAEEEAARQRAEA 2665
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKEL---EELSRQISALRK-------------DLARLEAEVEQ--LEERIAQLSKEL 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2666 ERILKEK---LAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKiVQLKKSSDAEMER 2742
Cdd:TIGR02168 757 TELEAEIeelEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL-RERLESLERRIAA 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2743 QKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRklaleeekrrreaee 2822
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS--------------- 900
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1678729579 2823 kvkkitAAEEEAARQRKIAQDELERLKKKAEEARKQKDEADVE 2865
Cdd:TIGR02168 901 ------EELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
866-971 |
2.86e-24 |
|
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: 100.26 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 866 RVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHKLQNVQIALDFLRHRQV 942
Cdd:cd21228 3 KIQQNTFTRWCNEHL---KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESI 79
|
90 100
....*....|....*....|....*....
gi 1678729579 943 KLVNIRNDDIADGNPKLTLGLIWTVILHF 971
Cdd:cd21228 80 KLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
989-1088 |
2.89e-24 |
|
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: 100.44 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 989 EKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDPED- 1067
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1678729579 1068 VDVQHPDEKSIITYVSSLYDV 1088
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2584-3452 |
2.97e-24 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 113.14 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2584 RKQLEDELAkvRSEMDILiqlKSKAEKETMSNTEKSKQLLeaeatkmRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRA 2663
Cdd:pfam02463 155 RLEIEEEAA--GSRLKRK---KKEALKKLIEETENLAELI-------IDLEELKLQELKLKEQAKKALEYYQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2664 EAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKivQLKKSSDAEMERQ 2743
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE--LKLLAKEEEELKS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2744 KAmvdDTLKQRRVVEEEirilKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKrrREAEEK 2823
Cdd:pfam02463 301 EL---LKLERRKVDDEE----KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ--EKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2824 VKKITAAEEEAARQR----KIAQDELERLKKKAEEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKEDS- 2898
Cdd:pfam02463 372 EEELLAKKKLESERLssaaKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKe 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2899 ------IMHKKLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAA 2972
Cdd:pfam02463 452 elekqeLKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2973 KRAQAEGAALKQKQ---QADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRG 3049
Cdd:pfam02463 532 GDLGVAVENYKVAIstaVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3050 QVEEElFKVKVQMEELLKLKLRIEDENQRLLKKDKDNSQKFlaeeAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQ 3129
Cdd:pfam02463 612 TLEAD-EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKG----VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAE 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3130 RALA-DKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEEtEEYQKSLEAERRRQLEIVAEAE 3208
Cdd:pfam02463 687 SELAkEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQ-KIDEEEEEEEKSRLKKEEKEEE 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3209 KLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLK 3288
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3289 KEAEELQNKSKEMADAQQKQIEHEKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQQMEE 3368
Cdd:pfam02463 846 QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3369 EKKKL--HATMHEALSKQKEAEKEMLSKQKEMQELEKKRLEQEI-------ILADENQKLREKLQQLEEAQKEQHTVPDK 3439
Cdd:pfam02463 926 EAEILlkYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKeelgkvnLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890
....*....|...
gi 1678729579 3440 ELICVTTVDTTKK 3452
Cdd:pfam02463 1006 KLIRAIIEETCQR 1018
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
973-1086 |
4.19e-24 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 100.53 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 973 ISDIQInglsEDMSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNV 1052
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1678729579 1053 AERDLGVTRLLDPED-VDVQHPDEKSIITYVSSLY 1086
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFY 111
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
986-1086 |
4.27e-24 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 99.81 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERdLGVTRLLDP 1065
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 1678729579 1066 EDVDVQH-PDEKSIITYVSSLY 1086
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
866-974 |
4.40e-24 |
|
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: 100.49 E-value: 4.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 866 RVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPRE---KGRMRFHKLQNVQIALDFLRHRQV 942
Cdd:cd21310 15 KIQQNTFTRWCNEHL---KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHI 91
|
90 100 110
....*....|....*....|....*....|..
gi 1678729579 943 KLVNIRNDDIADGNPKLTLGLIWTVILHFQIS 974
Cdd:cd21310 92 KLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
870-970 |
5.90e-24 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 99.31 E-value: 5.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 870 KTFTKWVNKHLIKRAESqhHVTDLYEDLRDGHNLISLLEVLSGDTLPREK---GRMRFHKLQNVQIALDFLRHRQVKLVN 946
Cdd:smart00033 1 KTLLRWVNSLLAEYDKP--PVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVL 78
|
90 100
....*....|....*....|....
gi 1678729579 947 IRNDDIADGnPKLTLGLIWTVILH 970
Cdd:smart00033 79 FEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
987-1090 |
1.89e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 97.94 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 987 AKEKLLLWSQRMTGDYqNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDPE 1066
Cdd:cd21245 4 AIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPE 82
|
90 100
....*....|....*....|....
gi 1678729579 1067 DVDVQHPDEKSIITYVSSLYDVMP 1090
Cdd:cd21245 83 DVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2620-3291 |
1.99e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.41 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2620 KQLLEAEAT--KMRDVAEEAGKLRAIAEEAK-----HQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKE 2692
Cdd:COG1196 222 LKELEAELLllKLRELEAELEELEAELEELEaeleeLEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2693 KEAENERLRRAAEDEAYQRKALEDEanqhkkEIEEKIVQLKkssdAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKAS 2772
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELA------ELEEELEELE----EELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2773 SGKLDLELELnklkniaEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRKIAQDELERLKKKA 2852
Cdd:COG1196 372 AELAEAEEEL-------EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2853 EEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKEDSIMHKKLKQeyekakklakeaeaakekaereaalL 2932
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE-------------------------A 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2933 RQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAqAEGAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQE 3012
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA-ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3013 LTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQmeellkLKLRIEDENQRLLKKDKDNSQKFLA 3092
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL------VAARLEAALRRAVTLAGRLREVTLE 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3093 EEAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQKLL 3172
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3173 EDKQLMQRRLEEETEEYQKSLEA----ERRRQLEivAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLheteia 3248
Cdd:COG1196 733 EREELLEELLEEEELLEEEALEElpepPDLEELE--RELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQR------ 804
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1678729579 3249 tkekmtvveklefERLNTSKEagDLRDAIADLEKDKARLKKEA 3291
Cdd:COG1196 805 -------------EDLEEARE--TLEEAIEEIDRETRERFLET 832
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2003-2808 |
8.22e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.61 E-value: 8.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2003 ERDVELDHYRQHLSGLQDRWKAVFAQMDIRQRELEQLGRQLGYYHESYDWLIHWITDAKERQEKIQAVsITDSKTLKEQL 2082
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-LYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2083 SQEKKLLEEiennkdnvdecqkyakayinSIKDYELQLVAYNAQADPLASPLKKTKLDSASdniiqeyvtLRTRYSELMt 2162
Cdd:TIGR02168 301 EQQKQILRE--------------------RLANLERQLEELEAQLEELESKLDELAEELAE---------LEEKLEELK- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2163 ltsqyikfitETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELKLMMKEEVNRREIAa 2242
Cdd:TIGR02168 351 ----------EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2243 vDAEKQKQNIQLELHELKNLSEqQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLRERAAEAERL 2322
Cdd:TIGR02168 420 -QQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2323 rkvaQEEAEKLHKQVIEETQKK--------RIAEK-ELQHKSEAEKEAAKQK--QKALDDLENLKKQAEEAerqVKQAEV 2391
Cdd:TIGR02168 498 ----QENLEGFSEGVKALLKNQsglsgilgVLSELiSVDEGYEAAIEAALGGrlQAVVVENLNAAKKAIAF---LKQNEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2392 EKERQIKVAHVAAQKSAAAELQSK--HSSFVEKTSKLEESLKQEHGAVLQL---------QQEAAHLKKQ---------- 2450
Cdd:TIGR02168 571 GRVTFLPLDSIKGTEIQGNDREILknIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddLDNALELAKKlrpgyrivtl 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2451 --------------QEDAINAREEAEKELEKWRQKANEalrlrlqAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEES 2516
Cdd:TIGR02168 651 dgdlvrpggvitggSAKTNSSILERRREIEELEEKIEE-------LEEKIAELEKALAELRKELEELEEELEQLRKELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2517 ALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRS 2596
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2597 EMDILIQLKSKAEKETMSNTEKSKQL---LEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKl 2673
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLerrIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER- 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2674 AAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKK--SSDAEMERQ--KAMVDD 2749
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErlSEEYSLTLEeaEALENK 962
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678729579 2750 TLKQRRVVEEEIRilklnfekassgklDLELELNKLKNIaeetqqsKLRAEEEAEKLRK 2808
Cdd:TIGR02168 963 IEDDEEEARRRLK--------------RLENKIKELGPV-------NLAAIEEYEELKE 1000
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
989-1089 |
1.03e-22 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 95.61 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 989 EKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDPEDV 1068
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1678729579 1069 DVQHPDEKSIITYVSSLYDVM 1089
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
991-1086 |
1.14e-22 |
|
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: 95.68 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 991 LLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDPED-VD 1069
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1678729579 1070 VQHPDEKSIITYVSSLY 1086
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
867-973 |
1.39e-22 |
|
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: 95.43 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 867 VQKKTFTKWVNKHLIKRAESQHhVTDLYEDLRDGHNLISLLEVLSGDTLP-REKGRMRFHKLQNVQIALDFLRHRQ-VKL 944
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGVR-VTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPK 80
|
90 100
....*....|....*....|....*....
gi 1678729579 945 VNIRNDDIADGNPKLTLGLIWTVILHFQI 973
Cdd:pfam00307 81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2832-3432 |
1.59e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.33 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2832 EEAARQRKIAQDELER-----------LKKKAEEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKEDSIM 2900
Cdd:COG1196 175 EEAERKLEATEENLERledilgelerqLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2901 HKKLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQAEGA 2980
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2981 ALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKV 3060
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3061 QMEELLKLKLRIEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKMLKEK 3140
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3141 MQAIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEA 3220
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3221 QTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLntSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKE 3300
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL--GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3301 MADAQQKQIEHEKTLLQQTFLTEREMLLKkeklieeekkklesqfEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEA 3380
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAEL----------------EELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1678729579 3381 LSKQKEAEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQLEEAQKE 3432
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2066-2735 |
1.91e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.45 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2066 KIQAVSITDSKTLKEQLSQEKK--LLEEIENNKDNVDECQKYAKAYINSIKDYELQLVAYNAQADPLAspLKKTKLDSAS 2143
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2144 DNIIQEYVTLRTRYSELmtltSQYIKFITETQRRLEDEEKAA-------KKLKAEEQKKMAEMQAELDKQKQLAAAHAKA 2216
Cdd:TIGR02168 284 EELQKELYALANEISRL----EQQKQILRERLANLERQLEELeaqleelESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2217 IAKAEKEAQELKLMMK---EEVNRREIAAVDAEKQKQNIQLELHELKNLSEQQIKDKGQLVDEALQSRTKIEE------- 2286
Cdd:TIGR02168 360 LEELEAELEELESRLEeleEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkelq 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2287 -EIYLIRIQLETTVKQKSTAESELKQLRERAAEAERLRKVA-----------------QEEAEKLHKQVIEETQKK---- 2344
Cdd:TIGR02168 440 aELEELEEELEELQEELERLEEALEELREELEEAEQALDAAerelaqlqarldslerlQENLEGFSEGVKALLKNQsgls 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2345 ----RIAEK-ELQHKSEAEKEAA----------KQKQKALDDLENLKK-----------------QAEEAERQVKQAE-- 2390
Cdd:TIGR02168 520 gilgVLSELiSVDEGYEAAIEAAlggrlqavvvENLNAAKKAIAFLKQnelgrvtflpldsikgtEIQGNDREILKNIeg 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2391 --------VEKERQIKVA--------HVAAQKSAAAELQSK---HSSFVEKTSKL--------EESLKQEHGaVLQLQQE 2443
Cdd:TIGR02168 600 flgvakdlVKFDPKLRKAlsyllggvLVVDDLDNALELAKKlrpGYRIVTLDGDLvrpggvitGGSAKTNSS-ILERRRE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2444 AAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDM 2523
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2524 AEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEV----IAAQQQRKQLEDELAKVRSEMD 2599
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllnEEAANLRERLESLERRIAATER 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2600 ILIQLKSKAEK--ETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAIS 2677
Cdd:TIGR02168 839 RLEDLEEQIEElsEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678729579 2678 EATHLKTEAEIALKEKEAE----NERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKS 2735
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
987-1086 |
9.16e-22 |
|
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: 93.40 E-value: 9.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 987 AKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDPE 1066
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1678729579 1067 D-VDVQHPDEKSIITYVSSLY 1086
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2656-3297 |
1.41e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.25 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2656 EEAA------RQRAEAERilkeKLAAISEatHLkTEAEIALKEKEAENERLRRAAEdeayqrKALEdeANQHKKEIEEKI 2729
Cdd:COG1196 162 EEAAgiskykERKEEAER----KLEATEE--NL-ERLEDILGELERQLEPLERQAE------KAER--YRELKEELKELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2730 VQLKKSSDAEMERQKAMVDDTLKQRrvvEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKl 2809
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEEL---EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2810 aleeekrrreaeekvKKITAAEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQS 2889
Cdd:COG1196 303 ---------------DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2890 VLAQQKEDSImhkklkqeyekakklakeaeaakekaereaallRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEF 2969
Cdd:COG1196 368 LEAEAELAEA---------------------------------EEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2970 EAAKRAQAEGAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDA----- 3044
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAaarll 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3045 VKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLLKKDK-----------DNSQKFLAEEAENMKRLAEDAAR------ 3107
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAayeaaleaalaAALQNIVVEDDEVAAAAIEYLKAakagra 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3108 -------LSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQ----ESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQ 3176
Cdd:COG1196 575 tflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGdtllGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3177 LMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVV 3256
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1678729579 3257 EKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNK 3297
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2655-3440 |
3.46e-21 |
|
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: 103.13 E-value: 3.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2655 EEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEieekivqLKK 2734
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEY-------YQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2735 SSDAEMERQKAMVDDTLK---QRRVVEEEIRILKLNFEKASSGKLDLELELNK--LKNIAEETQQSKLRAEEEAEKLRKL 2809
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKlneERIDLLQELLRDEQEEIESSKQEIEKEEEKLAqvLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2810 ALEEEKRRREAEEKVKKITAAEEEAARQRKiAQDELERLKKKAEEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQS 2889
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKK-AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2890 VLAQQKEDSimhKKLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEF 2969
Cdd:pfam02463 375 LLAKKKLES---ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2970 EAAKRaqaegAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLldDELQRLKDEVDDAVKQRG 3049
Cdd:pfam02463 452 ELEKQ-----ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKAR--SGLKVLLALIKDGVGGRI 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3050 QVEEELFKVKVQMEELLKLKLRIEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQ 3129
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3130 RALADKMLKEKMQAI--QESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEA 3207
Cdd:pfam02463 605 LAQLDKATLEADEDDkrAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3208 EKLKLQVSQLSEAQTKAEEEAKKFKKQADKiaARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARL 3287
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKK--LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEK 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3288 KKEAEELQNKSKEMADAQQKQIEHEKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQQME 3367
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 3368 EEKKKLHATMHEALS-KQKEAEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQLEEAQKEQHTVPDKE 3440
Cdd:pfam02463 843 KEEQKLEKLAEEELErLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKE 916
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
986-1086 |
5.19e-21 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 91.25 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDP 1065
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1678729579 1066 EDVDV--QHPDEKSIITYVSSLY 1086
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
1620-1686 |
1.76e-20 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 88.09 E-value: 1.76e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678729579 1620 QLKPRNptTSIKGKLPVQAVCDFKQQEITVHKGDECALLNNSQPFNWKVLNRFGNEAVVPSVCFMVP 1686
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
866-974 |
2.12e-19 |
|
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: 87.44 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 866 RVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHKLQNVQIALDFLRHRQV 942
Cdd:cd21309 16 KIQQNTFTRWCNEHL---KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESI 92
|
90 100 110
....*....|....*....|....*....|..
gi 1678729579 943 KLVNIRNDDIADGNPKLTLGLIWTVILHFQIS 974
Cdd:cd21309 93 KLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
866-974 |
4.00e-19 |
|
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: 86.68 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 866 RVQKKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHKLQNVQIALDFLRHRQV 942
Cdd:cd21308 19 KIQQNTFTRWCNEHL---KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESI 95
|
90 100 110
....*....|....*....|....*....|..
gi 1678729579 943 KLVNIRNDDIADGNPKLTLGLIWTVILHFQIS 974
Cdd:cd21308 96 KLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2309-2861 |
5.46e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 95.88 E-value: 5.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2309 LKQLRERAAEA----ERLRKVAQEEAEKLHKQvieetqkkrIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAER 2384
Cdd:PRK02224 164 LEEYRERASDArlgvERVLSDQRGSLDQLKAQ---------IEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2385 QVKQA-EVEKERQIKVAHVAAQKSAAAELQSKhssfVEKTSKLEESLKQEhgaVLQLQQEAAHLKKQQEDAInareeAEK 2463
Cdd:PRK02224 235 TRDEAdEVLEEHEERREELETLEAEIEDLRET----IAETEREREELAEE---VRDLRERLEELEEERDDLL-----AEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2464 ELEKWRQKANEALRLRLQAEEEAHKKSLAQE--DAEKQKEEAEREAKKRAKAEESALKQKDMA---EKELERQRKVADST 2538
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECrvAAQAHNEEAESLREDADDLEERAEELREEAaelESELEEAREAVEDR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2539 AQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRsemdiliqlkskaeketmSNTEK 2618
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR------------------ERVEE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2619 SKQLLEA----------EATKMRDVAEEA----GKLRAIAEEAKHQRQVAEE--EAARQRAEAERILKEKLAAISEATHL 2682
Cdd:PRK02224 445 AEALLEAgkcpecgqpvEGSPHVETIEEDrervEELEAELEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDLEEL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2683 KTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLkkssdAEMERQKAMVDDTLKQRRVVEEEir 2762
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV-----AELNSKLAELKERIESLERIRTL-- 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2763 ilklnFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLAleeekrrreaeekvKKITAAEEEAARQRKI-A 2841
Cdd:PRK02224 598 -----LAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELE--------------AEFDEARIEEAREDKErA 658
|
570 580
....*....|....*....|
gi 1678729579 2842 QDELERLKKKAEEARKQKDE 2861
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDD 678
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2159-3245 |
7.78e-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: 95.63 E-value: 7.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2159 ELMTLTSQYIKFITETQRRLEDEEKA-AKKLKAEEQ--KKMAEMQAELDKQKQlaaahakaiaKAEKEAQELKLMMKEEV 2235
Cdd:pfam01576 19 ERQQKAESELKELEKKHQQLCEEKNAlQEQLQAETElcAEAEEMRARLAARKQ----------ELEEILHELESRLEEEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2236 NRREIAAVDAEKQKQNIQLELHELKnlSEQQIKDKGQLVDEALQSRTK-IEEEIYLIRIQLETTVKQKSTAESELKQLRE 2314
Cdd:pfam01576 89 ERSQQLQNEKKKMQQHIQDLEEQLD--EEEAARQKLQLEKVTTEAKIKkLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2315 RAAEAERLRKVAQEEAEKlHKQVIEETQKKRiaEKELQHKSEAEKEAAKQKQKALDDLENLKK-QAEEAERQVKQAEVEK 2393
Cdd:pfam01576 167 NLAEEEEKAKSLSKLKNK-HEAMISDLEERL--KKEEKGRQELEKAKRKLEGESTDLQEQIAElQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2394 ERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQ-------LQQEAAHLKKQQEDAINArEEAEKELE 2466
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKaekqrrdLGEELEALKTELEDTLDT-TAAQQELR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2467 KWRQKANEALRLRLQAEEEAHKKSLAQ---------EDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADS 2537
Cdd:pfam01576 323 SKREQEVTELKKALEEETRSHEAQLQEmrqkhtqalEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2538 TAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDiliQLKSKAEKETMSNTE 2617
Cdd:pfam01576 403 SEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS---SLESQLQDTQELLQE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2618 KSKQLLeAEATKMRDVAEEAGKLraiaeeakhQRQVAEEEAARQRAEaerilkeklaaiseaTHLKTeAEIALKEkeaen 2697
Cdd:pfam01576 480 ETRQKL-NLSTRLRQLEDERNSL---------QEQLEEEEEAKRNVE---------------RQLST-LQAQLSD----- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2698 erLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDA--EMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSgK 2775
Cdd:pfam01576 529 --MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAydKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQK-K 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2776 LDLELElnKLKNIAEETQQSKLRAEEEAEKLRKLALeeekrrrEAEEKVKKITAAEEEAARQRKI----------AQD-- 2843
Cdd:pfam01576 606 FDQMLA--EEKAISARYAEERDRAEAEAREKETRAL-------SLARALEEALEAKEELERTNKQlraemedlvsSKDdv 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2844 -----ELERLKKKAEEARKQKDEADVEAEVQIVAAQQAALKCstaEHQVQSVLAQQKEDSIMHKKLKQEyekakklakea 2918
Cdd:pfam01576 677 gknvhELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRL---EVNMQALKAQFERDLQARDEQGEE----------- 742
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2919 eaakekaeREAALLRQQAE-EAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQAEgaALKQKQQADAEMAKHKK 2997
Cdd:pfam01576 743 --------KRRQLVKQVRElEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREE--AVKQLKKLQAQMKDLQR 812
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2998 LAEQTlkqKFQVEQELTKVKlkldDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQ 3077
Cdd:pfam01576 813 ELEEA---RASRDEILAQSK----ESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKR 885
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3078 RL------LKKDKDNSQKFLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDLiQQRALADKMLKEKMQAIQES--SR 3149
Cdd:pfam01576 886 RLeariaqLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESAR-QQLERQNKELKAKLQEMEGTvkSK 964
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3150 LKA-----EAEMLQRQKDLAQEQAQKLLEDKQLmqRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKA 3224
Cdd:pfam01576 965 FKSsiaalEAKIAQLEEQLEQESRERQAANKLV--RRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1130 1140
....*....|....*....|.
gi 1678729579 3225 EEEAKKFKKQADKIAARLHET 3245
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDA 1063
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2153-3083 |
1.97e-18 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 94.34 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2153 LRTRYSELMTLTS-----QYIKFITETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQEL 2227
Cdd:TIGR00606 171 LKQKFDEIFSATRyikalETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2228 KLMMKE-EVNRREIAAVDAEkqkqniqleLHELKNLSEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAE 2306
Cdd:TIGR00606 251 KNRLKEiEHNLSKIMKLDNE---------IKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKEREL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2307 SELKQLRERAAEAERLrkVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEkeaAKQKQKALDDLEnlkkQAEEAERQV 2386
Cdd:TIGR00606 322 VDCQRELEKLNKERRL--LNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQ---SLATRLELDGFE----RGPFSERQI 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2387 KQA-EVEKERQIKVAHVAAQKsaAAELQSKHSSFVEKTSKLEESLKqehGAVLQLQQEAAHLKKQQEDAINAREEAE--- 2462
Cdd:TIGR00606 393 KNFhTLVIERQEDEAKTAAQL--CADLQSKERLKQEQADEIRDEKK---GLGRTIELKKEILEKKQEELKFVIKELQqle 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2463 ---KELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEEsalkqkdMAEKELERQ-RKVADST 2538
Cdd:TIGR00606 468 gssDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQE-------MEQLNHHTTtRTQMEML 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2539 AQQKLTAEQ-----------ELIRLRADFDNAEQqrslLEDELYRLKNEViaaqqqrKQLEDELAKVRSEMDILIQLKSK 2607
Cdd:TIGR00606 541 TKDKMDKDEqirkiksrhsdELTSLLGYFPNKKQ----LEDWLHSKSKEI-------NQTRDRLAKLNKELASLEQNKNH 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2608 AEKETMSNTEKSKQLLEA--EATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATH-LKT 2684
Cdd:TIGR00606 610 INNELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvFQT 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2685 EAEIALKEKEAENerLRRAAEDEayqRKALEDEANQHKKEIEEKIVqLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRIL 2764
Cdd:TIGR00606 690 EAELQEFISDLQS--KLRLAPDK---LKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2765 KLNFEKASS--GKLDLELELNK--------LKNIAEETQQSKLRAEEEAEKLRKLALEEE-----KRRREAEEKVKKITA 2829
Cdd:TIGR00606 764 KNDIEEQETllGTIMPEEESAKvcltdvtiMERFQMELKDVERKIAQQAAKLQGSDLDRTvqqvnQEKQEKQHELDTVVS 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2830 AEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKEDSIMHKKLKQEye 2909
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKD-- 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2910 kakklakeaeaakekaereaallrqQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQAEGAALKQKQQAD 2989
Cdd:TIGR00606 922 -------------------------QQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKE 976
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2990 AEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEvdDAVKqrgQVEEELFKVKVQMEELLKLK 3069
Cdd:TIGR00606 977 TELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRE--NELK---EVEEELKQHLKEMGQMQVLQ 1051
|
970
....*....|....*...
gi 1678729579 3070 LRIE----DENQRLLKKD 3083
Cdd:TIGR00606 1052 MKQEhqklEENIDLIKRN 1069
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2282-3404 |
2.39e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 93.70 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2282 TKIEEEIYLIRIQLETTVKQKSTAESELKQLRERAAEAERLRKVAQE----------EAEKLHKQVIEETQKKRIAEKEL 2351
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEqlqaetelcaEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2352 QHKSEAEKEAAKQ----KQKALDDLENLKKQ--AEEAERQVKQAE-VEKERQIKV--AHVAAQKSAAAELQSKHSSFVEK 2422
Cdd:pfam01576 81 ESRLEEEEERSQQlqneKKKMQQHIQDLEEQldEEEAARQKLQLEkVTTEAKIKKleEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2423 TSKLEESLKQEHGAVLQLQQeaahLKKQQEDAINAREEAEKELEKWRQKAnEALRLRLQAEeeahKKSLAQEDAEKQKEE 2502
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSK----LKNKHEAMISDLEERLKKEEKGRQEL-EKAKRKLEGE----STDLQEQIAELQAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2503 AEREAKKRAKAEESALKQKDMAEKELER---QRKVADSTAQQkLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEV-- 2577
Cdd:pfam01576 232 AELRAQLAKKEEELQAALARLEEETAQKnnaLKKIRELEAQI-SELQEDLESERAARNKAEKQRRDLGEELEALKTELed 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2578 ----IAAQQQ------------RKQLEDELAKVRSEMDILIQLKSKA----------EKETMSNTEKSKQLLEAEATkmr 2631
Cdd:pfam01576 311 tldtTAAQQElrskreqevtelKKALEEETRSHEAQLQEMRQKHTQAleelteqleqAKRNKANLEKAKQALESENA--- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2632 DVAEEAGKLRAIAEEAKHQRQVAE----------EEAARQRAEAERILKEKLAAISEATHLKTEAEIAL----KEKEAEN 2697
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEgqlqelqarlSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNiklsKDVSSLE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2698 ERLRRAAE---DEAYQR-------KALEDEANQHKKEIEEKiVQLKKSSDAEMERQKAMVDDTLKQrrvVEEEirilKLN 2767
Cdd:pfam01576 468 SQLQDTQEllqEETRQKlnlstrlRQLEDERNSLQEQLEEE-EEAKRNVERQLSTLQAQLSDMKKK---LEED----AGT 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2768 FEKASSGKLDLELELNKLKNIAEEtqqsKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEaaRQRKIAQDELEr 2847
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEE----KAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEK--KQKKFDQMLAE- 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2848 lkKKAEEARKQKDEADVEAEvqivaAQQAALKCSTAEHQVQSVLAQQKEDSIMHKKLKQEYEKAKKLAKEAEAAKEKAER 2927
Cdd:pfam01576 613 --EKAISARYAEERDRAEAE-----AREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELER 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2928 EAALLRQQAEEAERQkaaaEQEAAIQAKAQEDAeRLRKEAEFEAAKraqaegAALKQKQQADAEMAKHKKlaEQTLKQKF 3007
Cdd:pfam01576 686 SKRALEQQVEEMKTQ----LEELEDELQATEDA-KLRLEVNMQALK------AQFERDLQARDEQGEEKR--RQLVKQVR 752
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3008 QVEQEltkvklkLDDTDKQKSL-------LDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELlklklriedenQRLL 3080
Cdd:pfam01576 753 ELEAE-------LEDERKQRAQavaakkkLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL-----------QREL 814
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3081 KKDKDNSQKFLAEEAENMKRLAedaarlSVEsqeaARLRQIAEDDLIQQRAladkmlkeKMQAIQESSRLKAEAEMLQRQ 3160
Cdd:pfam01576 815 EEARASRDEILAQSKESEKKLK------NLE----AELLQLQEDLAASERA--------RRQAQQERDELADEIASGASG 876
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3161 KDLAQEQAQKLleDKQLMQrrLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAA 3240
Cdd:pfam01576 877 KSALQDEKRRL--EARIAQ--LEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKA 952
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3241 RLHETEIATKEKmtvvekleferlntskeagdLRDAIADLEkdkARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQQTF 3320
Cdd:pfam01576 953 KLQEMEGTVKSK--------------------FKSSIAALE---AKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLL 1009
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3321 LTEREmllkkeklieeekKKLESQFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMLSKQKEMQE 3400
Cdd:pfam01576 1010 QVEDE-------------RRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVST 1076
|
....
gi 1678729579 3401 LEKK 3404
Cdd:pfam01576 1077 LKSK 1080
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
986-1085 |
2.69e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 83.30 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERdLGVTRLLDP 1065
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1678729579 1066 EDVDVQH-PDEKSIITYVSSL 1085
Cdd:cd21255 80 ADMVLLPiPDKLIVMTYLCQL 100
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
990-1088 |
2.97e-18 |
|
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: 83.55 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 990 KLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLD-PEDV 1068
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1678729579 1069 DVQHPDEKSIITYVSSLYDV 1088
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYEL 107
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
986-1084 |
2.98e-18 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 83.05 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYqniRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVY-RQSNLENLEQAFNVAERDLGVTRLLD 1064
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1678729579 1065 PEDVDVQHPDEKSIITYVSS 1084
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
989-1085 |
3.13e-18 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 82.75 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 989 EKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKV----YRQSNLENLEQAFNVAERDLGVTRLLD 1064
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVaaslSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1678729579 1065 PEDVDVQHPDEKSIITYVSSL 1085
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
868-971 |
3.37e-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: 83.01 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 868 QKKTFTKWVNKHLiKRAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGR--MRFHKLQNVQIALDFLRHRQVKLV 945
Cdd:cd21212 1 EIEIYTDWANHYL-EKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQ 79
|
90 100
....*....|....*....|....*.
gi 1678729579 946 NIRNDDIADGNPKLTLGLIWTVILHF 971
Cdd:cd21212 80 GITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2187-2875 |
4.30e-18 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 93.11 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2187 KLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELKLMMKEEVNRREIAAVDAEKQKQNIQLELHELKNLSEQQ 2266
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2267 IKDKGQLV--DEALQSRTKIEEEIYLIRIQLEttvkqksTAESELKQLRERAAEAERLRKVAQEEAEKlhKQVIEETQKK 2344
Cdd:TIGR00618 239 QQSHAYLTqkREAQEEQLKKQQLLKQLRARIE-------ELRAQEAVLEETQERINRARKAAPLAAHI--KAVTQIEQQA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2345 RIAEKELQHKsEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKERQIKV-AHVAAQKSAAAELQSKHSSFVEKT 2423
Cdd:TIGR00618 310 QRIHTELQSK-MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVaTSIREISCQQHTLTQHIHTLQQQK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2424 SKLEESLKQEHGAVLQLQQEAAhlkkqQEDAINAREEAEKElEKWRQKANEALRLRLQAEEEAHKKSLAQEdaEKQKEEA 2503
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREQA-----TIDTRTSAFRDLQG-QLAHAKKQQELQQRYAELCAAAITCTAQC--EKLEKIH 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2504 EREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQkLTAEQELIRLRADFDNAEQQRSLLEDELYRLkneVIAAQQQ 2583
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIDNPGPLTRR---MQRGEQT 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2584 RKQLEDELAKVRSEMD-ILIQLKSKAEKEtmsntEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQvAEEEAARQR 2662
Cdd:TIGR00618 537 YAQLETSEEDVYHQLTsERKQRASLKEQM-----QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE-KLSEAEDML 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2663 AEAERILKEKL------------------AAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKE 2724
Cdd:TIGR00618 611 ACEQHALLRKLqpeqdlqdvrlhlqqcsqELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2725 IEEKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEeeirilklNFEKASSGKLDLELE-LNKLKNIAEETQQSKLRAEEEA 2803
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE--------NASSSLGSDLAAREDaLNQSLKELMHQARTVLKARTEA 762
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678729579 2804 EKLRKLALEEEKRRREaeekvkKITAAEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEAEVQIVAAQQ 2875
Cdd:TIGR00618 763 HFNNNEEVTAALQTGA------ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ 828
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
986-1086 |
7.66e-18 |
|
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: 82.35 E-value: 7.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDP 1065
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
|
90 100
....*....|....*....|..
gi 1678729579 1066 ED-VDVQHPDEKSIITYVSSLY 1086
Cdd:cd21259 81 EDmVRMREPDWKCVYTYIQEFY 102
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2380-3434 |
9.80e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 91.78 E-value: 9.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2380 EEAERQVKQAEVEK--ERQIKVAhvaaqkSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHL--KKQQEDAI 2455
Cdd:pfam01576 3 QEEEMQAKEEELQKvkERQQKAE------SELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLaaRKQELEEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2456 NAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAER---EAKKRaKAEESALKQKDMAEKeLERQR 2532
Cdd:pfam01576 77 LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvttEAKIK-KLEEDILLLEDQNSK-LSKER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2533 K-----VADSTAQqkLTAEQELIRLRADFDNaeQQRSLLEDELYRLKNEVIAAQQQRK---QLEDELAKVRSEMdilIQL 2604
Cdd:pfam01576 155 KlleerISEFTSN--LAEEEEKAKSLSKLKN--KHEAMISDLEERLKKEEKGRQELEKakrKLEGESTDLQEQI---AEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2605 KSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKH----QRQVAEEEAARQRAEAE-RILKEKLAAisea 2679
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQiselQEDLESERAARNKAEKQrRDLGEELEA---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2680 thLKTEAEIALKEKEAENErLRRAAEDEAYQ-RKALEDEANQHKKEIeekivqlkkssdAEMERQKAMVDDTLKQRRvve 2758
Cdd:pfam01576 304 --LKTELEDTLDTTAAQQE-LRSKREQEVTElKKALEEETRSHEAQL------------QEMRQKHTQALEELTEQL--- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2759 EEIRILKLNFEKAssgKLDLELELNKLKNIAEETQQSKLRAEEEAEKLrklaleeekrrreaEEKVKKITAAEEEAARQR 2838
Cdd:pfam01576 366 EQAKRNKANLEKA---KQALESENAELQAELRTLQQAKQDSEHKRKKL--------------EGQLQELQARLSESERQR 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2839 KIAQDELERLKKKAEEARKQKDEADVEAevqivaaQQAALKCSTAEHQVQSVLAQQKEDSimHKKLKqeyekakklakEA 2918
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGKN-------IKLSKDVSSLESQLQDTQELLQEET--RQKLN-----------LS 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2919 EAAKEKAEREAALLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEF-----EAAKRAQAEGAALKQKQQADAEMA 2993
Cdd:pfam01576 489 TRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTlealeEGKKRLQRELEALTQQLEEKAAAY 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2994 khkklaEQTLKQKFQVEQELTKVKLKLDDT--------DKQK---SLLDDE---LQRLKDEVDDAVKQRGQVEEELFKVK 3059
Cdd:pfam01576 569 ------DKLEKTKNRLQQELDDLLVDLDHQrqlvsnleKKQKkfdQMLAEEkaiSARYAEERDRAEAEAREKETRALSLA 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3060 VQMEELLKLKLRIEDENQRL------LKKDKDNSQKFlAEEAENMKRLAE-DAARLSVESQEAARLRQIAEDdliqqral 3132
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLraemedLVSSKDDVGKN-VHELERSKRALEqQVEEMKTQLEELEDELQATED-------- 713
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3133 ADKMLKEKMQAiqessrLKAEAEM-LQRQKDLAQEQAQKLLedKQLMQRRLEEETEEYQKSLEAERRRQLEIvaEAEKLK 3211
Cdd:pfam01576 714 AKLRLEVNMQA------LKAQFERdLQARDEQGEEKRRQLV--KQVRELEAELEDERKQRAQAVAAKKKLEL--DLKELE 783
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3212 LQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEA 3291
Cdd:pfam01576 784 AQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQER 863
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3292 EELQNKSKEMADAQQKQIEHEKTLLQQTFLTEREMllkkeklieeekkklesqfEEEAKKSKALKDEQERQKQQMEEEKK 3371
Cdd:pfam01576 864 DELADEIASGASGKSALQDEKRRLEARIAQLEEEL-------------------EEEQSNTELLNDRLRKSTLQVEQLTT 924
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 3372 KLHAtmHEALSKQKEAEKEMLSKQkemqelekkrleqeiiladeNQKLREKLQQLEEAQKEQH 3434
Cdd:pfam01576 925 ELAA--ERSTSQKSESARQQLERQ--------------------NKELKAKLQEMEGTVKSKF 965
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2232-3156 |
1.23e-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: 91.67 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2232 KEEVNRREIAAVdaEKQKQNIQLELHELKNLSEQQIKDKGQLVD-EALQSRtKIEEEIYLIRIQLETTVKQKSTAESELK 2310
Cdd:TIGR02169 171 KKEKALEELEEV--EENIERLDLIIDEKRQQLERLRREREKAERyQALLKE-KREYEGYELLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2311 QLRERAAEAerlrkvaQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALD-DLENLKKQAEEAERQVKQA 2389
Cdd:TIGR02169 248 SLEEELEKL-------TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2390 EVEKerqikvahvaaqksaaAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWR 2469
Cdd:TIGR02169 321 EERL----------------AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2470 QKANEALRL--RLQAEEEAHKKSLAQEDAEKQKEEAEREakkRAKAEESALKQKdmaEKELERQRKVADSTAQQkltAEQ 2547
Cdd:TIGR02169 385 DELKDYREKleKLKREINELKRELDRLQEELQRLSEELA---DLNAAIAGIEAK---INELEEEKEDKALEIKK---QEW 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2548 ELIRLRADFDNAEQqrslledELYRLKNEViaaqqqrKQLEDELAKVRSEMDILiqlkskaeketmsntEKSKQLLEAEA 2627
Cdd:TIGR02169 456 KLEQLAADLSKYEQ-------ELYDLKEEY-------DRVEKELSKLQRELAEA---------------EAQARASEERV 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2628 TKMRDVAEEAGKLR-----AIAE--EAKHQRQVAEEEAARQR------------AEAERILKEKlaAISEATHL---KTE 2685
Cdd:TIGR02169 507 RGGRAVEEVLKASIqgvhgTVAQlgSVGERYATAIEVAAGNRlnnvvveddavaKEAIELLKRR--KAGRATFLplnKMR 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2686 AEIALKEKEAENERLRRAAEDEAYQRK-------------ALEDEANQHKKEIEEKIVQLkkssDAEM-ERQKAMVDDTL 2751
Cdd:TIGR02169 585 DERRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdtlVVEDIEAARRLMGKYRMVTL----EGELfEKSGAMTGGSR 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2752 KQRRV----VEEEIRILKLNFEKassGKLDLEL-----ELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRReaee 2822
Cdd:TIGR02169 661 APRGGilfsRSEPAELQRLRERL---EGLKRELsslqsELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE---- 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2823 kvkkiTAAEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKEDSIMHK 2902
Cdd:TIGR02169 734 -----KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVS 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2903 KlkqeyekakklakeaeaakekaereaalLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQAEGAAL 2982
Cdd:TIGR02169 809 R----------------------------IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN 860
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2983 KQKQQADAEMAKHKklaeqtlKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQM 3062
Cdd:TIGR02169 861 GKKEELEEELEELE-------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3063 EELLKLKLRIEDENQRLLkkDKDNSQKFLAEEAENMKRLaEDAARLSVESQEAARLRQiaeDDLIQQRALADKMLKEKMQ 3142
Cdd:TIGR02169 934 SEIEDPKGEDEEIPEEEL--SLEDVQAELQRVEEEIRAL-EPVNMLAIQEYEEVLKRL---DELKEKRAKLEEERKAILE 1007
|
970
....*....|....
gi 1678729579 3143 AIQESSRLKAEAEM 3156
Cdd:TIGR02169 1008 RIEEYEKKKREVFM 1021
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
869-969 |
1.74e-17 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 80.85 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 869 KKTFTKWVNKHLIKRaeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPRE--KGRMRFHKLQNVQIALDFLRHRQV-KLV 945
Cdd:cd00014 1 EEELLKWINEVLGEE--LPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELD 78
|
90 100
....*....|....*....|....*
gi 1678729579 946 NIRNDDI-ADGNPKLTLGLIWTVIL 969
Cdd:cd00014 79 LFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2226-2898 |
2.27e-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: 90.90 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2226 ELKLMMKE-EVNRREIAAVDAE------------KQKQNIQLELHELKNLSEQ---QIKDKGQlvDEALQSRTKIEEeiy 2289
Cdd:TIGR02169 224 EGYELLKEkEALERQKEAIERQlasleeelekltEEISELEKRLEEIEQLLEElnkKIKDLGE--EEQLRVKEKIGE--- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2290 lIRIQLETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQvIEETQKKRIAEKELQHKSEAEKEAAKQKqkal 2369
Cdd:TIGR02169 299 -LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE-IEEERKRRDKLTEEYAELKEELEDLRAE---- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2370 ddLENLKKQAEEAERQVKQAEVEKErqikvahvaaqksaaaELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKK 2449
Cdd:TIGR02169 373 --LEEVDKEFAETRDELKDYREKLE----------------KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2450 QQEDAINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKkRAKAEESALKQkdmAEKELE 2529
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA-EAEAQARASEE---RVRGGR 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2530 RQRKVADSTAQQKLTAEQELIRLRADFDNAeqqrslLEDEL-YRLKNEVIA----AQQQRKQLEDE---------LAKVR 2595
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATA------IEVAAgNRLNNVVVEddavAKEAIELLKRRkagratflpLNKMR 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2596 SE------------MDILIQLKSKAEK----------ET--MSNTEKSKQL--------LEAE------ATKMRDVAEEA 2637
Cdd:TIGR02169 585 DErrdlsilsedgvIGFAVDLVEFDPKyepafkyvfgDTlvVEDIEAARRLmgkyrmvtLEGElfeksgAMTGGSRAPRG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2638 GKLRAIAEEAKHQRQVAEEEA--------ARQRAEAERILKEKLAAISEATH----LKTEAEIALKEKEAENERLRRAAE 2705
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGlkrelsslQSELRRIENRLDELSQELSDASRkigeIEKEIEQLEQEEEKLKERLEELEE 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2706 DEAYQRKALE------DEANQHKKEIEEKIVQLKKSSdAEMERQKAM--VDDTLKQRRVVEEEIRILKLNFEkassgklD 2777
Cdd:TIGR02169 745 DLSSLEQEIEnvkselKELEARIEELEEDLHKLEEAL-NDLEARLSHsrIPEIQAELSKLEEEVSRIEARLR-------E 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2778 LELELNKL---KNIAEETQQSKLRAEEEAEKLRKlalEEEKRRREAEEKVKKITAAEEEAARQRKIAQDELERLKKKAEE 2854
Cdd:TIGR02169 817 IEQKLNRLtleKEYLEKEIQELQEQRIDLKEQIK---SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 2855 ARKQKDEA-----DVEAEVQIVAAQQAALKC--STAEHQVQSVLAQQKEDS 2898
Cdd:TIGR02169 894 LEAQLRELerkieELEAQIEKKRKRLSELKAklEALEEELSEIEDPKGEDE 944
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2007-2810 |
2.39e-17 |
|
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: 90.41 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2007 ELDHYRQHLSGLQDRWKAVFAQMDIRQRELEQLGRQLGYYHESYdwlihwiTDAKERQEKIQAVSITDSKTLKE---QLS 2083
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTY-------HERKQVLEKELKHLREALQQTQQshaYLT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2084 QEKKLLEEIENNKDNVDECQKYAKAYINSIKDYELQLVAYNAQADPLASPLKKTKLDSASDNIIQEYVTLRTRYSELMTL 2163
Cdd:TIGR00618 247 QKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2164 TSQYIKFI-----TETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELKLMMKE-EVNR 2237
Cdd:TIGR00618 327 LMKRAAHVkqqssIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKElDILQ 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2238 REIAAVDAEKQKQNIQlelhelknlseqqikdKGQLVdealqsRTKIEEEiylirIQLETTVKQKSTAESELKQLRERAA 2317
Cdd:TIGR00618 407 REQATIDTRTSAFRDL----------------QGQLA------HAKKQQE-----LQQRYAELCAAAITCTAQCEKLEKI 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2318 EAERLRKVAQEEAEKL-HKQVI--EETQKKRIAEKELQHKSEAEKEAAKQ------KQKALDDLENLKKQAEEAERQVKQ 2388
Cdd:TIGR00618 460 HLQESAQSLKEREQQLqTKEQIhlQETRKKAVVLARLLELQEEPCPLCGScihpnpARQDIDNPGPLTRRMQRGEQTYAQ 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2389 aevekerqikvaHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKW 2468
Cdd:TIGR00618 540 ------------LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2469 RQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQE 2548
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQS 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2549 LIR-LRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKEtmsntekskqlleaea 2627
Cdd:TIGR00618 688 EKEqLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ---------------- 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2628 tkmrdvAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLkteaeiaLKEKEAENERLRRAAEDE 2707
Cdd:TIGR00618 752 ------ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL-------LKTLEAEIGQEIPSDEDI 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2708 ayqrKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSgkldleleLNKLKN 2787
Cdd:TIGR00618 819 ----LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG--------INQIKI 886
|
810 820
....*....|....*....|...
gi 1678729579 2788 IAEETQQSKLRAEEEAEKLRKLA 2810
Cdd:TIGR00618 887 QFDGDALIKFLHEITLYANVRLA 909
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1981-2808 |
4.00e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 90.03 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1981 DSLEEELKKATVVSDKMSRVHSERDVELdhyrQHLSGLQDRWKAVFAQMDIRQRELEQLGRQLGYYHESYDWLIHWITDA 2060
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENKEEE----KEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2061 KERQEKIQAVSITDSKTLKEQLSQEKKLLEEIENNkdnvdecqkyakayinsikdYELQLVAYNAQADPLASPLKKTKLD 2140
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEEL--------------------EKLQEKLEQLEEELLAKKKLESERL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2141 SASDNIIQEYvtlrtryselMTLTSQYIKFITETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKqlaaaHAKAIAKA 2220
Cdd:pfam02463 387 SSAAKLKEEE----------LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ-----GKLTEEKE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2221 EKEAQELKLMMKEEVnrreiaavdaEKQKQNIQLELHELKNLSEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVK 2300
Cdd:pfam02463 452 ELEKQELKLLKDELE----------LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2301 QKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQK-QKALDDLENLKKQA 2379
Cdd:pfam02463 522 GRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKlKLPLKSIAVLEIDP 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2380 EEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKL------EESLKQEHGAVLQLQQEAAHLKKQQED 2453
Cdd:pfam02463 602 ILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLrkgvslEEGLAEKSEVKASLSELTKELLEIQEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2454 AINAREEAEKELEKWRQKANEALRLRLQAEEEAHKkslaqEDAEKQKEEAEREAKKRAKAEESALKQK-DMAEKELERQR 2532
Cdd:pfam02463 682 QEKAESELAKEEILRRQLEIKKKEQREKEELKKLK-----LEAEELLADRVQEAQDKINEELKLLKQKiDEEEEEEEKSR 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2533 KVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELakvrsEMDILIQLKSKAEKEt 2612
Cdd:pfam02463 757 LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAE-----LLEEEQLLIEQEEKI- 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2613 mSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQrQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKE 2692
Cdd:pfam02463 831 -KEEELEELALELKEEQKLEKLAEEELERLEEEITKEE-LLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2693 KEAENERLRRAAEDEAYQRKALEDEANQHKKE-IEEKIVQLKKSSDAEMERQKAmvddTLKQRRVVEEEIRILKLNFEKA 2771
Cdd:pfam02463 909 LNLLEEKENEIEERIKEEAEILLKYEEEPEELlLEEADEKEKEENNKEEEEERN----KRLLLAKEELGKVNLMAIEEFE 984
|
810 820 830
....*....|....*....|....*....|....*..
gi 1678729579 2772 SSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRK 2808
Cdd:pfam02463 985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
986-1087 |
4.23e-17 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 80.01 E-value: 4.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDP 1065
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80
|
90 100
....*....|....*....|....
gi 1678729579 1066 EDVDV--QHPDEKSIITYVSSLYD 1087
Cdd:cd21261 81 EDMMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
986-1094 |
5.61e-17 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 79.71 E-value: 5.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDP 1065
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80
|
90 100 110
....*....|....*....|....*....|.
gi 1678729579 1066 EDVDV--QHPDEKSIITYVSSLYDVMPRMDV 1094
Cdd:cd21258 81 EDMMImgKKPDSKCVFTYVQSLYNHLRRHEM 111
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2295-2907 |
1.01e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 88.49 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2295 LETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAA------KQKQKA 2368
Cdd:TIGR00618 172 LFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQqshaylTQKREA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2369 LDDLENLKKQAEEAERQVKQAEVEK----------ERQIKVAHVAAQKSAAAEL----QSKHSSFVEKTSKLEESLKQEH 2434
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEavleetqeriNRARKAAPLAAHIKAVTQIeqqaQRIHTELQSKMRSRAKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2435 GAVLQ---LQQEAAHLKKQQEDAINAREEAEKEL----EKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREA 2507
Cdd:TIGR00618 332 AHVKQqssIEEQRRLLQTLHSQEIHIRDAHEVATsireISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2508 KKRAKAEESALKQKDM-AEKELERQRKVAdstAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKN-EVIAAQQQRK 2585
Cdd:TIGR00618 412 IDTRTSAFRDLQGQLAhAKKQQELQQRYA---ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTkEQIHLQETRK 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2586 QLEDELAKVRsemdiLIQLKSKAEKETMSNTEKSKQLLEAEAT--KMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRA 2663
Cdd:TIGR00618 489 KAVVLARLLE-----LQEEPCPLCGSCIHPNPARQDIDNPGPLtrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2664 EAERILKEKLAAISEATHLKTEAEIALKEKeaenERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKS-------- 2735
Cdd:TIGR00618 564 QMQEIQQSFSILTQCDNRSKEDIPNLQNIT----VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRlhlqqcsq 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2736 SDAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIA---EETQQSKLRAEEEAEKLRKLALE 2812
Cdd:TIGR00618 640 ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTywkEMLAQCQTLLRELETHIEEYDRE 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2813 EEKRRREAEEKVKKItAAEEEAARQrkiAQDELERLKKkaeEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLA 2892
Cdd:TIGR00618 720 FNEIENASSSLGSDL-AAREDALNQ---SLKELMHQAR---TVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNR 792
|
650
....*....|....*
gi 1678729579 2893 QQKEDSIMHKKLKQE 2907
Cdd:TIGR00618 793 LREEDTHLLKTLEAE 807
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2233-2734 |
1.19e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 88.43 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2233 EEVNRREIAAVDAEKQKQniQLElhelknlseqQIKDKGQLVDEALQSRTKIEEEIYLIRIQlettvkqksTAESELKQL 2312
Cdd:COG4913 235 DDLERAHEALEDAREQIE--LLE----------PIRELAERYAAARERLAELEYLRAALRLW---------FAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2313 RERAAEAERLRKVAQEEAEKLhkqvieeTQKKRIAEKELQhksEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVE 2392
Cdd:COG4913 294 EAELEELRAELARLEAELERL-------EARLDALREELD---ELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2393 KERQIKVAHVAAQKSAA--AELQSKHSSFVEKTSKLEESLKQEHGAVL-----------QLQQEAAHLKKQQ----EDAI 2455
Cdd:COG4913 364 LEALLAALGLPLPASAEefAALRAEAAALLEALEEELEALEEALAEAEaalrdlrrelrELEAEIASLERRKsnipARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2456 NAREEAEKEL--------------------EKWRQKANEAL---RLRLQAEEEAHKKSLAQEDAEK-------QKEEAER 2505
Cdd:COG4913 444 ALRDALAEALgldeaelpfvgelievrpeeERWRGAIERVLggfALTLLVPPEHYAAALRWVNRLHlrgrlvyERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2506 EAKKRAKAEESALKQK---------DMAEKELERQRKVA--DSTAQQK-----LTAE------------QELIRLRAD-- 2555
Cdd:COG4913 524 PDPERPRLDPDSLAGKldfkphpfrAWLEAELGRRFDYVcvDSPEELRrhpraITRAgqvkgngtrhekDDRRRIRSRyv 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2556 --FDNAEqQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKE--------TMSNTEKSKQLLEA 2625
Cdd:COG4913 604 lgFDNRA-KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvasaerEIAELEAELERLDA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2626 EATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAAR---QRAEAERILKEKLAAISEATHLKTEAEIALKEkeaenERLRR 2702
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEELDELQDRLEAAEDLARLELRALLE-----ERFAA 757
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1678729579 2703 AAEDEAY---------QRKALEDEANQHKKEIEEKIVQLKK 2734
Cdd:COG4913 758 ALGDAVErelrenleeRIDALRARLNRAEEELERAMRAFNR 798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2239-2880 |
1.51e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.81 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2239 EIAAVDAEKQKQNIQLELHELKNL--SEQQIKDkgqLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLRERA 2316
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFikRTENIEE---LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2317 AEAERLRKvaqeEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQkaldDLENLKKQAEEAERQVkqaevekerq 2396
Cdd:PRK03918 238 EEIEELEK----ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK----ELKELKEKAEEYIKLS---------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2397 ikvahvaaqksaaaELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEAL 2476
Cdd:PRK03918 300 --------------EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2477 RLR-LQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEEsalkqkdmAEKELERQRKVADSTAQQKLTAEQELirLRAD 2555
Cdd:PRK03918 366 EAKaKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE--------EISKITARIGELKKEIKELKKAIEEL--KKAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2556 FDNAEQQRSLLEDELYRLKNEVIAaqqqrkqledELAKVRSEMDILIQLKSKAEKEtMSNTEKsKQLLEAEATKMRDVAE 2635
Cdd:PRK03918 436 GKCPVCGRELTEEHRKELLEEYTA----------ELKRIEKELKEIEEKERKLRKE-LRELEK-VLKKESELIKLKELAE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2636 EagkLRAIAEEAKhqrQVAEEEAARQRAEAERiLKEKLAAIS-EATHLKTEAEIA---LKEKEAENERLRRAAEDEAYQR 2711
Cdd:PRK03918 504 Q---LKELEEKLK---KYNLEELEKKAEEYEK-LKEKLIKLKgEIKSLKKELEKLeelKKKLAELEKKLDELEEELAELL 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2712 KALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMvddtlKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEE 2791
Cdd:PRK03918 577 KELEELGFESVEELEERLKELEPFYNEYLELKDAE-----KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2792 TQqsKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRKIAQDELERLKKKAEEARK-QKDEADVEAEVQI 2870
Cdd:PRK03918 652 LE--KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKlEKALERVEELREK 729
|
650
....*....|
gi 1678729579 2871 VAAQQAALKC 2880
Cdd:PRK03918 730 VKKYKALLKE 739
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2295-2793 |
1.76e-16 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 87.97 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2295 LETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEE--TQKKRIAEK--ELQHKSEAEKEAAKQKQKALD 2370
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLlrTLDDQWKEKrdELNGELSAADAAVAKDRSELE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2371 DLENLKKQAEEAERQVKQAEVEKERQIKvAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLqlqqeaAHLKKQ 2450
Cdd:pfam12128 326 ALEDQHGAFLDADIETAAADQEQLPSWQ-SELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDI------AGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2451 QEdaiNAREEAEKELEKWRQkANEALRLRLQAEEEAHKKSLaqEDAEKQKEEAEREAKKR---AKAEESALKQKDMAEKE 2527
Cdd:pfam12128 399 LA---KIREARDRQLAVAED-DLQALESELREQLEAGKLEF--NEEEYRLKSRLGELKLRlnqATATPELLLQLENFDER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2528 LERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQ------------RKQL---EDELA 2592
Cdd:pfam12128 473 IERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhflRKEApdwEQSIG 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2593 KVRSEmdiliQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEK 2672
Cdd:pfam12128 553 KVISP-----ELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2673 LAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMVDDTLK 2752
Cdd:pfam12128 628 VQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKE 707
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1678729579 2753 QRRvveeEIRILKLNFEKASSGKLDLELELNKLKNIAEETQ 2793
Cdd:pfam12128 708 QKR----EARTEKQAYWQVVEGALDAQLALLKAAIAARRSG 744
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
990-1088 |
2.79e-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: 77.61 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 990 KLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLD-PEDV 1068
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1678729579 1069 DVQHPDEKSIITYVSSLYDV 1088
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYEL 107
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
982-1089 |
3.70e-16 |
|
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: 77.30 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 982 SEDMSAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTR 1061
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*....
gi 1678729579 1062 LLDPEDV-DVQHPDEKSIITYVSSLYDVM 1089
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2633-3428 |
3.70e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 86.66 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2633 VAEEAGKLRAIAEEAKHQRQVAEEEaaRQRAEAERILKEKLAAIsEATHLKTEAEIALKEK---EAENERLRRAAEDEAY 2709
Cdd:TIGR02169 182 VEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREY-EGYELLKEKEALERQKeaiERQLASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2710 QRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIA 2789
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2790 EEtqqskLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRkiAQDELERLKKKAEEARKQKDEADVEAEVQ 2869
Cdd:TIGR02169 339 EE-----LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE--TRDELKDYREKLEKLKREINELKRELDRL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2870 IVAAQQAALKCSTAEHQVQSVLAQQKEdSIMHKKLKQEYEKAKKLAKEAeaakekaereaalLRQQAEEAERQKAAAEQE 2949
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIEAKINE-LEEEKEDKALEIKKQEWKLEQ-------------LAADLSKYEQELYDLKEE 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2950 AAIQAKAQEDAER--LRKEAEFEAAKRAQAEGAA---------------LKQKQQADAEMAKHKKLAEQTLKQKFQVEQE 3012
Cdd:TIGR02169 478 YDRVEKELSKLQRelAEAEAQARASEERVRGGRAveevlkasiqgvhgtVAQLGSVGERYATAIEVAAGNRLNNVVVEDD 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3013 LTKVK----LK---------LDDTDKQKSLLDDELQRLKDEVDDAV------KQRGQVEEELFKVKVQMEEL-----LKL 3068
Cdd:TIGR02169 558 AVAKEaielLKrrkagratfLPLNKMRDERRDLSILSEDGVIGFAVdlvefdPKYEPAFKYVFGDTLVVEDIeaarrLMG 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3069 KLRIEDENQRLLKKDKDNSQKFLAEE--AENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQE 3146
Cdd:TIGR02169 638 KYRMVTLEGELFEKSGAMTGGSRAPRggILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3147 SSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEyQKSLEAE-RRRQLEIVAEAEKL-KLQVSQLSEAQTKA 3224
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE-LKELEARiEELEEDLHKLEEALnDLEARLSHSRIPEI 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3225 EEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEmADA 3304
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE-LEA 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3305 QQKQIEHEKTLLQqtflteremllkkeklieeekkkleSQFEEEAKKSKALKDEQERQKQQMEEEKKKLhATMHEALSKQ 3384
Cdd:TIGR02169 876 ALRDLESRLGDLK-------------------------KERDELEAQLRELERKIEELEAQIEKKRKRL-SELKAKLEAL 929
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1678729579 3385 KEAEKEMLSKQKEMQELEKKRLEQEIILAdENQKLREKLQQLEE 3428
Cdd:TIGR02169 930 EEELSEIEDPKGEDEEIPEEELSLEDVQA-ELQRVEEEIRALEP 972
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
986-1085 |
3.92e-16 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 77.20 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERdLGVTRLLDP 1065
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1678729579 1066 ED-VDVQHPDEKSIITYVSSL 1085
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
986-1086 |
3.96e-16 |
|
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: 77.40 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAErDLGVTRLLDP 1065
Cdd:cd21199 8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTI 86
|
90 100
....*....|....*....|..
gi 1678729579 1066 ED-VDVQHPDEKSIITYVSSLY 1086
Cdd:cd21199 87 DEmVSMERPDWQSVMSYVTAIY 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2582-3421 |
5.60e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 86.28 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2582 QQRKQLEDELAKVrSEMDILIQlKSKAEKETMSNTEKSKQLLEAEA-------TKMRDVAEEAGKLRAIAEEAKHQRQVA 2654
Cdd:TIGR02169 153 VERRKIIDEIAGV-AEFDRKKE-KALEELEEVEENIERLDLIIDEKrqqlerlRREREKAERYQALLKEKREYEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2655 EEEAARqrAEAERILKEklaaISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKAL-EDEANQHKKEIEEKIVQLK 2733
Cdd:TIGR02169 231 EKEALE--RQKEAIERQ----LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2734 KSSDAEMERQKAMvDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEE 2813
Cdd:TIGR02169 305 SLERSIAEKEREL-EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2814 EKRRREAEEKVKKITAAEEEAARQRKIAQDELERLKKKAEEARKqkDEADVEAEVQIVAA--QQAALKCSTAEHQVQSVL 2891
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA--AIAGIEAKINELEEekEDKALEIKKQEWKLEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2892 AQQKEDSIMHKKLKQEYEKAKKLAKEaeaakekaereaalLRQQAEEAERQKAAAEQEAAIQAKAQED------------ 2959
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKELSK--------------LQRELAEAEAQARASEERVRGGRAVEEVlkasiqgvhgtv 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2960 AERLRKEAEFEAAKRAqAEGAALKQ---KQQADA----EMAKHKKLAEQT---LKQKFQVEQELTKVKLK--------LD 3021
Cdd:TIGR02169 528 AQLGSVGERYATAIEV-AAGNRLNNvvvEDDAVAkeaiELLKRRKAGRATflpLNKMRDERRDLSILSEDgvigfavdLV 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3022 DTDKQ-----KSLLDDELqrLKDEVDDAVKQRGQV-----EEELFK---------VKVQMEELLKLKLRIEDENQRLLKK 3082
Cdd:TIGR02169 607 EFDPKyepafKYVFGDTL--VVEDIEAARRLMGKYrmvtlEGELFEksgamtggsRAPRGGILFSRSEPAELQRLRERLE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3083 DKDNSQKFLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKA---------E 3153
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEnvkselkelE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3154 AEMLQRQKDLAQEQAQ-KLLEDKQLMQRrLEEETEEYQKsLEAERRRQLEIVAEAE----KLKLQVSQLSEAQTKAEEEA 3228
Cdd:TIGR02169 765 ARIEELEEDLHKLEEAlNDLEARLSHSR-IPEIQAELSK-LEEEVSRIEARLREIEqklnRLTLEKEYLEKEIQELQEQR 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3229 KKFKKQADKIAARLHETEIATKEKMTVVEKLEferlntsKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMADAQQKQ 3308
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEEELEELE-------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3309 IEHEKTLLQQTFLTEREMLLKKEKLIeeekkklesQFEEEAKKSKALKDEQErQKQQMEEEKKKLHATMHEALSKQKEAE 3388
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKG---------EDEEIPEEELSLEDVQA-ELQRVEEEIRALEPVNMLAIQEYEEVL 985
|
890 900 910
....*....|....*....|....*....|...
gi 1678729579 3389 KEMLSKQKEMQELEKKRLEQEIILADENQKLRE 3421
Cdd:TIGR02169 986 KRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1956-2735 |
8.73e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.49 E-value: 8.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1956 VKEVETYRTKLKKMRGEAEGEQPVFDSLEEELKKATVVSDKMSRVHSERDVELDHYRQHLSGLQDRWKAVFAQMDIRQRE 2035
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2036 LEQLGRQLGYYHESYDWLIHWITDAKERQEKIQAVSITDSKTLKEQLSQEKKLLEEIENNKDNVDECQKYAKAYINSIKD 2115
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2116 YELQLVAYNAQADPLASplKKTKLDSASDNIIQEYVTLRTRYSELMtltsqyikfITETQRRLEDEEKAAKKLKAEEqkk 2195
Cdd:TIGR02168 391 LELQIASLNNEIERLEA--RLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEEL--- 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2196 mAEMQAELDKQKQLAAAHAKAIAKAEKEAQELklmmkeevNRREIAAVDAEKQKQNIQLELHELKNlSEQQIKDKGQLVD 2275
Cdd:TIGR02168 457 -ERLEEALEELREELEEAEQALDAAERELAQL--------QARLDSLERLQENLEGFSEGVKALLK-NQSGLSGILGVLS 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2276 EALQSRTKIEE--EIYLIRIQLETTVKQKSTAESELKQLREraaeaERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQH 2353
Cdd:TIGR02168 527 ELISVDEGYEAaiEAALGGRLQAVVVENLNAAKKAIAFLKQ-----NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFL 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2354 KSEAE-KEAAKQKQKAL----------DDLEN---LKKQAEEAERQV--------------------KQAEVEKERQIK- 2398
Cdd:TIGR02168 602 GVAKDlVKFDPKLRKALsyllggvlvvDDLDNaleLAKKLRPGYRIVtldgdlvrpggvitggsaktNSSILERRREIEe 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2399 -VAHVAAQKSAAAELQSKHSsfvEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQkaNEALR 2477
Cdd:TIGR02168 682 lEEKIEELEEKIAELEKALA---ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ--LSKEL 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2478 LRLQAEEEAHKKSLAQEDAEKQKEEAEREA-KKRAKAEESALKQkdmAEKELERQRKVADSTAQQKLTAEQELIRLRADF 2556
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEElEAQIEQLKEELKA---LREALDELRAELTLLNEEAANLRERLESLERRI 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2557 DNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKskqlLEAEATKMRDVAEE 2636
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE----LEELSEELRELESK 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2637 AGKLRAIAEEAKHqrQVAEEEAARQRAEAERI-LKEKLAA---ISEATHLKTEAEIALKEKEAENE--RLRR-------- 2702
Cdd:TIGR02168 910 RSELRRELEELRE--KLAQLELRLEGLEVRIDnLQERLSEeysLTLEEAEALENKIEDDEEEARRRlkRLENkikelgpv 987
|
810 820 830
....*....|....*....|....*....|....*
gi 1678729579 2703 --AAEDEAYQRKALEDEANQHKKEIEEKIVQLKKS 2735
Cdd:TIGR02168 988 nlAAIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2076-2647 |
1.15e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 84.73 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2076 KTLKEQLSQEKKLL---EEIENNKDNVDECQKYAKAYINSIKDYELQLVAYNAQADPLASPLKKTKLDSASDNIiqEYVT 2152
Cdd:PRK03918 172 KEIKRRIERLEKFIkrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEK--ELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2153 LRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKKLKA--EEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELKLM 2230
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2231 MKEeVNRREIAAVDAEKQKQNIQLELHELKNlSEQQIKDKGQLVDEALQSRTKIE-EEIYLIRIQLETTVKQKSTAESEL 2309
Cdd:PRK03918 330 IKE-LEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2310 KQLRERAAEAERLRKVAQEEAEKLHK---------QVIEETQKKRIAEK---ELQHKSEAEKEAAKQKQKALDDLENLKK 2377
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKakgkcpvcgRELTEEHRKELLEEytaELKRIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2378 QAEEAERQVKQAEVEKerQIKVAHVAAQKSAAAELQSKHSSF---VEKTSKLE---ESLKQEHGAVLQLQQEAAHLKKQQ 2451
Cdd:PRK03918 488 VLKKESELIKLKELAE--QLKELEEKLKKYNLEELEKKAEEYeklKEKLIKLKgeiKSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2452 EDAINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQ 2531
Cdd:PRK03918 566 DELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2532 RKvadstaqqkltaeqELIRLRADFDNAEQQRslLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILiqlksKAEKE 2611
Cdd:PRK03918 646 RK--------------ELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-----KEELE 704
|
570 580 590
....*....|....*....|....*....|....*.
gi 1678729579 2612 TMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEA 2647
Cdd:PRK03918 705 EREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
865-966 |
1.29e-15 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 76.03 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 865 DRVQKKTFTKWVNKHLIKRAESQhhVTDLYEDLRDGHNLISLLEVLSGDTLPRE---KGRMRFHKLQNVQIALDFLRHR- 940
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGIPK--ISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDl 79
|
90 100
....*....|....*....|....*.
gi 1678729579 941 QVKLVNIRNDDIADGNPKLTLGLIWT 966
Cdd:cd21225 80 KIRVQGIGAEDFVDNNKKLILGLLWT 105
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2232-2687 |
1.54e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 84.05 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2232 KEEVNRREIAAvdAEKQKQNIQLELHELKNLsEQQIKDKGQLVDEALQSRTKIEEEIYLIR--IQLETTVKQKSTAESEL 2309
Cdd:COG4717 65 KPELNLKELKE--LEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2310 KQLRERA----------AEAERLRKVAQEEAEKLHKQVIEETQKKRIA-EKELQHKSEAEKEAAKQKQKALDDLENLKKQ 2378
Cdd:COG4717 142 AELPERLeeleerleelRELEEELEELEAELAELQEELEELLEQLSLAtEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2379 AEEAERQVKQAEVEKERQIKVAHVAAQK------SAAAELQSKHSSFVEKTSKLEESLKQEHGAVL-----QLQQEAAHL 2447
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLAllfllLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2448 KKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQE--DAEKQKEEAEREAK-KRAKAEESALKQKDMA 2524
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEElqELLREAEELEEELQlEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2525 EKELERQRKVADSTAQQKLTAEQELI--RLRADFDNAEQQ-----RSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSE 2597
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELeeQLEELLGELEELlealdEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2598 MDiliQLKSKAEKETMsnteksKQLLEAEATKMRDVAEEAGKLRAIAEE-AKHQRQVAEEEAARQRAEAERILKE----- 2671
Cdd:COG4717 462 LE---QLEEDGELAEL------LQELEELKAELRELAEEWAALKLALELlEEAREEYREERLPPVLERASEYFSRltdgr 532
|
490
....*....|....*..
gi 1678729579 2672 -KLAAISEATHLKTEAE 2687
Cdd:COG4717 533 yRLIRIDEDLSLKVDTE 549
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
988-1086 |
1.93e-15 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 75.51 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 988 KEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDPED 1067
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1678729579 1068 -VDVQHPDEKSIITYVSSLY 1086
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4862-4900 |
2.22e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 72.75 E-value: 2.22e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1678729579 4862 LLEAQIATGGIIDPEESHRLPVEVAYKRGFFDEEMNEIL 4900
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1981-2599 |
8.43e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 8.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1981 DSLEEELKKATVVSDKMSRVHSERDVELDHYRQHLSGLQDRWKAVFAQMDIRQRELEQLGRQLGYYHESydwlihwITDA 2060
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER-------RREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2061 KERQEKIQAvsitdskTLKEQLSQEKKLLEEIENNKDNVDECQKYAKAYINSIKDYELQLVaynaqadplasplkktkld 2140
Cdd:COG1196 315 EERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL------------------- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2141 sasdniiqeyvtlrtryselmtltsqyikfitETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKA 2220
Cdd:COG1196 369 --------------------------------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2221 EKEAQElklmmKEEVNRREIAAVDAEKQKQNIQLELHELKNLSEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVK 2300
Cdd:COG1196 417 ERLEEE-----LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2301 QKSTAESELKQLRERAAEAERLRKVAQeeAEKLHKQVIEETQKKRIAEKELqhkseAEKEAAKQKQKALDDLENLKKQAE 2380
Cdd:COG1196 492 RLLLLLEAEADYEGFLEGVKAALLLAG--LRGLAGAVAVLIGVEAAYEAAL-----EAALAAALQNIVVEDDEVAAAAIE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2381 EAERQvkqaevEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREE 2460
Cdd:COG1196 565 YLKAA------KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2461 AEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQ 2540
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678729579 2541 QKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMD 2599
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
868-971 |
1.03e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 73.10 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 868 QKKTFTKWVNKHLIKRAESQHhVTDLYEDLRDGHNLISLLEVLSGDTL------PREKGRMRfhklQNVQIALDFLRHRQ 941
Cdd:cd21213 1 QLQAYVAWVNSQLKKRPGIRP-VQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKR 75
|
90 100 110
....*....|....*....|....*....|
gi 1678729579 942 VKLVNIRNDDIADGNPKLTLGLIWTVILHF 971
Cdd:cd21213 76 IRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2306-2678 |
1.57e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.26 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2306 ESELKQLRERAAEAErlrkvaqEEAEKLHKQVIEetqkkriAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQ 2385
Cdd:TIGR02168 676 RREIEELEEKIEELE-------EKIAELEKALAE-------LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2386 VKQAEVEKERQikvahvaaqKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKEL 2465
Cdd:TIGR02168 742 VEQLEERIAQL---------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2466 EKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTA 2545
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2546 EQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEA 2625
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1678729579 2626 EATKMRDVAEEAGK--LRAIAE-EAKHQRQvaeEEAARQRAEAERILKEKLAAISE 2678
Cdd:TIGR02168 973 RLKRLENKIKELGPvnLAAIEEyEELKERY---DFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
986-1086 |
1.82e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 72.80 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAErDLGVTRLLDP 1065
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1678729579 1066 ED-VDVQHPDEKSIITYVSSLY 1086
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3149-3433 |
2.23e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3149 RLKAEAEMLQRQKDLAQEQaqklleDKQLmqRRLEEE---TEEYQK-SLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKA 3224
Cdd:COG1196 180 KLEATEENLERLEDILGEL------ERQL--EPLERQaekAERYRElKEELKELEAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3225 EEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMADA 3304
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3305 QQKQIEHEKTLLQQtfLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQ 3384
Cdd:COG1196 332 LEELEEELEELEEE--LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1678729579 3385 KEAEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQLEEAQKEQ 3433
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2326-2548 |
2.81e-14 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 78.31 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2326 AQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKalddlenlkkQAEEAERQVKQAEVEKERQIKVAHVAAQ 2405
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK----------QAEEAAKQAALKQKQAEEAAAKAAAAAK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2406 KSAAAElqskhssfvektskleeslkqehgavlqlQQEAAHLKKQQEDAINAREEAEKElekwRQKANEAlrlRLQAEEE 2485
Cdd:PRK09510 147 AKAEAE-----------------------------AKRAAAAAKKAAAEAKKKAEAEAA----KKAAAEA---KKKAEAE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678729579 2486 AHKKslAQEDAEKQ-----KEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQE 2548
Cdd:PRK09510 191 AAAK--AAAEAKKKaeaeaKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
988-1087 |
4.92e-14 |
|
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: 71.22 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 988 KEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDmgKVYRQSN-----LENLEQAFNVAER-DLGVTR 1061
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIP--KINKKPKspfkkRENINLFLNACKKlGLPELD 78
|
90 100
....*....|....*....|....*.
gi 1678729579 1062 LLDPEDVdVQHPDEKSIITYVSSLYD 1087
Cdd:cd00014 79 LFEPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2255-2809 |
4.99e-14 |
|
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: 79.01 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2255 ELHELKNLSEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLRERAAEAERLRKvAQEEAEKLH 2334
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR-EQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2335 KQVIEETQKKriaekeLQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKER-----QIKVAHVAAQKSAA 2409
Cdd:pfam05557 82 KKYLEALNKK------LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEElqerlDLLKAKASEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2410 AELQSKHSSFVEKTSKLEEsLKQEhgavLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKaNEALRlrlqaeEEAHKK 2489
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKE-LEFE----IQSQEQDSEIVKNSKSELARIPELEKELERLREH-NKHLN------ENIENK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2490 SLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMaEKELERQRKVADSTA-----------------QQKLTAEQELIRL 2552
Cdd:pfam05557 224 LLLKEEVEDLKRKLEREEKYREEAATLELEKEKL-EQELQSWVKLAQDTGlnlrspedlsrrieqlqQREIVLKEENSSL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2553 RADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQ-------LEDELAKVRSEMDILIQLKSKAEKEtMSNTEKSKQLLEa 2625
Cdd:pfam05557 303 TSSARQLEKARRELEQELAQYLKKIEDLNKKLKRhkalvrrLQRRVLLLTKERDGYRAILESYDKE-LTMSNYSPQLLE- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2626 eatKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEA---ERILK-----EKLAAISEATHLKTEAEIALKEKEAEN 2697
Cdd:pfam05557 381 ---RIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAqtlERELQalrqqESLADPSYSKEEVDSLRRKLETLELER 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2698 ERLRRaaedeayQRKALEDEANQHK-----KEIEEKIVQLKKSSDAEMERQKAMVDDTLkqrrvvEEEIRILKLNFEKAs 2772
Cdd:pfam05557 458 QRLRE-------QKNELEMELERRClqgdyDPKKTKVLHLSMNPAAEAYQQRKNQLEKL------QAEIERLKRLLKKL- 523
|
570 580 590
....*....|....*....|....*....|....*....
gi 1678729579 2773 SGKLDLELELNKLKNIAEETQQSKLRAE-EEAE-KLRKL 2809
Cdd:pfam05557 524 EDDLEQVLRLPETTSTMNFKEVLDLRKElESAElKNQRL 562
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2171-2732 |
5.09e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2171 ITETQRRLEDEEKAAKKLK--AEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELKLmmkeEVNRREIAAVDAEKQ 2248
Cdd:COG4913 237 LERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL----EELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2249 KQNIQLELH--ELKNLSEQQIKDKGQLVDEA---LQSRTKIEEEIYLIRIQLETTVKQ-KSTAESELKQLRERAAEAERL 2322
Cdd:COG4913 313 RLEARLDALreELDELEAQIRGNGGDRLEQLereIERLERELEERERRRARLEALLAAlGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2323 RKVAQEEAEKLHKQVIEETQKKRIAEKELQHKsEAEKEAAKQKQKALD-DLENLKKQAEEA----ER---------QVKQ 2388
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELREL-EAEIASLERRKSNIPaRLLALRDALAEAlgldEAelpfvgeliEVRP 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2389 AE------VEK----------------------------ERQIKVAHVAAQKSAAAELQSKHSSFVEK----TSKLEESL 2430
Cdd:COG4913 472 EEerwrgaIERvlggfaltllvppehyaaalrwvnrlhlRGRLVYERVRTGLPDPERPRLDPDSLAGKldfkPHPFRAWL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2431 KQEhgavlqLQQEAAHLK-------KQQEDAI-------NAREEAEKELEKWRQKA------NEALRLRLQAEEEAHKKS 2490
Cdd:COG4913 552 EAE------LGRRFDYVCvdspeelRRHPRAItragqvkGNGTRHEKDDRRRIRSRyvlgfdNRAKLAALEAELAELEEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2491 LAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELER-QRKVADstaqqkltAEQELIRLRADFDNAEQqrslLEDE 2569
Cdd:COG4913 626 LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaEREIAE--------LEAELERLDASSDDLAA----LEEQ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2570 LYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKH 2649
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2650 QRQVAEEEAARQRAEAERILKE--------------KLAAISE-ATHLKTEAEIALKEKEAENERLRRAAEDEayQRKAL 2714
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAfnrewpaetadldaDLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIE--FVADL 851
|
650
....*....|....*...
gi 1678729579 2715 EDEANQHKKEIEEKIVQL 2732
Cdd:COG4913 852 LSKLRRAIREIKERIDPL 869
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2322-2766 |
7.85e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 78.66 E-value: 7.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2322 LRKVAQEEAEKLHKQvieETQKKRIAEKELQHKSEAEKEAAKQK---QKALDDLENLKKQAEEAERQVKQAEVEKERqik 2398
Cdd:COG4717 47 LLERLEKEADELFKP---QGRKPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEK--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2399 vahvaaqksaaAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDainaREEAEKELEKWRQKANEALRL 2478
Cdd:COG4717 121 -----------LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2479 RLQAEEEAHKKSLAQ-EDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKvadstaQQKLTAEQELIRLRADFD 2557
Cdd:COG4717 186 LSLATEEELQDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL------EERLKEARLLLLIAAALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2558 NAEQQRSLLEDELYRLKNEVIAA----------QQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEAEA 2627
Cdd:COG4717 260 ALLGLGGSLLSLILTIAGVLFLVlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2628 TKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQ-------------------RAEAERILKEKLAAISEATHLKTEAEI 2688
Cdd:COG4717 340 LELLDRIEELQELLREAEELEEELQLEELEQEIAallaeagvedeeelraaleQAEEYQELKEELEELEEQLEELLGELE 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678729579 2689 ALKEKEAEnERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKK-SSDAEMERQKAMVDDTLKQRRVVEEEIRILKL 2766
Cdd:COG4717 420 ELLEALDE-EELEEELEELEEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
986-1086 |
8.38e-14 |
|
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: 70.83 E-value: 8.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAErDLGVTRLLDP 1065
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1678729579 1066 ED-VDVQHPDEKSIITYVSSLY 1086
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4215-4253 |
8.45e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 68.12 E-value: 8.45e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1678729579 4215 LLEAQASTGFLVDPVRNQCLTVDEAVKSGLVGPELHEKL 4253
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2421-2810 |
1.10e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 77.89 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2421 EKTSKLEEsLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANealRLRLQAEEEAHKKSLAQEDAEKQk 2500
Cdd:COG4717 75 ELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ---LLPLYQELEALEAELAELPERLE- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2501 eeaerEAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQK-LTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIA 2579
Cdd:COG4717 150 -----ELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2580 AQQQRKQLEDE---------------LAKVRSEMDILIQLKSKAEKET-----------------MSNTEKSKQLLEAEA 2627
Cdd:COG4717 225 LEEELEQLENEleaaaleerlkearlLLLIAAALLALLGLGGSLLSLIltiagvlflvlgllallFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2628 TKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDE 2707
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2708 A--YQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMVDDTLKQR-RVVEEEIRILKLNFEKASSGKLDLELELNK 2784
Cdd:COG4717 385 EelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420
....*....|....*....|....*.
gi 1678729579 2785 LKNiAEETQQSKLRAEEEAEKLRKLA 2810
Cdd:COG4717 465 LEE-DGELAELLQELEELKAELRELA 489
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1445-1634 |
1.11e-13 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 73.63 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1445 LHGFISAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDLQAMGERLVRDGHPGKKTVESFT 1524
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1525 AALQTQWSWILQLCCCIEAHLKENTAYYQFFADVKEAQDKMKKMQENMKkkySCDRSTTATRLEDLLQDAVEEKEQLNEY 1604
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 1678729579 1605 KTLATGLNKRAKSIIQLKPRNPTTSIKGKL 1634
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
889-968 |
1.17e-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: 70.31 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 889 HVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRM----RFHKLQNVQIALDFLRHRQV----KLVNIRNDDIADGNPKLT 960
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1678729579 961 LGLIWTVI 968
Cdd:cd21223 105 LALLWRII 112
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2690-3427 |
1.28e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 78.47 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2690 LKEKEAEN-ERLRRAAEDEAYQRKALEDEANqhKKEIEEKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRilklnf 2768
Cdd:TIGR00618 158 LKAKSKEKkELLMNLFPLDQYTQLALMEFAK--KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELK------ 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2769 ekassgklDLELELNKLKnIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRKIAQDELErl 2848
Cdd:TIGR00618 230 --------HLREALQQTQ-QSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAH-- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2849 KKKAEEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKEDSIMHKKlKQEYEKAKKLAKEAEAAKEKAERE 2928
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ-EIHIRDAHEVATSIREISCQQHTL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2929 AALLRQQAEEAERQKAAAEQEAAIqaKAQEDAERLRKEAEFEAAKRAQAEGAALKQKQQADAEMAKHKKLA-EQTLKQKF 3007
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKLQSLCKE--LDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAiTCTAQCEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3008 QVEQELTKVKLKLDDTDKQKSLLDDELQRL--KDEVDDAVKQRGQVEEELFK-----VKVQMEELLKLK------LRIED 3074
Cdd:TIGR00618 456 LEKIHLQESAQSLKEREQQLQTKEQIHLQEtrKKAVVLARLLELQEEPCPLCgscihPNPARQDIDNPGpltrrmQRGEQ 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3075 ENQRLLKKDKDNSQKfLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEA 3154
Cdd:TIGR00618 536 TYAQLETSEEDVYHQ-LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQ 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3155 EMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAqtkAEEEAKKFKKQ 3234
Cdd:TIGR00618 615 HALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQL---ALQKMQSEKEQ 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3235 ADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQN-KSKEMADAQQKQIEHEK 3313
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARtVLKARTEAHFNNNEEVT 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3314 TLLQ-----QTFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQQMEEEKK----KLHATMHEALSKQ 3384
Cdd:TIGR00618 772 AALQtgaelSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleEKSATLGEITHQL 851
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1678729579 3385 KEAEK------EMLSKQKEMQELEKKrleQEIILADENQKLREKLQQLE 3427
Cdd:TIGR00618 852 LKYEEcskqlaQLTQEQAKIIQLSDK---LNGINQIKIQFDGDALIKFL 897
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2247-2577 |
1.30e-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: 77.86 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2247 KQKQNIQLELHELKNLSEQQIKDKGQLVDEAL----QSRTKIEEEIYLIRIQLETTVKQ-KSTAESELKQLRERAAEAER 2321
Cdd:pfam17380 303 QEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKRElERIRQEEIAMEISRMRELER 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2322 LRKVAQEEAEKLhKQVIEETQKKRIAEKELQHKSEAEKEaakqkqkaldDLENLKKQAEEA-ERQVKQAEVEKERQIkva 2400
Cdd:pfam17380 383 LQMERQQKNERV-RQELEAARKVKILEEERQRKIQQQKV----------EMEQIRAEQEEArQREVRRLEEERAREM--- 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2401 hvaaqksaaaelqskhssfvektskleESLKQEHgavLQLQQEAAHLKKQQEDAINAREEAEKELEKwRQKANEALRLRL 2480
Cdd:pfam17380 449 ---------------------------ERVRLEE---QERQQQVERLRQQEEERKRKKLELEKEKRD-RKRAEEQRRKIL 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2481 QAEEEAHKKSLAQEDAEK---QKEEAER-----EAKKRAKAEESALKQKDMAEKElerqrkvadSTAQQKLTAEQELIRL 2552
Cdd:pfam17380 498 EKELEERKQAMIEEERKRkllEKEMEERqkaiyEEERRREAEEERRKQQEMEERR---------RIQEQMRKATEERSRL 568
|
330 340
....*....|....*....|....*
gi 1678729579 2553 RADFDNAEQQRSLLEDELYRLKNEV 2577
Cdd:pfam17380 569 EAMEREREMMRQIVESEKARAEYEA 593
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4548-4586 |
1.34e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 67.74 E-value: 1.34e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1678729579 4548 LLETQAATGFIVDPVNNETLTVDEAVRKGVVGPEIHDKL 4586
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2465-3098 |
1.59e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.77 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2465 LEKWRQKANEAlrlRLQAEEEAHKKSLAQEDAEKQKEEAE-REAKKRAKAEESALKQKDMAEKELERQRKVADST---AQ 2540
Cdd:PRK02224 164 LEEYRERASDA---RLGVERVLSDQRGSLDQLKAQIEEKEeKDLHERLNGLESELAELDEEIERYEEQREQARETrdeAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2541 QKLTA----EQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDIliqlkSKAEKETMsnt 2616
Cdd:PRK02224 241 EVLEEheerREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGL-----DDADAEAV--- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2617 EKSKQLLEAEATKMRDVAEE----AGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEAThlktEAEIALKE 2692
Cdd:PRK02224 313 EARREELEDRDEELRDRLEEcrvaAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE----DRREEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2693 KEAENERLRRAAEDEAYQRKALEDeanqHKKEIEEKIVQLKkSSDAEMERQKAMVDDTLKQRRV-------------VEE 2759
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAED----FLEELREERDELR-EREAELEATLRTARERVEEAEAlleagkcpecgqpVEG 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2760 EIRILKLNFEKASSGKLDLELElnklkniAEETQQSKLRAE-EEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQR 2838
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELE-------DLEEEVEEVEERlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2839 KiaqdelerlkkKAEEARKQKDEADVEAEVQIVAAQQAalkcstaehqvqsvlaqqkedsimhkklkqeyekakklakea 2918
Cdd:PRK02224 537 E-----------RAEELRERAAELEAEAEEKREAAAEA------------------------------------------ 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2919 eaakekaereaallRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQAEGAALKQKQQADAEMAKHKKL 2998
Cdd:PRK02224 564 --------------EEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERL 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2999 AE-----QTLKQKFQvEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELfkvkvqmEELLKLKLRIE 3073
Cdd:PRK02224 630 AEkrerkRELEAEFD-EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL-------EELEELRERRE 701
|
650 660
....*....|....*....|....*
gi 1678729579 3074 DENQRLLKKDKDNSQkflAEEAENM 3098
Cdd:PRK02224 702 ALENRVEALEALYDE---AEELESM 723
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3142-3454 |
1.73e-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: 77.47 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3142 QAIQESSRLKAEAEMLQRQKDLAQEQAQKLLEdkQLMQRRLEEETEEyqKSLEAERRRQLEivaEAEKLKlQVSQLSEAQ 3221
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFE--KMEQERLRQEKEE--KAREVERRRKLE---EAEKAR-QAEMDRQAA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3222 TKAEEE--AKKFKKQADKIA--------ARLHETEIATK-EKMTVVEKLEFERLNTSKEAGDLRDAIAD---LEKDKAR- 3286
Cdd:pfam17380 335 IYAEQErmAMERERELERIRqeerkrelERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKvkiLEEERQRk 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3287 LKKEAEELQNKSKEMADAQQKQIEhektLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQQM 3366
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEARQREVR----RLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3367 EEEKKKLHATMH-------EALSKQKEAEKEMLSKQKEMQE-----------------LEKKRLEQEIILADEN------ 3416
Cdd:pfam17380 491 EQRRKILEKELEerkqamiEEERKRKLLEKEMEERQKAIYEeerrreaeeerrkqqemEERRRIQEQMRKATEErsrlea 570
|
330 340 350
....*....|....*....|....*....|....*....
gi 1678729579 3417 -QKLREKLQQLEEAQKEQhtvpdKELICVTTVDTTKKVY 3454
Cdd:pfam17380 571 mEREREMMRQIVESEKAR-----AEYEATTPITTIKPIY 604
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2360-3107 |
2.64e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.26 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2360 EAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKT---------SKLEESL 2430
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRrlelleaelEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2431 KQEHGAVLQLQQEAAHLKKQQEDAINAR--------EEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEE 2502
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2503 AEREAKKRAKAEESalkqkdmaekELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELyrlkneviaaQQ 2582
Cdd:COG4913 385 LRAEAAALLEALEE----------ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL----------LA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2583 QRKQLEDELAKVRSEMDI---LIQLKSKAEketmsntekskqlleaeatKMRDVAEEA--GKLRAIAEEAKHQRQVA--- 2654
Cdd:COG4913 445 LRDALAEALGLDEAELPFvgeLIEVRPEEE-------------------RWRGAIERVlgGFALTLLVPPEHYAAALrwv 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2655 EEEAARQRAEAERILKEKLAAISEATHLKTEAE-IALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKiVQLK 2733
Cdd:COG4913 506 NRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGkLDFKPHPFRAWLEAELGRRFDYVCVDSPEELRRHPRAITRA-GQVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2734 KSSDAemeRQKamvDDtlkQRRVVEEEIrilkLNFEKASsgKLD-LELELNKLKNIAEETQQSKLRAEEEAEKLRKLALE 2812
Cdd:COG4913 585 GNGTR---HEK---DD---RRRIRSRYV----LGFDNRA--KLAaLEAELAELEEELAEAEERLEALEAELDALQERREA 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2813 EEKRRREAEEKVKKITAAEEEAARQRKIAQ-----DELERLKKKAEEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQV 2887
Cdd:COG4913 650 LQRLAEYSWDEIDVASAEREIAELEAELERldassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2888 QSVLAQQKEDSIMHKKLKQEYEKAkklakeaeaakekaereaalLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEA 2967
Cdd:COG4913 730 DELQDRLEAAEDLARLELRALLEE--------------------RFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2968 E--FEAAKRAQAEGAALKQKQQADAE--MAKHKKLAEQTL---KQKFQveqeltkvKLKLDDTDKQKSLLddeLQRLKDE 3040
Cdd:COG4913 790 EraMRAFNREWPAETADLDADLESLPeyLALLDRLEEDGLpeyEERFK--------ELLNENSIEFVADL---LSKLRRA 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3041 VDDAVKQRGQVEEELFKVKVQMEELLKLKLRIE-----DENQRLLKKDKDNSQKFLAEEAEN--------MKRLAEDAAR 3107
Cdd:COG4913 859 IREIKERIDPLNDSLKRIPFGPGRYLRLEARPRpdpevREFRQELRAVTSGASLFDEELSEArfaalkrlIERLRSEEEE 938
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
861-965 |
3.28e-13 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 68.85 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 861 EDERDrvqKKTFTKWVNKHLIKraesqHHVTDLYEDLRDGhnlISLLEVLsgDTL-P---------REKGRMRFHKLQNV 930
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLD-----PLINNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENC 67
|
90 100 110
....*....|....*....|....*....|....*
gi 1678729579 931 QIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIW 965
Cdd:cd21219 68 NYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVW 102
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2933-3249 |
3.54e-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: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2933 RQQAEEAERQKAAAEQEAAIQaKAQEdAERLRKEAEFEAAKRAQAEGAALKQKQQADAEMAKHKKL----AEQTLKQKFQ 3008
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEE-KARE-VERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELerirQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3009 VEQELTKVKL-KLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLLkkdkdns 3087
Cdd:pfam17380 365 IRQEEIAMEIsRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV------- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3088 QKFLAEEAENMKRLAEDAARlsvESQEAARLRQIAEDDliQQRALADKMLKEKMQAIQESSRLKAEAEMLQR-QKDLAQE 3166
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQE---RQQQVERLRQQEEER--KRKKLELEKEKRDRKRAEEQRRKILEKELEERkQAMIEEE 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3167 QAQKLLEdKQLMQRRLEEETEEYQKSLEAERRRQLEIvAEAEKLKLQVSQLSEAQTKAE--EEAKKFKKQADKIAARLHE 3244
Cdd:pfam17380 513 RKRKLLE-KEMEERQKAIYEEERRREAEEERRKQQEM-EERRRIQEQMRKATEERSRLEamEREREMMRQIVESEKARAE 590
|
....*
gi 1678729579 3245 TEIAT 3249
Cdd:pfam17380 591 YEATT 595
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2309-2529 |
6.29e-13 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 74.46 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2309 LKQLRERAAEAERLR-KVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDlenlKKQAEEAerQVK 2387
Cdd:PRK09510 67 QQQQQKSAKRAEEQRkKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALK----QKQAEEA--AAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2388 QAEVEK---ERQIKVAHVAAQKSAAaelqskhssfvEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDainAREEAEKE 2464
Cdd:PRK09510 141 AAAAAKakaEAEAKRAAAAAKKAAA-----------EAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAE---AKKKAEAE 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678729579 2465 LEKwrqkanealrlrlQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELE 2529
Cdd:PRK09510 207 AKK-------------KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2364-2715 |
8.86e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 75.16 E-value: 8.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2364 QKQKALDDLENLKKQAEEAERQVKQAEVEKERQikvahvaaqksaaaelqskhssfVEKTSKLEESLKQEHGAvlqLQQE 2443
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKARE-----------------------VERRRKLEEAEKARQAE---MDRQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2444 AAHLKKQQEDAInareEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEeSALKQKDM 2523
Cdd:pfam17380 333 AAIYAEQERMAM----ERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELE-AARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2524 AEkelERQRKVADSTAQ-QKLTAEQELIRLRaDFDNAEQQRsllEDELYRLKNEVIAAQQQ---RKQLEDELAKVRSEMD 2599
Cdd:pfam17380 408 EE---ERQRKIQQQKVEmEQIRAEQEEARQR-EVRRLEEER---AREMERVRLEEQERQQQverLRQQEEERKRKKLELE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2600 iliqlksKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVA-EEEAARQRAEAER---ILKEKLAA 2675
Cdd:pfam17380 481 -------KEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAiYEEERRREAEEERrkqQEMEERRR 553
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1678729579 2676 ISEATHLKTEAEIALKEKEAENERLRRAAEDEAyQRKALE 2715
Cdd:pfam17380 554 IQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2503-2705 |
9.12e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 73.64 E-value: 9.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2503 AEREAKKRAKAEESALKQK-DMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQ 2581
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2582 QQRKQLEDELAKV---------RSEMDILiqLKSKAEKETMSNTEKSKQLLEA---EATKMRDVAEEAGKLRAIAEEAKH 2649
Cdd:COG4942 97 AELEAQKEELAELlralyrlgrQPPLALL--LSPEDFLDAVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1678729579 2650 QRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAE 2705
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3557-3594 |
1.34e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 64.66 E-value: 1.34e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1678729579 3557 LLEAQAATGYMLDPMKNQKLSVNEAVKEGLIGPELHNK 3594
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2306-2714 |
1.38e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 74.99 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2306 ESELKQLRERAAEAERlrKVAQEEaeklhkqvieetqkkriaEKELQHKSEAEkeAAKQKQKALDDL---------ENLK 2376
Cdd:PRK04863 836 EAELRQLNRRRVELER--ALADHE------------------SQEQQQRSQLE--QAKEGLSALNRLlprlnlladETLA 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2377 KQAEEAERQVKQAEVEKerqikvAHVAAQKSAAAELQSKHSSFVEKTSKLEEsLKQEHGAVLQLQQEAahlkKQQEDAI- 2455
Cdd:PRK04863 894 DRVEEIREQLDEAEEAK------RFVQQHGNALAQLEPIVSVLQSDPEQFEQ-LKQDYQQAQQTQRDA----KQQAFALt 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2456 --NAR------EEAEKELEKwRQKANEALRLRLqaeeeahkkslaqedaeKQKEEAEREAKKRAKAEESALKQKDMAEKE 2527
Cdd:PRK04863 963 evVQRrahfsyEDAAEMLAK-NSDLNEKLRQRL-----------------EQAEQERTRAREQLRQAQAQLAQYNQVLAS 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2528 LerqrKVADSTAQQKLT-AEQEL--IRLRADFdNAEQQRSLLEDELYrlkNEVIAAQQQRKQLEDELAKVRSEMDILIQL 2604
Cdd:PRK04863 1025 L----KSSYDAKRQMLQeLKQELqdLGVPADS-GAEERARARRDELH---ARLSANRSRRNQLEKQLTFCEAEMDNLTKK 1096
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2605 KSKAEKetmsnteKSKQLLEAEatkmrdVAEEAGKLRAIaeeakhqrqvaeeEAARQRAEAERILKEKLAAISeATHLKT 2684
Cdd:PRK04863 1097 LRKLER-------DYHEMREQV------VNAKAGWCAVL-------------RLVKDNGVERRLHRRELAYLS-ADELRS 1149
|
410 420 430
....*....|....*....|....*....|
gi 1678729579 2685 EAEIALkekeaenERLRRAAEDEAYQRKAL 2714
Cdd:PRK04863 1150 MSDKAL-------GALRLAVADNEHLRDVL 1172
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2300-2542 |
2.51e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.49 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2300 KQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVieETQKKRIAEKELQHKsEAEKEAAKQKQKalddLENLKKQA 2379
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL--AALERRIAALARRIR-ALEQELAALEAE----LAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2380 EEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKHSSfvektSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINARE 2459
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDF-----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2460 EAEKELEKWRQ--KANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADS 2537
Cdd:COG4942 168 ELEAERAELEAllAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*
gi 1678729579 2538 TAQQK 2542
Cdd:COG4942 248 FAALK 252
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2326-2542 |
2.98e-12 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 71.80 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2326 AQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENlKKQAEEAERQVKQAEVEKERQIKVAHVAAQ 2405
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQ-RAAAEKAAKQAEQAAKQAEEKQKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2406 KSAAaelqskhssfvEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRlRLQAEEE 2485
Cdd:TIGR02794 127 KQAA-----------EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEA-KAKAEEA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678729579 2486 AHKKSLAQEDAEKQ-KEEAEREAKKRAKAEesalKQKDMAEKELERQRKVADSTAQQK 2542
Cdd:TIGR02794 195 KAKAEAAKAKAAAEaAAKAEAEAAAAAAAE----AERKADEAELGDIFGLASGSNAEK 248
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2276-2671 |
3.97e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2276 EALQSR-TKIEEEIYLIRIQLETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHK 2354
Cdd:PRK02224 317 EELEDRdEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2355 SEAEKEAAKQKQKALDDLENLKKQ-----AEEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEES 2429
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREErdelrEREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRER 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2430 LKQEHGAVLQLQQEAAHLKKQQEDAINAReEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAK- 2508
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEe 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2509 KRAKAEESALKQKDMAEK-------------ELERQRKVADSTAQQKlTAEQELIRL---RADFDNAEQQR--------- 2563
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEvaelnsklaelkeRIESLERIRTLLAAIA-DAEDEIERLrekREALAELNDERrerlaekre 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2564 --SLLEDELYrlKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKEtMSNTEKSKQLLEAEATKMRDVAEEAGKLR 2641
Cdd:PRK02224 635 rkRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAE-IGAVENELEELEELRERREALENRVEALE 711
|
410 420 430
....*....|....*....|....*....|....
gi 1678729579 2642 AIAEEAKH----QRQVAEEEAARQRAEAERILKE 2671
Cdd:PRK02224 712 ALYDEAEElesmYGDLRAELRQRNVETLERMLNE 745
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2844-3431 |
4.47e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 73.08 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2844 ELERLKKKAEEARKQKDEADVEAEVQIVAAQQAAL-----------KCSTAEHQVQSVLAQQKEDSIMHKKLKQEYEKAK 2912
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctpcmpdtyheRKQVLEKELKHLREALQQTQQSHAYLTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2913 KLAKeaeaakekaereaalLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAefeaakRAQAEGAALKQKQQADAEM 2992
Cdd:TIGR00618 254 EQLK---------------KQQLLKQLRARIEELRAQEAVLEETQERINRARKAA------PLAAHIKAVTQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2993 AKHKKLAEQTLKQKFQVEQELTKVKLKLddtdKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRI 3072
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSI----EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3073 EdenqRLLKKDKDNSQKFLAEEAENMKRLAEDAARlSVESQEAARLR---QIAEDDLIQQRALADKMLKEKMQAIQESSR 3149
Cdd:TIGR00618 389 T----TLTQKLQSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKkqqELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3150 ----LKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQvsQLSEAQTKAE 3225
Cdd:TIGR00618 464 saqsLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ--RGEQTYAQLE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3226 EEAKKFKKQADKIAARLHEteiaTKEKMTvvekleferlntskeagDLRDAIADLEKDKARLKKEAEELQNKSKEMADAQ 3305
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRAS----LKEQMQ-----------------EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3306 QKQIEHEKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQfeEEAKKSKALKDEQERQKQQMEEEK-------KKLHATMH 3378
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ--ELALKLTALHALQLTLTQERVREHalsirvlPKELLASR 678
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1678729579 3379 EALSKQKEAEKEMLSKQKEM--QELEKKRLEQEIILadENQKLREKLQQLEEAQK 3431
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMlaQCQTLLRELETHIE--EYDREFNEIENASSSLG 731
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2315-2794 |
6.10e-12 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 71.98 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2315 RAAEAERlRKVAQEEAEKLHKQVIEETQKKRIAEKelqhkseaekeaakQKQKALDDLENLKKQAEEAERQVKQAEVEKE 2394
Cdd:pfam05701 30 RIQTVER-RKLVELELEKVQEEIPEYKKQSEAAEA--------------AKAQVLEELESTKRLIEELKLNLERAQTEEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2395 R--------QIKVAH----VAAQKSAAAELQ-----SKHSSFVE--KTSKLE-ESLKQEHGAVLQLQQEAAhlkKQQEDA 2454
Cdd:pfam05701 95 QakqdselaKLRVEEmeqgIADEASVAAKAQlevakARHAAAVAelKSVKEElESLRKEYASLVSERDIAI---KRAEEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2455 INAREEAEK-------ELEKWRQKANEALRLRLQAEEEAHKKSLA-QEDA---EKQKEEAEREAKK-------------- 2509
Cdd:pfam05701 172 VSASKEIEKtveeltiELIATKESLESAHAAHLEAEEHRIGAALArEQDKlnwEKELKQAEEELQRlnqqllsakdlksk 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2510 ---------RAKAE-----ESALKQKDMAEKELErqrKVADSTAQQKLTAEQELIRLRADFDNAEQQRSL-------LED 2568
Cdd:pfam05701 252 letasalllDLKAElaaymESKLKEEADGEGNEK---KTSTSIQAALASAKKELEEVKANIEKAKDEVNClrvaaasLRS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2569 ELYRLKNEVIAAQQQR-------KQLEDELAKVRSEMDiLIQLKSKAEKETMsnTEKSKQLLEAeatkmrdvAEEAGKLR 2641
Cdd:pfam05701 329 ELEKEKAELASLRQREgmasiavSSLEAELNRTKSEIA-LVQAKEKEAREKM--VELPKQLQQA--------AQEAEEAK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2642 AIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEA--ENERLRRAAEDEAYQR-------- 2711
Cdd:pfam05701 398 SLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTNQEDSPRgvtlslee 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2712 ------KALEDEANQHKKeIEEKIVQLKKSSDAEMeRQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKL 2785
Cdd:pfam05701 478 yyelskRAHEAEELANKR-VAEAVSQIEEAKESEL-RSLEKLEEVNREMEERKEALKIALEKAEKAKEGKLAAEQELRKW 555
|
....*....
gi 1678729579 2786 KniAEETQQ 2794
Cdd:pfam05701 556 R--AEHEQR 562
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2306-2754 |
7.87e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 72.68 E-value: 7.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2306 ESELKQLRERAAEAERlrkvAQEEAEklhkqvieetqkkriaEKELQHKSEAEkeAAKQKQKALDDL---------ENLK 2376
Cdd:COG3096 835 EAELAALRQRRSELER----ELAQHR----------------AQEQQLRQQLD--QLKEQLQLLNKLlpqanlladETLA 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2377 KQAEEAERQVKQAEVEKerqikvAHVAAQKSAAAELQSKHSSfVEKTSKLEESLKQEHGAVLQLQQEAahlkKQQEDAIN 2456
Cdd:COG3096 893 DRLEELREELDAAQEAQ------AFIQQHGKALAQLEPLVAV-LQSDPEQFEQLQADYLQAKEQQRRL----KQQIFALS 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2457 ---------AREEAEKELEKwRQKANEALRLRLqaeeeahkkslaqEDAEKQKEEAeREAKKRAKAeesalkQKDMAEKE 2527
Cdd:COG3096 962 evvqrrphfSYEDAVGLLGE-NSDLNEKLRARL-------------EQAEEARREA-REQLRQAQA------QYSQYNQV 1020
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2528 LERQRKVADSTAQQKLTAEQEL--IRLRADfDNAEQQRSLLEDELYrlkNEVIAAQQQRKQLEDELAKVRSEMDILIQLK 2605
Cdd:COG3096 1021 LASLKSSRDAKQQTLQELEQELeeLGVQAD-AEAEERARIRRDELH---EELSQNRSRRSQLEKQLTRCEAEMDSLQKRL 1096
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2606 SKAEKETmsnTEKSKQLLEAEATKMRdvaeeagkLRAIAEEAKHQRQVAEEEAARQRAeaerilkEKLAAISEathlktE 2685
Cdd:COG3096 1097 RKAERDY---KQEREQVVQAKAGWCA--------VLRLARDNDVERRLHRRELAYLSA-------DELRSMSD------K 1152
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678729579 2686 AEIALKEKEAENERLR---RAAEDEAY-QRK-ALEDEANQHKKE-IEEKIVQLKKSSDA--EMERQKAMVDDTLKQR 2754
Cdd:COG3096 1153 ALGALRLAVADNEHLRdalRLSEDPRRpERKvQFYIAVYQHLRErIRQDIIRTDDPVEAieQMEIELARLTEELTSR 1229
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2347-2603 |
7.97e-12 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 70.26 E-value: 7.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2347 AEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAerqvKQAEVEKERQIKVAHVAAQKSAAAELQSKhssfvektskl 2426
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQ----RAAEQARQKELEQRAAAEKAAKQAEQAAK----------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2427 eeslkqehgAVLQLQQEAAHLKKQQEDAINAREEAEKElekwrQKANEALRLrlQAEEEAHKKslAQEDAEKQKEEAERE 2506
Cdd:TIGR02794 113 ---------QAEEKQKQAEEAKAKQAAEAKAKAEAEAE-----RKAKEEAAK--QAEEEAKAK--AAAEAKKKAEEAKKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2507 AKKRAKAEESALKQK--DMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQR 2584
Cdd:TIGR02794 175 AEAEAKAKAEAEAKAkaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
|
250
....*....|....*....
gi 1678729579 2585 KQLEDELAKVRSEMDILIQ 2603
Cdd:TIGR02794 255 AAAGSEVDKYAAIIQQAIQ 273
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2624-3441 |
8.55e-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: 72.46 E-value: 8.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2624 EAEATKMRDVAEEAGK--LRAIAEEAKHQrqvAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLR 2701
Cdd:pfam15921 58 EVELDSPRKIIAYPGKehIERVLEEYSHQ---VKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2702 RAAEDEAYQRKALEDEANQHK--KEIEEKIVqlkKSSDAEMERQKAMvddtLKQRRVVEEEIRILKLNFEKASSGKLDLE 2779
Cdd:pfam15921 135 RESQSQEDLRNQLQNTVHELEaaKCLKEDML---EDSNTQIEQLRKM----MLSHEGVLQEIRSILVDFEEASGKKIYEH 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2780 LELNKLKNIAEETQQSKLRAEEEAEklrklaleeekrrreAEEKVKKITAAEEEAARQRKIAQDELERLKKKAEEARKQK 2859
Cdd:pfam15921 208 DSMSTMHFRSLGSAISKILRELDTE---------------ISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2860 DEadvEAEVQIVAAQQaalKCSTAEHQVQSVLAQQKedsIMHKKLKQEYEKAKKLAKEAEAAKEKaereaalLRQQAEEA 2939
Cdd:pfam15921 273 IS---EHEVEITGLTE---KASSARSQANSIQSQLE---IIQEQARNQNSMYMRQLSDLESTVSQ-------LRSELREA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2940 ERqkaAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQAEGAALKQKQQADAEMAKHKKlaeqtlkqKFQVEQELTKvklK 3019
Cdd:pfam15921 337 KR---MYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREK--------ELSLEKEQNK---R 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3020 LDDTDKQKSLLDDELQRlkdEVDDAVKQRGQVEEELFKVKVQMEELLKLKLR-IEDENQRLLKKDKDNSQkfLAEEAENM 3098
Cdd:pfam15921 403 LWDRDTGNSITIDHLRR---ELDDRNMEVQRLEALLKAMKSECQGQMERQMAaIQGKNESLEKVSSLTAQ--LESTKEML 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3099 KRLAED--AARLSVESQEaarlrqiaeddliqqRALAD--KMLKEKMQAIQESSrlkAEAEMLQRQKDLAQEQAQKL--- 3171
Cdd:pfam15921 478 RKVVEEltAKKMTLESSE---------------RTVSDltASLQEKERAIEATN---AEITKLRSRVDLKLQELQHLkne 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3172 ---LEDKQLMQRRLEEETEEYQKSLEAERRR---QLEIVAE----AEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAAR 3241
Cdd:pfam15921 540 gdhLRNVQTECEALKLQMAEKDKVIEILRQQienMTQLVGQhgrtAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3242 LHETEI--------------ATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEaeeLQNKSKEMADAQQK 3307
Cdd:pfam15921 620 IRELEArvsdlelekvklvnAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN---FRNKSEEMETTTNK 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3308 ---QIEHEKTLLQQTFLTEREM---------------LLKKEKLIEEEKKKLESQFEEEA-----KKSKALKDEQERQKQ 3364
Cdd:pfam15921 697 lkmQLKSAQSELEQTRNTLKSMegsdghamkvamgmqKQITAKRGQIDALQSKIQFLEEAmtnanKEKHFLKEEKNKLSQ 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3365 QME---EEKKKLHATMhEALSKQKEAEKEMLSKQKemQELEKKRLE----QEIILADENQKLREKLqqleeaqkeQHTVP 3437
Cdd:pfam15921 777 ELStvaTEKNKMAGEL-EVLRSQERRLKEKVANME--VALDKASLQfaecQDIIQRQEQESVRLKL---------QHTLD 844
|
....
gi 1678729579 3438 DKEL 3441
Cdd:pfam15921 845 VKEL 848
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3022-3435 |
1.08e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3022 DTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLLKKDKdNSQKFLAEEAENMKRL 3101
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEG-SKRKLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3102 AEDAARLSVESQEAARLRQIAEDDL--IQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQkdlaqeqaqklLEDKQLMQ 3179
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER-----------IKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3180 RRLEEETEEyqkslEAERRRQLEIVAEAEKLKLQVSQLseaQTKAEEEAKKFK-KQADKIAARLHETEIATKEKMTVVEK 3258
Cdd:PRK03918 338 ERLEELKKK-----LKELEKRLEELEERHELYEEAKAK---KEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3259 LEFERLNTSKEAGDLRDAIADLEKDKAR----------------LKKEAEELQNKSKEMA--DAQQKQIEHEKTLLQQTF 3320
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKELKeiEEKERKLRKELRELEKVL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3321 LTEREMllkkeklieeekkkleSQFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMLSKQKEMQE 3400
Cdd:PRK03918 490 KKESEL----------------IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
410 420 430
....*....|....*....|....*....|....*
gi 1678729579 3401 LEKKRLEqeiiladenqkLREKLQQLEEAQKEQHT 3435
Cdd:PRK03918 554 LKKKLAE-----------LEKKLDELEEELAELLK 577
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
988-1083 |
1.09e-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: 64.33 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 988 KEKLLLWSQRMTGDyqnIRCDNFSTSWRDGKLFNAVIHKHHPRLI-DMGKVYRQSNLENLEQAFNVAERDLGVTRLLDPE 1066
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1678729579 1067 DVDVQHPDEKSIITYVS 1083
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5136-5174 |
1.34e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.34e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1678729579 5136 LLEAQACTGGIIDPTTGERFQVSDATEKGLVDKIMVDRL 5174
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2135-2482 |
1.36e-11 |
|
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: 71.63 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2135 KKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKKLKAEEQKKMAEMQ------AELDKQKQ 2208
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAqlskelTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2209 LAAAHAKAIAKAEKEAQELKLMMKEEVNRREIAAVDAEKQKQNIQLELHELK----------NLSEQQIKDKGQLVDEAL 2278
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaanlrerlESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2279 QSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAE 2358
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2359 KEAAKQKQKALDDLENLKKQAEEaerqvkqaEVEKERQIKVAHVAAQKSAAAELQskhssfvEKTSKLEESLKqEHGAV- 2437
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSE--------EYSLTLEEAEALENKIEDDEEEAR-------RRLKRLENKIK-ELGPVn 988
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1678729579 2438 -------LQLQQEAAHLKKQQEDAinarEEAEKELEKWRQKANEALRLRLQA 2482
Cdd:TIGR02168 989 laaieeyEELKERYDFLTAQKEDL----TEAKETLEEAIEEIDREARERFKD 1036
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2052-2728 |
1.39e-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: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2052 WLIHWITDAKERQEKIQ---AVSITDSKTLKE-QLSQEK---KLLEEIENNKDNVDEcQKYAKAYINSIKdyelQLVAYN 2124
Cdd:pfam05483 93 WKVSIEAELKQKENKLQenrKIIEAQRKAIQElQFENEKvslKLEEEIQENKDLIKE-NNATRHLCNLLK----ETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2125 AQadplasplKKTKLDSASDNIIQEYVTLRTRYsELMTLTSQYIKFITETQR-----RLEDEEKAAKKLKAEEQKKMAEM 2199
Cdd:pfam05483 168 AE--------KTKKYEYEREETRQVYMDLNNNI-EKMILAFEELRVQAENARlemhfKLKEDHEKIQHLEEEYKKEINDK 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2200 QAEL-----------DKQKQLAAAHAKAIAKAEKEAQELKLM---MKEEVNRREIAAVDAEKQKQNIQLELHELKNLSEQ 2265
Cdd:pfam05483 239 EKQVsllliqitekeNKMKDLTFLLEESRDKANQLEEKTKLQdenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEED 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2266 -QIKDKG--QLVDEA---LQSRTKIEEEIYLIRIQLETTVkqkSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIE 2339
Cdd:pfam05483 319 lQIATKTicQLTEEKeaqMEELNKAKAAHSFVVTEFEATT---CSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2340 ETQKKRIAEKELqhksEAEKEAAKQKQKALDDLENLKKQAEEAE---------RQVKQAEVEK-ERQIKVAHVAAQ---- 2405
Cdd:pfam05483 396 MTKFKNNKEVEL----EELKKILAEDEKLLDEKKQFEKIAEELKgkeqeliflLQAREKEIHDlEIQLTAIKTSEEhylk 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2406 --KSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRlqAE 2483
Cdd:pfam05483 472 evEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR--DE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2484 EEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMA--EKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQ 2561
Cdd:pfam05483 550 LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENK 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2562 QRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVrsemdilIQLKSKAEKETMSNTEKSKQLLEaEATKMRD-----VAEE 2636
Cdd:pfam05483 630 QLNAYEIKVNKLELELASAKQKFEEIIDNYQKE-------IEDKKISEEKLLEEVEKAKAIAD-EAVKLQKeidkrCQHK 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2637 AGKLRAIAEEAKHQRQVAEEEaarqRAEAERILKEKLaaiSEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALED 2716
Cdd:pfam05483 702 IAEMVALMEKHKHQYDKIIEE----RDSELGLYKNKE---QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKM 774
|
730
....*....|..
gi 1678729579 2717 EANQHKKEIEEK 2728
Cdd:pfam05483 775 EAKENTAILKDK 786
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2526-3409 |
1.46e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 71.62 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2526 KELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRslleDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLK 2605
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIR----DQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2606 SKAEK-----ETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQV--AEEEAARQRAEAERILKEKLAAISE 2678
Cdd:TIGR00606 262 SKIMKldneiKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVreKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2679 ATHLktEAEIALKEKEAENERLRRAAEDEAYQRKALEDEAN--QHKKEIEEKIVQLKKSSDAEMERQKAMV--------- 2747
Cdd:TIGR00606 342 KTEL--LVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDgfERGPFSERQIKNFHTLVIERQEDEAKTAaqlcadlqs 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2748 DDTLKQRRVVEEEIRILKLNfEKASSGKLDLELELNKLKNIAEETQQSK------LRAEEEAEK-LRKLALEEEKRRREA 2820
Cdd:TIGR00606 420 KERLKQEQADEIRDEKKGLG-RTIELKKEILEKKQEELKFVIKELQQLEgssdriLELDQELRKaERELSKAEKNSLTET 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2821 EEKVKKITAAEEEAARQRKIAQDELERLKKKAEEARKQ-----KDEADVEAEVQIVAAQQAALKCSTAEHqvqsvLAQQK 2895
Cdd:TIGR00606 499 LKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQmemltKDKMDKDEQIRKIKSRHSDELTSLLGY-----FPNKK 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2896 EDSIMHKKLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAAIQAKAQE---DAERLRKEAEFEAA 2972
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDeesDLERLKEEIEKSSK 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2973 KRAQAEGAALKQKQQADAEMAKHKKLAEqTLKQKFQVEQELTKVKLKLDDT-----DKQKSLlDDELQRLKDEVDDAVKQ 3047
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTDENQSCCP-VCQRVFQTEAELQEFISDLQSKlrlapDKLKST-ESELKKKEKRRDEMLGL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3048 RGQVEEELFKVKVQMEELLKLKLRIEDENQRLlKKDKDNSQKFLAE---EAENMKRLAEDAA---RLSVESQEAAR--LR 3119
Cdd:TIGR00606 732 APGRQSIIDLKEKEIPELRNKLQKVNRDIQRL-KNDIEEQETLLGTimpEEESAKVCLTDVTimeRFQMELKDVERkiAQ 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3120 QIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQKLledkqlmQRRLEE-ETEEYQKSLEAERR 3198
Cdd:TIGR00606 811 QAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL-------KSKTNElKSEKLQIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3199 RQLE-----IVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKlefERLNTSKEAGDL 3273
Cdd:TIGR00606 884 QQFEeqlveLSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE---KVKNIHGYMKDI 960
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3274 RDAIADLEKDKARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQQTFLTER--------EMLLKKEKLIEEEKKKLESQF 3345
Cdd:TIGR00606 961 ENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKiqerwlqdNLTLRKRENELKEVEEELKQH 1040
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 3346 EEEAKKSKALKDEQERQKqqMEEEKKKLHATMHEALSKQKEAEKEMLSKQKEMQELEKKRLEQE 3409
Cdd:TIGR00606 1041 LKEMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
860-974 |
1.60e-11 |
|
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: 64.18 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 860 IEDERDrvqKKTFTKWVNkhlikraeS---QHHVTDLYEDLRDGHNLISLLEVL-------SGDTLPREKGRMRFHKLQN 929
Cdd:cd21298 2 IEETRE---EKTYRNWMN--------SlgvNPFVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIEN 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1678729579 930 VQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTVILHFQIS 974
Cdd:cd21298 71 CNYAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2152-2806 |
2.18e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 70.55 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2152 TLRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDkqkqlaaahakaiakaekeaqelKLMM 2231
Cdd:pfam07111 52 SLELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELD-----------------------ALAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2232 KEEVNRRE-----IAAVDAEKQKQNI----QLELHELKNLSEQQIKDKGQLVDEALQSRTKIEEEIyliriqlettvkQK 2302
Cdd:pfam07111 109 AEKAGQAEaeglrAALAGAEMVRKNLeegsQRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGL------------EK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2303 STAESELKqlreRAAEAERLrKVAQEEAEKLHKQvIEETQKKRIAEKELqhkseaekeaakqkqkalddLENLKKQ-AEE 2381
Cdd:pfam07111 177 SLNSLETK----RAGEAKQL-AEAQKEAELLRKQ-LSKTQEELEAQVTL--------------------VESLRKYvGEQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2382 AERQVKQAEVEKERQIKVAHVAAQKSAAAELQSkhssfvekTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAR--E 2459
Cdd:pfam07111 231 VPPEVHSQTWELERQELLDTMQHLQEDRADLQA--------TVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEfpK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2460 EAEKELEKWRQKANeALRLRLQAEEEAHKKSLAQedaeKQKEEAEREAKKRAKAEESALKQKDMAEK--ELERQRKVADS 2537
Cdd:pfam07111 303 KCRSLLNRWREKVF-ALMVQLKAQDLEHRDSVKQ----LRGQVAELQEQVTSQSQEQAILQRALQDKaaEVEVERMSAKG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2538 TAQQKLTAEQELIRLRADFDNAEQQRSL-----------LEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKS 2606
Cdd:pfam07111 378 LQMELSRAQEARRRQQQQTASAEEQLKFvvnamsstqiwLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2607 KAE--KETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQvAEEEAARQRAEAERILKEKLAAISEATHLKT 2684
Cdd:pfam07111 458 LAQlrQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQQLEQELQRA 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2685 EAEIALKEKEAENER--LRRAAEDEAYQRKALEDEANQHKKEIEEKIVQL------------KKSSDAEMERQKAMVDDT 2750
Cdd:pfam07111 537 QESLASVGQQLEVARqgQQESTEEAASLRQELTQQQEIYGQALQEKVAEVetrlreqlsdtkRRLNEARREQAKAVVSLR 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 2751 LKQRRVVEE-----EIRILKLNFEKASSGKLDLEL-ELNKLKNIAEET-QQSKLRAEEEAEKL 2806
Cdd:pfam07111 617 QIQHRATQEkernqELRRLQDEARKEEGQRLARRVqELERDKNLMLATlQQEGLLSRYKQQRL 679
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
863-965 |
2.46e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 63.98 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 863 ERDRvQKKTFTKWVNKHLIKRAesqhhVTDLYEDLRDGHNLISLLEVLSGDT--------LPREKGRMRFHKLQNVQIAL 934
Cdd:cd21300 4 EGER-EARVFTLWLNSLDVEPA-----VNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAV 77
|
90 100 110
....*....|....*....|....*....|.
gi 1678729579 935 DFLRHRQVKLVNIRNDDIADGNPKLTLGLIW 965
Cdd:cd21300 78 ELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4786-4824 |
2.82e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.80 E-value: 2.82e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1678729579 4786 LLEAQASTGYVIDPIKNLKLTVNEAVRMGIVGPEFKDKL 4824
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2299-2687 |
2.92e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 70.76 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2299 VKQKSTAESEL-KQLRERAAEAERLRKVAQEEAEklhkqvIEEtqkkriAEKELQHKSEAEKE----------AAKQKQK 2367
Cdd:PRK04863 285 LEEALELRRELyTSRRQLAAEQYRLVEMARELAE------LNE------AESDLEQDYQAASDhlnlvqtalrQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2368 ALDDLENLKKQAEEaerqvkQAEVEKERQIKVAHVAAQKSAAAE----LQSKHSSFVEKTSKLEESLKQEHGAVlQLQQE 2443
Cdd:PRK04863 353 YQADLEELEERLEE------QNEVVEEADEQQEENEARAEAAEEevdeLKSQLADYQQALDVQQTRAIQYQQAV-QALER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2444 AAHLkkQQEDAINArEEAEKELEKWRQKANEALRLRLQAEeeaHKKSLAQeDAEKQKEEAEREAKK------RAKAEESA 2517
Cdd:PRK04863 426 AKQL--CGLPDLTA-DNAEDWLEEFQAKEQEATEELLSLE---QKLSVAQ-AAHSQFEQAYQLVRKiagevsRSEAWDVA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2518 LKqkdmAEKELERQRKVAD---------STAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEviaAQQQRKQLE 2588
Cdd:PRK04863 499 RE----LLRRLREQRHLAEqlqqlrmrlSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE---LEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2589 DELAKV---RSEM-DILIQLKSKAEKetmsNTEKSKQLLEAEA--TKMRDVAEEA--------GKLRAIAEEAKHQRQVA 2654
Cdd:PRK04863 572 ESVSEArerRMALrQQLEQLQARIQR----LAARAPAWLAAQDalARLREQSGEEfedsqdvtEYMQQLLERERELTVER 647
|
410 420 430
....*....|....*....|....*....|...
gi 1678729579 2655 EEEAARQRAEAERILKEKLAAISEATHLKTEAE 2687
Cdd:PRK04863 648 DELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2183-2805 |
3.29e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 70.64 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2183 KAAKKLKAEEQKKMAEMQAELdkqkqlaaahakaiakaekeaqELKLMMKEEVNRREIAAVDAEK--QKQNIQLELHELK 2260
Cdd:pfam12128 268 KSDETLIASRQEERQETSAEL----------------------NQLLRTLDDQWKEKRDELNGELsaADAAVAKDRSELE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2261 NLSEQqikdKGQLVDEALQSRTKIEEEIYLIRIQLE---------TTVKQKSTAESE-LKQLR--ERAAEAERL--RKVA 2326
Cdd:pfam12128 326 ALEDQ----HGAFLDADIETAAADQEQLPSWQSELEnleerlkalTGKHQDVTAKYNrRRSKIkeQNNRDIAGIkdKLAK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2327 QEEAEKLHKQVIEETQKKRiaEKELQHKSEAEKEAAKQKQKALDD-LENLKKQAEEA--------ERQVKQAEVEKERQI 2397
Cdd:pfam12128 402 IREARDRQLAVAEDDLQAL--ESELREQLEAGKLEFNEEEYRLKSrLGELKLRLNQAtatpelllQLENFDERIERAREE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2398 KVAHVAAQKSAAAELqskhSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREE-AEKELEKWRQKANE-- 2474
Cdd:pfam12128 480 QEAANAEVERLQSEL----RQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHfLRKEAPDWEQSIGKvi 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2475 --------------------------ALRLRLQAEEeaHKKSLAQEDAEKQK----EEAEREAKKRAKAEESALKQkdmA 2524
Cdd:pfam12128 556 spellhrtdldpevwdgsvggelnlyGVKLDLKRID--VPEWAASEEELRERldkaEEALQSAREKQAAAEEQLVQ---A 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2525 EKELERQRKVADSTAQQKLTAEQELIRLradFDNAEQQRSLLEDELYRLKNEviaAQQQRKQLEDELAKVRSEmdilIQL 2604
Cdd:pfam12128 631 NGELEKASREETFARTALKNARLDLRRL---FDEKQSEKDKKNKALAERKDS---ANERLNSLEAQLKQLDKK----HQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2605 KSKAEKETMS--NTEKSKQLLEAEATkmRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERilkeklaAISEATHL 2682
Cdd:pfam12128 701 WLEEQKEQKReaRTEKQAYWQVVEGA--LDAQLALLKAAIAARRSGAKAELKALETWYKRDLASL-------GVDPDVIA 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2683 KTEAEIALKEKEAENERLRRAA---------EDEAYQRKALEDEANQHKKEIEEKIVQL-KKSSDAEMERQKAMV--DDT 2750
Cdd:pfam12128 772 KLKREIRTLERKIERIAVRRQEvlryfdwyqETWLQRRPRLATQLSNIERAISELQQQLaRLIADTKLRRAKLEMerKAS 851
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2751 LKQRRVVEEEIRILKLNFEKASSGKLD-----LELELNKLKNIAEETQQSKLRAEEEAEK 2805
Cdd:pfam12128 852 EKQQVRLSENLRGLRCEMSKLATLKEDanseqAQGSIGERLAQLEDLKLKRDYLSESVKK 911
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
986-1083 |
3.53e-11 |
|
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: 62.79 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQ-RMTGDYQNircdNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSN-LENLEQAFNVAERDLGVTRLL 1063
Cdd:cd21230 1 TPKQRLLGWIQnKIPQLPIT----NFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLI 76
|
90 100
....*....|....*....|
gi 1678729579 1064 DPEDVDVQHPDEKSIITYVS 1083
Cdd:cd21230 77 TPEEIINPNVDEMSVMTYLS 96
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2698-3432 |
5.31e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.71 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2698 ERLRRAAEDEAYQRKALEDEANQHKKE------IEEKIVQLKKSSDaemERQKAMVDDTLkQRRVVEEEIRILKLNFEKA 2771
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIerldliIDEKRQQLERLRR---EREKAERYQAL-LKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2772 SSGKLDLELELNKLK----NIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKK----ITAAEEEAARQRKIAQD 2843
Cdd:TIGR02169 236 ERQKEAIERQLASLEeeleKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkigeLEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2844 ELERLkkkaeEARKQKDEADVEAevqiVAAQQAALKCSTAEHQVQsvLAQQKEDsimHKKLKQEYEKAKKLAKEAEAAKE 2923
Cdd:TIGR02169 316 ELEDA-----EERLAKLEAEIDK----LLAEIEELEREIEEERKR--RDKLTEE---YAELKEELEDLRAELEEVDKEFA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2924 KAEREAALLRQQAEEA--ERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQAEGAAlkQKQQADAEMAKHKKLAEQ 3001
Cdd:TIGR02169 382 ETRDELKDYREKLEKLkrEINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE--EKEDKALEIKKQEWKLEQ 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3002 TLKQKFQVEQELTKVKLKLDDtdkqkslLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELlklklriedenqrllk 3081
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDR-------VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVL---------------- 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3082 kdKDNSQKFLAEEAENMKrlAEDAARLSVESQEAARLRQIA-EDDLIQQRALadKMLKE------------KMQAIQESS 3148
Cdd:TIGR02169 517 --KASIQGVHGTVAQLGS--VGERYATAIEVAAGNRLNNVVvEDDAVAKEAI--ELLKRrkagratflplnKMRDERRDL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3149 RLKAEAEMLQRQKDLAQ-----EQAQKLLEDKQLMQRRLEE-------------ETEEYQKSLE----AERRRQLEIVAE 3206
Cdd:TIGR02169 591 SILSEDGVIGFAVDLVEfdpkyEPAFKYVFGDTLVVEDIEAarrlmgkyrmvtlEGELFEKSGAmtggSRAPRGGILFSR 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3207 AEKLKLQvsQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKE--KMTVVEKLEFERLNtskeagdlrdaiADLEKDK 3284
Cdd:TIGR02169 671 SEPAELQ--RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDasRKIGEIEKEIEQLE------------QEEEKLK 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3285 ARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQQtfltEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQ 3364
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKSELKELEARIEEL----EEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEA 812
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678729579 3365 QMEEEKKKLhatmhEALSKQKE-AEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQLEEAQKE 3432
Cdd:TIGR02169 813 RLREIEQKL-----NRLTLEKEyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2307-2720 |
7.24e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.60 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2307 SELKQLRERAAEAER-------LRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSE--AEKEAAKQKQKALD----DLE 2373
Cdd:COG3096 278 NERRELSERALELRRelfgarrQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlNLVQTALRQQEKIEryqeDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2374 NLKKQAEEAERQVKQAEVEKERQIKVAHVAAQ-----KSAAAELQskhssfvektskleESLKQEHGAVLQLQQEAAHLK 2448
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEevdslKSQLADYQ--------------QALDVQQTRAIQYQQAVQALE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2449 KQQE----DAINArEEAEKELEKWRQKANEALRLRLQAEeeaHKKSLAqEDAEKQKEEAEREAKKRAkaeesalkqkdma 2524
Cdd:COG3096 424 KARAlcglPDLTP-ENAEDYLAAFRAKEQQATEEVLELE---QKLSVA-DAARRQFEKAYELVCKIA------------- 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2525 eKELERQRkvADSTAQQKLtaeQELIRLRADFDNAEQQRSLLeDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQL 2604
Cdd:COG3096 486 -GEVERSQ--AWQTARELL---RRYRSQQALAQRLQQLRAQL-AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEEL 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2605 KSKAEketmsntekskQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQvaeeeAARQRAEAERILKEKLAAISEATH--L 2682
Cdd:COG3096 559 LAELE-----------AQLEELEEQAAEAVEQRSELRQQLEQLRARIK-----ELAARAPAWLAAQDALERLREQSGeaL 622
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1678729579 2683 KTEAEI-ALKEKEAENERLRRAAEDEAYQRK-ALEDEANQ 2720
Cdd:COG3096 623 ADSQEVtAAMQQLLEREREATVERDELAARKqALESQIER 662
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3885-3922 |
7.42e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.65 E-value: 7.42e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1678729579 3885 LEAQAGTGYVVDPIHDQKYTVDEAVKAGVVGPELHEKL 3922
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1349-1538 |
7.88e-11 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 65.16 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1349 LRYVKDLLAWVEENQLRIDGAEWGSDLPAVESQLGSHRGLHQTVEDFRAKIERARADESQL---SSVSKGSYKEYMGKLD 1425
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1426 LQYGKLLNSSKSRLRNLD---SLHGFISAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDL 1502
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1678729579 1503 QAMGERLVRDGHPGK-KTVESFTAALQTQWSWILQLC 1538
Cdd:cd00176 166 NELAEELLEEGHPDAdEEIEEKLEELNERWEELLELA 202
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2793-3434 |
8.97e-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: 8.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2793 QQSKLRAEEEAEKLRKLALeeekrrreaeekvkkitaaEEEAARQRkIAQDELERLKKKAEEARKQKDEADVEAEVQIVA 2872
Cdd:pfam02463 140 QGGKIEIIAMMKPERRLEI-------------------EEEAAGSR-LKRKKKEALKKLIEETENLAELIIDLEELKLQE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2873 AQQAALKCSTAEHQVQSVLAQQ-KEDSIMHKKLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAA 2951
Cdd:pfam02463 200 LKLKEQAKKALEYYQLKEKLELeEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2952 IQAKAQEDAERLRKEAEFEAAKRAQAEGAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQ------ELTKVKLKLDDTDK 3025
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEElekelkELEIKREAEEEEEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3026 QKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLLKKDKDNSQKFLAEEA--ENMKRLAE 3103
Cdd:pfam02463 360 ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELeiLEEEEESI 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3104 DAARLSVESQEAARLRQIAEDDLIQQralADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLE 3183
Cdd:pfam02463 440 ELKQGKLTEEKEELEKQELKLLKDEL---ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALI 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3184 EETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFER 3263
Cdd:pfam02463 517 KDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3264 LNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQQTFLTEREMLLKKEKLIEeekkkles 3343
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASL-------- 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3344 qfEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKL 3423
Cdd:pfam02463 669 --SELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID 746
|
650
....*....|.
gi 1678729579 3424 QQLEEAQKEQH 3434
Cdd:pfam02463 747 EEEEEEEKSRL 757
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2172-2672 |
9.37e-11 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 68.50 E-value: 9.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2172 TETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKqkqlaaahakaiakaekeaqelklmmkeevnRREIAAVDAEKQKQN 2251
Cdd:NF033838 47 TVTSSGNESQKEHAKEVESHLEKILSEIQKSLDK-------------------------------RKHTQNVALNKKLSD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2252 IQLE-LHELKNLSEQQikdkgqlvDEALQSRTKIEEEIYLIRIQLETTVKQKSTAESELKqlrerAAEAERLRKVAQEEA 2330
Cdd:NF033838 96 IKTEyLYELNVLKEKS--------EAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKK-----VEEAEKKAKDQKEED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2331 EKLHKQVIEETQKKRIAEKELQHKsEAEKEAAKQKQKALDDLENLKKQaeEAERQVKQAEVEKERQIKVAHVAAQKSAAA 2410
Cdd:NF033838 163 RRNYPTNTYKTLELEIAESDVEVK-KAELELVKEEAKEPRDEEKIKQA--KAKVESKKAEATRLEKIKTDREKAEEEAKR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2411 ELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAekelekwrqkanealrlrlqAEEEAHKKS 2490
Cdd:NF033838 240 RADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSV--------------------GEETLPSPS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2491 LAQE----DAEKQKEEAEREAKKRAKAEESALKQKDMAEKELErqrkVADSTAQQKlTAEQELIRlradfDNAEQQRSll 2566
Cdd:NF033838 300 LKPEkkvaEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKTLELE----IAESDVKVK-EAELELVK-----EEAKEPRN-- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2567 EDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDiliQLKSKAEKETMSNTEKSKQLLEAEATKmrdVAEEAGKLRAIAEE 2646
Cdd:NF033838 368 EEKIKQAKAKVESKKAEATRLEKIKTDRKKAEE---EAKRKAAEEDKVKEKPAEQPQPAPAPQ---PEKPAPKPEKPAEQ 441
|
490 500
....*....|....*....|....*....
gi 1678729579 2647 AKHQR---QVAEEEAARQRAEAERILKEK 2672
Cdd:NF033838 442 PKAEKpadQQAEEDYARRSEEEYNRLTQQ 470
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3032-3432 |
1.02e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3032 DELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKL--KLRIEDENQRLLKKDKDNSQKfLAEEAENMKRL-AEDAARL 3108
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAE-LAELPERLEELeERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3109 SVESQEAARLRQIAEddliQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEE 3188
Cdd:COG4717 160 ELEEELEELEAELAE----LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3189 YQKSLEAERRRQLEIVAE----------------------AEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETE 3246
Cdd:COG4717 236 LEAAALEERLKEARLLLLiaaallallglggsllsliltiAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3247 IATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQnkskemadaQQKQIEHEKTLLQQTFLTEREM 3326
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ---------LEELEQEIAALLAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3327 LLkkeklieeekkklesQFEEEAKKSKALKDEQERQKQQMEEEKKKLHATM-----HEALSKQKEAEKEMLSKQKEMQEL 3401
Cdd:COG4717 387 LR---------------AALEQAEEYQELKEELEELEEQLEELLGELEELLealdeEELEEELEELEEELEELEEELEEL 451
|
410 420 430
....*....|....*....|....*....|...
gi 1678729579 3402 --EKKRLEQEIILADENQKLREKLQQLEEAQKE 3432
Cdd:COG4717 452 reELAELEAELEQLEEDGELAELLQELEELKAE 484
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3960-3998 |
1.15e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.26 E-value: 1.15e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1678729579 3960 LLDAQMTTGGIIDPVKSHHIPHDVACKRNYFDDEMKQIL 3998
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4625-4662 |
1.23e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.26 E-value: 1.23e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1678729579 4625 LEAQTATGGIIDPEFQFHLPADIAMQRGYINKETNERL 4662
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2294-2752 |
1.66e-10 |
|
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: 67.92 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2294 QLETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQK---KRIAEKELQHKSEAEKEAAKQKQKALD 2370
Cdd:pfam10174 367 QLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQlagLKERVKSLQTDSSNTDTALTTLEEALS 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2371 D----LENLKKQaEEAERQVKQAEVE------KERQIKV----AHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGA 2436
Cdd:pfam10174 447 EkeriIERLKEQ-REREDRERLEELEslkkenKDLKEKVsalqPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIA 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2437 VLQLQQEAAHLKKQQEDAINAREEAekelekwRQKANEALRLRLQAEEEAHKKslaqEDAEKQKEEAER--EAKKRAKAE 2514
Cdd:pfam10174 526 VEQKKEECSKLENQLKKAHNAEEAV-------RTNPEINDRIRLLEQEVARYK----EESGKAQAEVERllGILREVENE 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2515 ESaLKQKDMAEKELERQRKVADST--AQQKLTAEQElirlradfdnaEQQRSLLEDELYRLKNEVIAAQQQRKQLED--- 2589
Cdd:pfam10174 595 KN-DKDKKIAELESLTLRQMKEQNkkVANIKHGQQE-----------MKKKGAQLLEEARRREDNLADNSQQLQLEElmg 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2590 ELAKVRSEMDiliqlkskAEKETMSNTEKSKQLLEAEATKMRdvaeeagklraiaeeakHQRQVAEEEAARQRAEAeril 2669
Cdd:pfam10174 663 ALEKTRQELD--------ATKARLSSTQQSLAEKDGHLTNLR-----------------AERRKQLEEILEMKQEA---- 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2670 keKLAAISEathlkTEAEIALKEKEAENerlrraaedeayqrkaledeanqhKKEIEEKIVQLKKSSDAEMERQKAMVDD 2749
Cdd:pfam10174 714 --LLAAISE-----KDANIALLELSSSK------------------------KKKTQEEVMALKREKDRLVHQLKQQTQN 762
|
...
gi 1678729579 2750 TLK 2752
Cdd:pfam10174 763 RMK 765
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2177-2808 |
2.12e-10 |
|
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: 67.44 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2177 RLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELKLMMKEEVNR------------------R 2238
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdlikennatrhlcnllK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2239 EIAAVDAEK------QKQNIQLELHELKNLSEQQIKDKGQLVDEALQSRT----KIEEEIYLIRIQLETTVKQKSTAESE 2308
Cdd:pfam05483 162 ETCARSAEKtkkyeyEREETRQVYMDLNNNIEKMILAFEELRVQAENARLemhfKLKEDHEKIQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2309 LKQLRERAAEAERLRK---VAQEEAEKLHKQVIEETQKKRIAEKEL---QHKSEAEKEAAKQK-QKALDDLENLKKQAEE 2381
Cdd:pfam05483 242 VSLLLIQITEKENKMKdltFLLEESRDKANQLEEKTKLQDENLKELiekKDHLTKELEDIKMSlQRSMSTQKALEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2382 AERQVKQAEVEKERQIKVAHVA--AQKSAAAELQSKHSSFVE----KTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAI 2455
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAkaAHSFVVTEFEATTCSLEEllrtEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2456 NAREE--------AEKELEKWRQKANEALRLRLQAEEEAHKKSLaqEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKE 2527
Cdd:pfam05483 402 NKEVEleelkkilAEDEKLLDEKKQFEKIAEELKGKEQELIFLL--QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2528 LERQR-KVADSTAQ--------QKLTAEQ-----ELIRLRADFDNAEQQRSlledelyRLKNEVIAAQQQRKQLEDELAK 2593
Cdd:pfam05483 480 LEKEKlKNIELTAHcdklllenKELTQEAsdmtlELKKHQEDIINCKKQEE-------RMLKQIENLEEKEMNLRDELES 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2594 VRSEmdiLIQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEE-----EAARQRAEAE-- 2666
Cdd:pfam05483 553 VREE---FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEElhqenKALKKKGSAEnk 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2667 -----RILKEKLAAISEATHLKTEAEIALKEKEAENERL-RRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEM 2740
Cdd:pfam05483 630 qlnayEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKIsEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALM 709
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678729579 2741 ERQKAMVDDTLKQRrvvEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRK 2808
Cdd:pfam05483 710 EKHKHQYDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKM 774
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2997-3432 |
2.18e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2997 KLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEeelfkvkvQMEELLKLKLRIEDEN 3076
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP--------LYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3077 QRLlkkdkdnsqKFLAEEAENMKRLAEDAARLSVESQEAarlrqiaeddliqQRALADKMLKEKMQAIQESSRLKAEAEM 3156
Cdd:COG4717 146 ERL---------EELEERLEELRELEEELEELEAELAEL-------------QEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3157 LQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAE----------------------AEKLKLQV 3214
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3215 SQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEEL 3294
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3295 QnkskemadaQQKQIEHEKTLLQQTFLTEREMLLKKEKLIeeekkkleSQFEEEAKKSKALKDEQERQKQQMEE-----E 3369
Cdd:COG4717 364 Q---------LEELEQEIAALLAEAGVEDEEELRAALEQA--------EEYQELKEELEELEEQLEELLGELEEllealD 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678729579 3370 KKKLHATMHEALSKQKEAEKEMLSKQKEMQEL--EKKRLEQEIILADENQKLREKLQQLEEAQKE 3432
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEELREELAELeaELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2969-3212 |
2.22e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.33 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2969 FEAAKRAQAEGAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQR 3048
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3049 GQVEEELFKVKVQMEELLKLKLRIEDENQRLLKKDKDNSQKFlAEEAENMKRLAE-DAARLSVESQEAARLRQIaEDDLI 3127
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDA-VRRLQYLKYLAPaRREQAEELRADLAELAAL-RAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3128 QQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEA 3207
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 1678729579 3208 EKLKL 3212
Cdd:COG4942 251 LKGKL 255
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2765-3320 |
2.26e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2765 KLNFEKASSGKLDLELE-LNKLKNIAEET-QQSKLRAEEEAEKLRKLAleeekrrrEAEEKVKKITAAEEEAARQRKIAQ 2842
Cdd:PRK02224 207 RLNGLESELAELDEEIErYEEQREQARETrDEADEVLEEHEERREELE--------TLEAEIEDLRETIAETEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2843 DELERLKKKAEEARKQKDEADVEAEV-----QIVAAQQAALkcSTAEHQVQSVLAQQKEDSIMHKKLKQEYEKAKKLAKE 2917
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLddadaEAVEARREEL--EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2918 AEAAkekaereaalLRQQAEEAErqkAAAEQEAAIQAKAQEDAERLRKEAEfEAAKR-----AQAEGAALKQKQQADAEM 2992
Cdd:PRK02224 357 RAEE----------LREEAAELE---SELEEAREAVEDRREEIEELEEEIE-ELRERfgdapVDLGNAEDFLEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2993 AKHKKLAE-----QTLKQKFQVEQEL---------------TKVKLKLDDTDKQKSLLDDELQRLKDEVDDavkqrgqVE 3052
Cdd:PRK02224 423 ELREREAEleatlRTARERVEEAEALleagkcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEE-------VE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3053 EELfkvkVQMEELLKLKLRIEDenqrlLKKDKDNSQKFLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRAL 3132
Cdd:PRK02224 496 ERL----ERAEDLVEAEDRIER-----LEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3133 ADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRR--LEEETEEYQKSLEA--ERRRQLEIvaeae 3208
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKReaLAELNDERRERLAEkrERKRELEA----- 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3209 klKLQVSQLSEAQTKaEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKlEFERLNTSKEAgdlRDAIADLEKDKARLK 3288
Cdd:PRK02224 642 --EFDEARIEEARED-KERAEEYLEQVEEKLDELREERDDLQAEIGAVEN-ELEELEELRER---REALENRVEALEALY 714
|
570 580 590
....*....|....*....|....*....|...
gi 1678729579 3289 KEAEELQNKSKEM-ADAQQKQIEHEKTLLQQTF 3320
Cdd:PRK02224 715 DEAEELESMYGDLrAELRQRNVETLERMLNETF 747
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3633-3670 |
2.52e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.11 E-value: 2.52e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1678729579 3633 VLEAQLATGGIIDPINSHRVPNETAYKQGQYDVEMNKI 3670
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2996-3432 |
2.59e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2996 KKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSllddELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKlRIEDE 3075
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3076 NQRLLKKDKDNSQKFLAEEAENMKRlaedaARLSVESqeaarlrqiAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAE 3155
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELEK-----AKEEIEE---------EISKITARIGELKKEIKELKKAIEELKKAKGKCP 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3156 MLQRQkdLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRR--QLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKK 3233
Cdd:PRK03918 440 VCGRE--LTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKElrELEKVLKKESELIKLKELAEQLKELEEKLKKYNL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3234 QADKIAARLHET---EIATKEKMTVVEKLEFERLNT-SKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMADAQQKQI 3309
Cdd:PRK03918 518 EELEKKAEEYEKlkeKLIKLKGEIKSLKKELEKLEElKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKEL 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3310 E--HEKTLLQQTflTEREMLLKKEKLIEEEKKKLESqFEEEAKKSKALkdeqERQKQQMEEEKKKLHATMHEALSKQK-E 3386
Cdd:PRK03918 598 EpfYNEYLELKD--AEKELEREEKELKKLEEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEYEELREEYlE 670
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1678729579 3387 AEKEMLSKQKEMQELEKKRLEQEIILadenQKLREKLQQLEEAQKE 3432
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTL----EKLKEELEEREKAKKE 712
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2244-2808 |
2.61e-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: 67.35 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2244 DAEKQKQNIQLELHELknlsEQQIKDkgqLVDEALQSRTKIEE---EIYLIRIQLETTVKQKSTAESELKQLRERAaeae 2320
Cdd:TIGR04523 65 KDEEKINNSNNKIKIL----EQQIKD---LNDKLKKNKDKINKlnsDLSKINSEIKNDKEQKNKLEVELNKLEKQK---- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2321 rlrkvaqEEAEKLHKQVIEETQKKriaEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKER-QIKV 2399
Cdd:TIGR04523 134 -------KENKKNIDKFLTEIKKK---EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKlELLL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2400 AHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLR 2479
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2480 LQAEEEAHKKSLAQEDAEKQKEEaerEAKKRAKAE-ESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRAdfDN 2558
Cdd:TIGR04523 284 KELEKQLNQLKSEISDLNNQKEQ---DWNKELKSElKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES--EN 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2559 AEQQRSLLE--DELYRLKNEVIAAQQQRKQLEDELAKVRSEmdILIQLKSKAEKET-MSNTEKSKQLLEAEATKMRDVAE 2635
Cdd:TIGR04523 359 SEKQRELEEkqNEIEKLKKENQSYKQEIKNLESQINDLESK--IQNQEKLNQQKDEqIKKLQQEKELLEKEIERLKETII 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2636 EAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLrraaedeayqrkale 2715
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL--------------- 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2716 deaNQHKKEIEEKIVQLKKSSDAEMERQKAM-VDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQ 2794
Cdd:TIGR04523 502 ---NEEKKELEEKVKDLTKKISSLKEKIEKLeSEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQK 578
|
570
....*....|....
gi 1678729579 2795 SKLRAEEEAEKLRK 2808
Cdd:TIGR04523 579 SLKKKQEEKQELID 592
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
986-1086 |
2.76e-10 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 60.44 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTGDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERDLGVTRLLDP 1065
Cdd:cd21196 3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
|
90 100
....*....|....*....|.
gi 1678729579 1066 EDVdVQHPDEKSIITYVSSLY 1086
Cdd:cd21196 83 QAV-VAGSDPLGLIAYLSHFH 102
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
869-968 |
3.10e-10 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 60.67 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 869 KKTFTKWVNKHLIKRAESQHHVT------DLYEDLRDGHNLISLLEVLSGDTLPREKGRMR-----FHKLQNVQIALDFL 937
Cdd:cd21217 3 KEAFVEHINSLLADDPDLKHLLPidpdgdDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1678729579 938 RHRQVKLVNIRNDDIADGNPKLTLGLIWTVI 968
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2176-2507 |
3.69e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.02 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2176 RRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELKlmMKEEVNRREIAAVdaEKQKQNIQLE 2255
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE--QEEEKLKERLEEL--EEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2256 LHELKNLSEQQIKDKGQLVDEALQSRTKIEE-EIYLIRIQLETTVKQKSTAESELKQLRERAAEAER-------LRKVAQ 2327
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrltlEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2328 EEAEKLHKQVIE-ETQKKRIAEK--ELQHKSEAEKEAAKQKQKALDDLE----NLKKQAEEAERQVKQAEvEKERQIKvA 2400
Cdd:TIGR02169 833 KEIQELQEQRIDlKEQIKSIEKEieNLNGKKEELEEELEELEAALRDLEsrlgDLKKERDELEAQLRELE-RKIEELE-A 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2401 HVAAQKSAAAELQSKHSSFVEKTSKLEESLKQ---EHGAVLQLQQEAAHLKKQQED-----AINAREEAEKELEKWRQKA 2472
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeIPEEELSLEDVQAELQRVEEEiralePVNMLAIQEYEEVLKRLDE 990
|
330 340 350
....*....|....*....|....*....|....*
gi 1678729579 2473 NEALRLRLQAEEEAHKKSLaqEDAEKQKEEAEREA 2507
Cdd:TIGR02169 991 LKEKRAKLEEERKAILERI--EEYEKKKREVFMEA 1023
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2747-3433 |
3.70e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2747 VDDTLKQRRVVEEEIR-ILKLN-FEKASSGKLDLELELNKLKniaeETQQSKLRAEEEAEKLRKlalEEEKRRREAEEKV 2824
Cdd:PRK03918 137 IDAILESDESREKVVRqILGLDdYENAYKNLGEVIKEIKRRI----ERLEKFIKRTENIEELIK---EKEKELEEVLREI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2825 KKITAAEEEAARQRKIAQDELERLKKKAEE-ARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQ-SVLAQQKEDSIMHK 2902
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEELKEEiEELEKELESLEGSKRKLEEKIRELEERIEELKKEiEELEEKVKELKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2903 KLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQkaaaeqeaaiQAKAQEDAERLRKEAEFEaaKRAQAEGAAL 2982
Cdd:PRK03918 290 EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER----------IKELEEKEERLEELKKKL--KELEKRLEEL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2983 KQKQQAdAEMAKHKKLAEQTLKQKFQVEqELTKVKLKLDDTDKQKSLLDDELQRLKDEvddavkqRGQVEEELFKVKVQM 3062
Cdd:PRK03918 358 EERHEL-YEEAKAKKEELERLKKRLTGL-TPEKLEKELEELEKAKEEIEEEISKITAR-------IGELKKEIKELKKAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3063 EELLKLKLRIEDENQRLLKKDKDNsqkFLAEEAENMKRLAEDAARLsvesqeAARLRQIaeddliqqralaDKMLKEKMQ 3142
Cdd:PRK03918 429 EELKKAKGKCPVCGRELTEEHRKE---LLEEYTAELKRIEKELKEI------EEKERKL------------RKELRELEK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3143 AIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDkqlmqrrLEEETEEYQKSLEaerrRQLEIVAEAEKLKLQVSQLSEAQT 3222
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNLEE-------LEKKAEEYEKLKE----KLIKLKGEIKSLKKELEKLEELKK 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3223 KAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMA 3302
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELA 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3303 DAQQKQIEHEKTL--LQQTFLTERemllkkeklieeekkklesqFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMhEA 3380
Cdd:PRK03918 637 ETEKRLEELRKELeeLEKKYSEEE--------------------YEELREEYLELSRELAGLRAELEELEKRREEIK-KT 695
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 3381 LSKQKEAEKEMLSKQKEMQELEKKRleqeiilaDENQKLREKLQQLEEAQKEQ 3433
Cdd:PRK03918 696 LEKLKEELEEREKAKKELEKLEKAL--------ERVEELREKVKKYKALLKER 740
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2343-2545 |
3.88e-10 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 66.05 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2343 KKRIAE-KELQHKSEAEKEAAKQKQKAlddlenlkkqaeEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQskhssfve 2421
Cdd:COG2268 191 RRKIAEiIRDARIAEAEAERETEIAIA------------QANREAEEAELEQEREIETARIAEAEAELAKKK-------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2422 ktskleeslkqehgAVLQLQQEAAhlkkqqedainaREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKE 2501
Cdd:COG2268 251 --------------AEERREAETA------------RAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEA 304
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1678729579 2502 EAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTA 2545
Cdd:COG2268 305 ELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4293-4329 |
6.01e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 57.34 E-value: 6.01e-10
10 20 30
....*....|....*....|....*....|....*..
gi 1678729579 4293 EAQMVSGGIIDPVNSHRVPIDVAYQKNIFSKEIAKTL 4329
Cdd:pfam00681 3 EAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1906-2794 |
6.02e-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: 66.22 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1906 QKMDHAYMLSSvYLEKLKTVEMViRNTQGAEgvLKQYEDCLREVHTVPGDVKEVetyRTKLKKMRGEAEGEQPVFDSLEE 1985
Cdd:TIGR00606 173 QKFDEIFSATR-YIKALETLRQV-RQTQGQK--VQEHQMELKYLKQYKEKACEI---RDQITSKEAQLESSREIVKSYEN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1986 ELKKAtvvsdkmsrvhSERDVELDHYRQHLSGLQDRWKAvfaqMDIRQRELEQLGRQLGYYHESydwlIHWITDakerqE 2065
Cdd:TIGR00606 246 ELDPL-----------KNRLKEIEHNLSKIMKLDNEIKA----LKSRKKQMEKDNSELELKMEK----VFQGTD-----E 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2066 KIQAVSITDSKTLKEQLSQEKKLLEEIENNKDNVDECQKYAKAYINSIKDYELQLVAYNAQADPLASPLKKTKLDSASDN 2145
Cdd:TIGR00606 302 QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDG 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2146 IiqeyvtLRTRYSELmtltsQYIKFITETQRRLEDEEKAAKKLKAEEQKKMAEmqaeldKQKQLAAAHAKAIAKAEKEAQ 2225
Cdd:TIGR00606 382 F------ERGPFSER-----QIKNFHTLVIERQEDEAKTAAQLCADLQSKERL------KQEQADEIRDEKKGLGRTIEL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2226 ELKLMMKEEVNRREIaavdaEKQKQNIQLELHELKNLSEQQIKDKGQL--VDEALQSRTKIEEEIYLIRIQLETtvkqks 2303
Cdd:TIGR00606 445 KKEILEKKQEELKFV-----IKELQQLEGSSDRILELDQELRKAERELskAEKNSLTETLKKEVKSLQNEKADL------ 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2304 taeseLKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAA-----KQKQKALDDLENLKKQ 2378
Cdd:TIGR00606 514 -----DRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGyfpnkKQLEDWLHSKSKEINQ 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2379 AEEAERQVkQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEhgavlQLQQEAAHLKKQQ---EDAI 2455
Cdd:TIGR00606 589 TRDRLAKL-NKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLE-----RLKEEIEKSSKQRamlAGAT 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2456 NAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQED----AEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQ 2531
Cdd:TIGR00606 663 AVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSklrlAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2532 RKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLK---NEVIAAQQQRKQLEDELAKVR--------SEMDI 2600
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvclTDVTIMERFQMELKDVERKIAqqaaklqgSDLDR 822
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2601 LIQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERI------LKEKLA 2674
Cdd:TIGR00606 823 TVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLvelsteVQSLIR 902
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2675 AISEATHLKTEAEIALKEKEAENERL-------RRAAEDEAYQRKALEDEANQHKKEIEEKIVQ----LKKSSDAEMERQ 2743
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELissketsNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgkddYLKQKETELNTV 982
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678729579 2744 KAMVDDTLKQRRVVEEEIRILKLNF------EKASSGKLDLELELNKLKNIAEETQQ 2794
Cdd:TIGR00606 983 NAQLEECEKHQEKINEDMRLMRQDIdtqkiqERWLQDNLTLRKRENELKEVEEELKQ 1039
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2344-2720 |
6.09e-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: 65.80 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2344 KRIAEKELQHKSEAEKEAAKQKQKAlDDLENLKKQAEeAERQVKQAEVEKErqikvahvaAQKSaaaELQSKHSSFVEKT 2423
Cdd:NF033838 108 KEKSEAELTSKTKKELDAAFEQFKK-DTLEPGKKVAE-ATKKVEEAEKKAK---------DQKE---EDRRNYPTNTYKT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2424 SKLE--ESLKQEHGAVLQLQQEAAHlKKQQEDAINAreeAEKELEkwrQKANEALRLrlqaeeeahkkslaqEDAEKQKE 2501
Cdd:NF033838 174 LELEiaESDVEVKKAELELVKEEAK-EPRDEEKIKQ---AKAKVE---SKKAEATRL---------------EKIKTDRE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2502 EAEREAKKRAKAEESALKQKDMAEKELERQRKVAdstaqqKLTAEQELIRLRADFDNAEQQRSLLEDELY---RLKNEVI 2578
Cdd:NF033838 232 KAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRA------KRGVLGEPATPDKKENDAKSSDSSVGEETLpspSLKPEKK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2579 AAQQQRKQLE-DELAKVRSEMDiliqlkskaEKETMSNTEKSKQLLEAEAtkmrDVAEEAGKLRAIAEEAKHQRQvaEEE 2657
Cdd:NF033838 306 VAEAEKKVEEaKKKAKDQKEED---------RRNYPTNTYKTLELEIAES----DVKVKEAELELVKEEAKEPRN--EEK 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 2658 AARQRAEAErilkEKLAaisEATHLKteaEIALKEKEAENERLRRAAEDEayqrKALEDEANQ 2720
Cdd:NF033838 371 IKQAKAKVE----SKKA---EATRLE---KIKTDRKKAEEEAKRKAAEED----KVKEKPAEQ 419
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2539-3404 |
6.44e-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: 66.13 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2539 AQQKLTAEQE-LIRLRADFDNAEQQRSLLEDElYRLKNEVIAAQQQRKQLEDELAKVRSEMDiliQLKSKAEKETMSNTE 2617
Cdd:COG3096 297 ARRQLAEEQYrLVEMARELEELSARESDLEQD-YQAASDHLNLVQTALRQQEKIERYQEDLE---ELTERLEEQEEVVEE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2618 KSKQLLEAEATKMR---DVAEEAGKL----RAIaeEAKHQRQVAEEEAARQRAEAERILKekLAAISEATHLKTEAEIAL 2690
Cdd:COG3096 373 AAEQLAEAEARLEAaeeEVDSLKSQLadyqQAL--DVQQTRAIQYQQAVQALEKARALCG--LPDLTPENAEDYLAAFRA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2691 KEKEAENERLrraaedEAYQRKALEDEA-NQHkkeieEKIVQLKKSSDAEMERQKAmvDDTLKQrrvVEEEIRILKLNFE 2769
Cdd:COG3096 449 KEQQATEEVL------ELEQKLSVADAArRQF-----EKAYELVCKIAGEVERSQA--WQTARE---LLRRYRSQQALAQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2770 KASSgkldLELELNKLKNIAEETQqsklRAEEEAEKLRKLAleeekrrreaeekvKKITAAEEEAARQRKIAQDELERLK 2849
Cdd:COG3096 513 RLQQ----LRAQLAELEQRLRQQQ----NAERLLEEFCQRI--------------GQQLDAAEELEELLAELEAQLEELE 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2850 KKAEEARKQKdeADVEAEVQIVAAQQAAL-KCSTAEHQVQSVLAQQKEDSIMHKKLKQEYEKakklakeaeaakekaere 2928
Cdd:COG3096 571 EQAAEAVEQR--SELRQQLEQLRARIKELaARAPAWLAAQDALERLREQSGEALADSQEVTA------------------ 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2929 aalLRQQAEEAERQkaaaeqeaaiqAKAQEDAERLRKEAEFEAAKRAQAEGAAlkqkqqADAEMakhKKLAEQ----TLK 3004
Cdd:COG3096 631 ---AMQQLLERERE-----------ATVERDELAARKQALESQIERLSQPGGA------EDPRL---LALAERlggvLLS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3005 QKFQ---------------------VEQELTKVKLKLDDTDkqkSLLDDEL--QRLKDEVDDAVKQrgqVEEELFKVKVQ 3061
Cdd:COG3096 688 EIYDdvtledapyfsalygparhaiVVPDLSAVKEQLAGLE---DCPEDLYliEGDPDSFDDSVFD---AEELEDAVVVK 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3062 MEELlklKLRIE--DENQRLLKKDKDNSQKFLAEEAENmkrLAEDAARLSVESQEAARLRQIAEDDLIQQRALA-----D 3134
Cdd:COG3096 762 LSDR---QWRYSrfPEVPLFGRAAREKRLEELRAERDE---LAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAfapdpE 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3135 KMLKEKMQAIQESSRLKAEAE----MLQRQKDLAQEQAQ---------KLLEDKQLMQRrLEEETEEYQKSLEAERR--- 3198
Cdd:COG3096 836 AELAALRQRRSELERELAQHRaqeqQLRQQLDQLKEQLQllnkllpqaNLLADETLADR-LEELREELDAAQEAQAFiqq 914
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3199 -----RQLE-IVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADkiaarlheteiATKEKMTVVEKLEFErlntskEAGD 3272
Cdd:COG3096 915 hgkalAQLEpLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIF-----------ALSEVVQRRPHFSYE------DAVG 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3273 LRDAIADL-EKDKARLKkEAEELQNKSKEMADAQQKQIE---HEKTLLQQTFLTEREMLLkkeklieeekkklesQFEEE 3348
Cdd:COG3096 978 LLGENSDLnEKLRARLE-QAEEARREAREQLRQAQAQYSqynQVLASLKSSRDAKQQTLQ---------------ELEQE 1041
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3349 akkskaLKDEQERQKQQMEE----EKKKLHATMHEALSKQKEAEKEMLSKQKEMQELEKK 3404
Cdd:COG3096 1042 ------LEELGVQADAEAEErariRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKR 1095
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2239-2746 |
7.77e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.91 E-value: 7.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2239 EIAAVDAEKQKQnIQLELHELKN-----LSEQQIKDKGqLVDEALQSRTK---IEEEIYLI----RIQLETTVKQKSTAE 2306
Cdd:pfam15921 246 QLEALKSESQNK-IELLLQQHQDrieqlISEHEVEITG-LTEKASSARSQansIQSQLEIIqeqaRNQNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2307 SELKQLRERAAEAERLRKVAQEEAEK---LHKQVIEETQKKRIA--------EKELQ------HKSEAEKEAAKQKQKAL 2369
Cdd:pfam15921 324 STVSQLRSELREAKRMYEDKIEELEKqlvLANSELTEARTERDQfsqesgnlDDQLQklladlHKREKELSLEKEQNKRL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2370 DD--------LENLKKQAEEAERQVKQAEV-----------EKERQI-----------KVAHVAAQKSAAAE-------- 2411
Cdd:pfam15921 404 WDrdtgnsitIDHLRRELDDRNMEVQRLEAllkamksecqgQMERQMaaiqgknesleKVSSLTAQLESTKEmlrkvvee 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2412 -------LQSKHSSFVEKTSKLEE---SLKQEHGAVLQLQ-------QEAAHLKKQQEDAINAREEAE----------KE 2464
Cdd:pfam15921 484 ltakkmtLESSERTVSDLTASLQEkerAIEATNAEITKLRsrvdlklQELQHLKNEGDHLRNVQTECEalklqmaekdKV 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2465 LEKWRQKANEALRLRLQaeeeaHKKSLAQEDAEKQKEEAEREAKKRAKAEESALK-QKDMAEKELErqRKVADSTAQQKL 2543
Cdd:pfam15921 564 IEILRQQIENMTQLVGQ-----HGRTAGAMQVEKAQLEKEINDRRLELQEFKILKdKKDAKIRELE--ARVSDLELEKVK 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2544 TAEQELIRLRADFDnAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMD-----ILIQLKS-KAEKETMSNTE 2617
Cdd:pfam15921 637 LVNAGSERLRAVKD-IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnkLKMQLKSaQSELEQTRNTL 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2618 KSKQLLEAEATKM-----RDVAEEAGKLRAIaeeaKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKE 2692
Cdd:pfam15921 716 KSMEGSDGHAMKVamgmqKQITAKRGQIDAL----QSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGE 791
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 2693 KEAENERLRRAAEDEAYQRKALeDEANQHKKEIEEkIVQLKKSSDAEMERQKAM 2746
Cdd:pfam15921 792 LEVLRSQERRLKEKVANMEVAL-DKASLQFAECQD-IIQRQEQESVRLKLQHTL 843
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2833-3155 |
7.86e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 65.53 E-value: 7.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2833 EAARQRKIAQDELERLKKKAEEARKQKDEADVEAEVQivAAQQAALKCSTAEHQVQSVLAQQKE---DSIMHKKLKQEYE 2909
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE--KARQAEMDRQAAIYAEQERMAMERErelERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2910 KAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAAIQakaQEDAERLRKEAEFEAAK-RAQAEGAALKQKQQA 2988
Cdd:pfam17380 364 RIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKIL---EEERQRKIQQQKVEMEQiRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2989 DAEMAKH-KKLAEQTLKQKFQVEqeltkvKLKLDDTDKQKSllddelqrlKDEVDDAVKQRGQVEEELFKVKVQMEELLK 3067
Cdd:pfam17380 441 EEERAREmERVRLEEQERQQQVE------RLRQQEEERKRK---------KLELEKEKRDRKRAEEQRRKILEKELEERK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3068 LKLRIEDENQRLLKKDKDNSQKFLAEEAEnmKRLAEDAARLSVESQEAARLRQIAEdDLIQQRALADKMLKEK--MQAIQ 3145
Cdd:pfam17380 506 QAMIEEERKRKLLEKEMEERQKAIYEEER--RREAEEERRKQQEMEERRRIQEQMR-KATEERSRLEAMERERemMRQIV 582
|
330
....*....|
gi 1678729579 3146 ESSRLKAEAE 3155
Cdd:pfam17380 583 ESEKARAEYE 592
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2076-2629 |
9.24e-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: 65.43 E-value: 9.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2076 KTLKEQLSQEKKLLEEIENNKDNVDECQKYAKAYINSIKDYELQLVAYNAQadplasplkKTKLDSASDNIIQEYVTLRT 2155
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE---------KLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2156 RYSELMTLTSQYIKFITETQRrLEDEEKAAKKLKAEEQKKMAEMQAELDK-QKQLAAAHAKAIAKAEKEAQELKlmmkeE 2234
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISE-LKKQNNQLKDNIEKKQQEINEKTTEISNtQTQLNQLKDEQNKIKKQLSEKQK-----E 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2235 VNRREIAAVDAEKQKQNIQLELHELKNLSEQQIKDKgqlvdealqsrtkIEEEIYLIRIQLETTVKQKSTAESELKQLRE 2314
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKE-------------LKSELKNQEKKLEEIQNQISQNNKIISQLNE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2315 RAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEK- 2393
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKe 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2394 --ERQIKV--AHVAAQKSAAAELQSKHSSFVEKTSKLEESLKqehgavlQLQQEAAHLKKQQEDAINAREEAEKELEkwr 2469
Cdd:TIGR04523 423 llEKEIERlkETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE-------SLETQLKVLSRSINKIKQNLEQKQKELK--- 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2470 QKANEALRLRlqaeeeAHKKSLAQEDAEKQKEEAerEAKKRAKAEESALKQKDMAEKELERQRKVADSTaqqkLTAEQel 2549
Cdd:TIGR04523 493 SKEKELKKLN------EEKKELEEKVKDLTKKIS--SLKEKIEKLESEKKEKESKISDLEDELNKDDFE----LKKEN-- 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2550 irLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKEtMSNTEKSKQLLEAEATK 2629
Cdd:TIGR04523 559 --LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE-LEKAKKENEKLSSIIKN 635
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2319-2765 |
1.04e-09 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 65.16 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2319 AERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQkQKALDDLENLKKQAEEAERQVKQAEVEKERQIK 2398
Cdd:pfam09731 43 GEEVVLYALGEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQ-VKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2399 VAHVAaqKSAAAELQSKHSSFVEKTSKLEESLKQEhgavlQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKAnEALRL 2478
Cdd:pfam09731 122 SEQEK--EKALEEVLKEAISKAESATAVAKEAKDD-----AIQAVKAHTDSLKEASDTAEISREKATDSALQKA-EALAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2479 RLQAEEEAHKKSLAQEDAEkQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRAD-FD 2557
Cdd:pfam09731 194 KLKEVINLAKQSEEEAAPP-LLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDiIP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2558 NAEQQRSLLEDELYRL----KNEVIAAQQQ--------RKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQL-LE 2624
Cdd:pfam09731 273 VLKEDNLLSNDDLNSLiahaHREIDQLSKKlaelkkreEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLeFE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2625 AEATKMRDVAEEagKLRAIAEeakhqrqvaeeeaaRQRAEAERILKEKLaaISEATHLKTEAEIALKEKEAENERLRRAA 2704
Cdd:pfam09731 353 REREEIRESYEE--KLRTELE--------------RQAEAHEEHLKDVL--VEQEIELQREFLQDIKEKVEEERAGRLLK 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2705 EDEAYQR-KALEDEANQHKKEIEE--KIVQLKKSSDAemerqkamVDDTLK------QRRVVEEEIRILK 2765
Cdd:pfam09731 415 LNELLANlKGLEKATSSHSEVEDEnrKAQQLWLAVEA--------LRSTLEdgsadsRPRPLVRELKALK 476
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2149-2405 |
1.11e-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: 65.14 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2149 EYVTLRTRYSELMTLTSQYIKFITETQRRLEdeekaakKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELK 2228
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEISRMRELE-------RLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2229 LMMK--EEVNRREIAAVDAEKQKQNIQLELHELKNlsEQQIKDKGQlvDEALQSRTKIEEEIYLiRIQLETTVKQKSTAE 2306
Cdd:pfam17380 424 QIRAeqEEARQREVRRLEEERAREMERVRLEEQER--QQQVERLRQ--QEEERKRKKLELEKEK-RDRKRAEEQRRKILE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2307 SELKQLRERAAEAERLRKVAQEEAEKLHKQVIEEtQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQV 2386
Cdd:pfam17380 499 KELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-ERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREM 577
|
250
....*....|....*....
gi 1678729579 2387 KQAEVEKERQIKVAHVAAQ 2405
Cdd:pfam17380 578 MRQIVESEKARAEYEATTP 596
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2158-2715 |
1.45e-09 |
|
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: 64.76 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2158 SELMTLTSQYIKFITETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELKLMMKEEVnr 2237
Cdd:pfam05557 9 ARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLE-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2238 reiAAVDAEKQKQNIQLELHELKNLSEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAE---SEL-KQLR 2313
Cdd:pfam05557 87 ---ALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEqlrQNLeKQQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2314 ERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAE-KELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVE 2392
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARiPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2393 KER----QIKVAHVAAQ---------------------KSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHL 2447
Cdd:pfam05557 244 REEaatlELEKEKLEQElqswvklaqdtglnlrspedlSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2448 KKQQEDAINAREEAEKELEKWRQKANEALRLR--LQAEEEAHKKSLAQEDAEKQKEEAEREA-----KKRAKAEESALkQ 2520
Cdd:pfam05557 324 LKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgYRAILESYDKELTMSNYSPQLLERIEEAedmtqKMQAHNEEMEA-Q 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2521 KDMAEKELERQRKVADstaqqklTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDI 2600
Cdd:pfam05557 403 LSVAEEELGGYKQQAQ-------TLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRC 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2601 LIQlkskaeketMSNTEKSK--QLLEAEATKMRDV-AEEAGKLRaiaeeakhqrqvAEEEAARQRAEAERILKEKLAAIS 2677
Cdd:pfam05557 476 LQG---------DYDPKKTKvlHLSMNPAAEAYQQrKNQLEKLQ------------AEIERLKRLLKKLEDDLEQVLRLP 534
|
570 580 590
....*....|....*....|....*....|....*...
gi 1678729579 2678 EATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALE 2715
Cdd:pfam05557 535 ETTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKIQE 572
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2997-3232 |
1.57e-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: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2997 KLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELfkvKVQMEELLKLKLRIEdEN 3076
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAELAELEKEIA-EL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3077 QRLLKKDKDNSQKFLAeEAENMKRLAEDAARLSVES-QEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAE 3155
Cdd:COG4942 96 RAELEAQKEELAELLR-ALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3156 MLQRQKDLAQEQAQKL---LEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFK 3232
Cdd:COG4942 175 ELEALLAELEEERAALealKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2519-2751 |
2.02e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 63.29 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2519 KQKDMAEKELERQRKvadstAQQKltaEQELIRLRAdfdnAEQQRsLLEDELYRLkneviAAQQQRKQLEDELAKVRSEm 2598
Cdd:PRK09510 70 QQKSAKRAEEQRKKK-----EQQQ---AEELQQKQA----AEQER-LKQLEKERL-----AAQEQKKQAEEAAKQAALK- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2599 diliqlKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAgklraiAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISE 2678
Cdd:PRK09510 131 ------QKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKA------AAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAE 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 2679 AthlKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDeanqhKKEIEEKIVQLKKSSDAEMERQKAMVDDTL 2751
Cdd:PRK09510 199 A---KKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAE-----AKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2379-2810 |
2.27e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.59 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2379 AEEAERQVKQA-EVEKERQIKVAHVAAQKSAAAELQSKhssfVEKTSKLEESLKQEHGAV---LQLQQEAAHLKKQQEDA 2454
Cdd:PRK04863 278 ANERRVHLEEAlELRRELYTSRRQLAAEQYRLVEMARE----LAELNEAESDLEQDYQAAsdhLNLVQTALRQQEKIERY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2455 INAREEAEKELEkwrqkanEALRLRLQAEEEahkkslaQEDAEKQKEEAEREAKkRAKAEESALKQK-DMAEKelerqRK 2533
Cdd:PRK04863 354 QADLEELEERLE-------EQNEVVEEADEQ-------QEENEARAEAAEEEVD-ELKSQLADYQQAlDVQQT-----RA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2534 VADSTAQQKLTAEQELIRLrADF--DNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKE 2611
Cdd:PRK04863 414 IQYQQAVQALERAKQLCGL-PDLtaDNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2612 TMSNTEKSkqlLEAEATKMRDVAEEAGKLRAIAEEAKhQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALk 2691
Cdd:PRK04863 493 EAWDVARE---LLRRLREQRHLAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARL- 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2692 ekEAENERLRRAAEDEAYQRkaledeanQHKKEIEEKIVQLKKSS------DAEMERQKAMVDDTLKQRRVVEEEIRILK 2765
Cdd:PRK04863 568 --ESLSESVSEARERRMALR--------QQLEQLQARIQRLAARApawlaaQDALARLREQSGEEFEDSQDVTEYMQQLL 637
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1678729579 2766 LNFEKASSGKLDLELELNKLKNIAEETQQsklRAEEEAEKLRKLA 2810
Cdd:PRK04863 638 ERERELTVERDELAARKQALDEEIERLSQ---PGGSEDPRLNALA 679
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3031-3240 |
3.17e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.54 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3031 DDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLlKKDKDNSQKFLAE----EAENMKRLAEDAA 3106
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEaeaeIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3107 RLSVESQEAARLRQIAE----DDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRL 3182
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678729579 3183 EEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAA 3240
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2547-3230 |
3.53e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2547 QELIRLRADFDNAEQQRSLLEdELYRLKNEVIAAQQQRKQLEDELAKVRSEMDiliQLKSKAEKETMSNTEKSKQLLEAE 2626
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFA---QRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2627 atkMRDVAEEAGKLRAIAEEAKHQRQ----VAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRR 2702
Cdd:COG4913 311 ---LERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2703 AAEDEAYQRKALEDEANQHKKEIEEKIVQLKKssdaemerqkamvddtlkQRRVVEEEIRILKlnfekasSGKLDLELEL 2782
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRR------------------ELRELEAEIASLE-------RRKSNIPARL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2783 NKLKN-IAEETQQSK-----------LRAEEE-----AEK-LRKLALEEekrrreaeekvkkITAAEEEAARQRKIAQDE 2844
Cdd:COG4913 443 LALRDaLAEALGLDEaelpfvgelieVRPEEErwrgaIERvLGGFALTL-------------LVPPEHYAAALRWVNRLH 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2845 L------ERLKKKAEEARKQKDEADVEAEV-------------QIVAAQQAALKCSTAE---HQVQSVLA--QQKEDSIM 2900
Cdd:COG4913 510 LrgrlvyERVRTGLPDPERPRLDPDSLAGKldfkphpfrawleAELGRRFDYVCVDSPEelrRHPRAITRagQVKGNGTR 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2901 HKKLKQEYEKAKKLA-KEAEAAKEKAEREAALLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEA-AKRAQAE 2978
Cdd:COG4913 590 HEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdVASAERE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2979 GAALK-QKQQADAEMAKHKKLAEQtLKqkfQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAvkqRGQVEEELFK 3057
Cdd:COG4913 670 IAELEaELERLDASSDDLAALEEQ-LE---ELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL---QDRLEAAEDL 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3058 VKVQMEELLKLKLR--IEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDAAR--------------LSVESQE--AARLR 3119
Cdd:COG4913 743 ARLELRALLEERFAaaLGDAVERELRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldADLESLPeyLALLD 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3120 QIAEDDLIQQRALADKMLKEkmQAIQESSRLKAEaemLQRQKDLAQEQAQKL---LEDKQ---------LMQRRLEEETE 3187
Cdd:COG4913 823 RLEEDGLPEYEERFKELLNE--NSIEFVADLLSK---LRRAIREIKERIDPLndsLKRIPfgpgrylrlEARPRPDPEVR 897
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1678729579 3188 EYQKSL-EAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKK 3230
Cdd:COG4913 898 EFRQELrAVTSGASLFDEELSEARFAALKRLIERLRSEEEESDR 941
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2313-2541 |
4.17e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 62.58 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2313 RERAAEAERLRKVAQEEAEKlhkqvieETQKKriaekelqhKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVE 2392
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAER-------ETEIA---------IAQANREAEEAELEQEREIETARIAEAEAELAKKKAEER 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2393 KERQIKvahvAAQKSAAAELQskhssfvektsklEESLKQEhgavLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKA 2472
Cdd:COG2268 255 REAETA----RAEAEAAYEIA-------------EANAERE----VQRQLEIAEREREIELQEKEAEREEAELEADVRKP 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2473 NEALRLRLQAEEEAHKkslaqeDAEKQKEEAEREAkKRAKAE-ESALKQKDMAEKELERQRKVADSTAQQ 2541
Cdd:COG2268 314 AEAEKQAAEAEAEAEA------EAIRAKGLAEAEG-KRALAEaWNKLGDAAILLMLIEKLPEIAEAAAKP 376
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2304-2595 |
4.78e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2304 TAESELKQLRERAAEAERLRKVAQEEAEKLhKQVIEETQKKRIAEKELQHKSEAEKEAAkQKQKALDDLENLKKQAEEAE 2383
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEAL-EAELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2384 RQVKQAevekERQIKvahvaaqksaaaelqskhssfvektsKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEK 2463
Cdd:COG4913 685 DDLAAL----EEQLE--------------------------ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2464 ELEKWRQKANEALRLRLQAEeeahkksLAQEDAEKQKEEAEREAKKRAKAEESALKQkdmAEKELERQRK---------V 2534
Cdd:COG4913 735 RLEAAEDLARLELRALLEER-------FAAALGDAVERELRENLEERIDALRARLNR---AEEELERAMRafnrewpaeT 804
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 2535 ADSTA--------QQKLT--AEQELIRLRADFDNAEQQRS--LLEDELYRLKNEVIAAQQQRKQLEDELAKVR 2595
Cdd:COG4913 805 ADLDAdleslpeyLALLDrlEEDGLPEYEERFKELLNENSieFVADLLSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3205-3415 |
5.08e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3205 AEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEferlntsKEAGDLRDAIADLEKDK 3284
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-------QELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3285 ARLKKEAEELQNKSKEMADAQQKQIEHEKTLL----------------QQTFLTEREMLLKKEKLIEEEKKKLESQFEEE 3348
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678729579 3349 AKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMLSKQKEMQELEK--KRLEQEIILADE 3415
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAliARLEAEAAAAAE 241
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2479-2810 |
6.93e-09 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 61.62 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2479 RLQAEEEAHKKSLAQE--DAEKQKEEAERE---AKKRAKAEESALKQkdmAEKELERQRKVADSTAQQKLTAEQELirlr 2553
Cdd:pfam19220 55 ALLAQERAAYGKLRRElaGLTRRLSAAEGEleeLVARLAKLEAALRE---AEAAKEELRIELRDKTAQAEALERQL---- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2554 adFDNAEQQRSLlEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQ----LKSKAEK---ETMSNTEKSKQLLEAE 2626
Cdd:pfam19220 128 --AAETEQNRAL-EEENKALREEAQAAEKALQRAEGELATARERLALLEQenrrLQALSEEqaaELAELTRRLAELETQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2627 ATKMRDVAEEAGKLraIAEEAKHQRQVAEEEAARQRAEAERI-LKEKLAAIS---EAT-HLKTEAEIALKEKEAENERLR 2701
Cdd:pfam19220 205 DATRARLRALEGQL--AAEQAERERAEAQLEEAVEAHRAERAsLRMKLEALTaraAATeQLLAEARNQLRDRDEAIRAAE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2702 RAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQK--AMVDDTLKQRRVVEE--EIRILKLNfEKASSGKLD 2777
Cdd:pfam19220 283 RRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEEraEMLTKALAAKDAALEraEERIASLS-DRIAELTKR 361
|
330 340 350
....*....|....*....|....*....|....
gi 1678729579 2778 LELELNKLkniaeETQQSKLRAEEEAEKL-RKLA 2810
Cdd:pfam19220 362 FEVERAAL-----EQANRRLKEELQRERAeRALA 390
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2308-2660 |
6.97e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 61.09 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2308 ELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEK----ELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAE 2383
Cdd:pfam13868 7 ELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMmeeeRERALEEEEEKEEERKEERKRYRQELEEQIEERE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2384 RQVKQAEVEKERQIKVAHVAAQKSAAAELQSKhssfvEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAR-EEAE 2462
Cdd:pfam13868 87 QKRQEEYEEKLQEREQMDEIVERIQEEDQAEA-----EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERiLEYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2463 KELEKwRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQK 2542
Cdd:pfam13868 162 KEKAE-REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2543 LTAEQELIRLRadfdnaeQQRSLLEDELYRLKNEviaaqqQRKQLEDELAKVRSEMDILIQLKSKAEKEtmsnteksKQL 2622
Cdd:pfam13868 241 REEQIELKERR-------LAEEAEREEEEFERML------RKQAEDEEIEQEEAEKRRMKRLEHRRELE--------KQI 299
|
330 340 350
....*....|....*....|....*....|....*...
gi 1678729579 2623 LEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAAR 2660
Cdd:pfam13868 300 EEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5134-5171 |
7.12e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.03 E-value: 7.12e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1678729579 5134 QRLLEAQACTGGIIDPTTGERFQVSDATEKGLVDKIMV 5171
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2966-3280 |
7.41e-09 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 62.62 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2966 EAEFEAAKRAQAEGAALKQKQQADAEMAKHKKLAEQTL---KQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVD 3042
Cdd:PRK11281 32 NGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3043 DAVKQR------GQVEEELFKVKVQMEELLKlklRIEDENQRL--LKKDKDNSQKFLaeeAENMKRLAEDAARLSVESQE 3114
Cdd:PRK11281 112 EETRETlstlslRQLESRLAQTLDQLQNAQN---DLAEYNSQLvsLQTQPERAQAAL---YANSQRLQQIRNLLKGGKVG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3115 AARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKaeaEMLQRQKDLAQEQAQKLLEDKQLMQ-----RRLE--EET- 3186
Cdd:PRK11281 186 GKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQ---DLLQKQRDYLTARIQRLEHQLQLLQeainsKRLTlsEKTv 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3187 EEYQKSLEAERRRQLEIVAEAEKLKLQVSQ-LSEAQTKAEE---EAKKFKKQADkiaaRLHETEIATKEKMTVVE-KLEF 3261
Cdd:PRK11281 263 QEAQSQDEAARIQANPLVAQELEINLQLSQrLLKATEKLNTltqQNLRVKNWLD----RLTQSERNIKEQISVLKgSLLL 338
|
330 340
....*....|....*....|....*..
gi 1678729579 3262 ER--------LNTSKEAGDLRDAIADL 3280
Cdd:PRK11281 339 SRilyqqqqaLPSADLIEGLADRIADL 365
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2610-2907 |
7.83e-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: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2610 KETMSNTEKSKQLLEAEATKMRDVAEEagklraIAEEAKHQRQVAEEEAARQrAEAERilKEKLAAISEATHLKTEAE-- 2687
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEE------KAREVERRRKLEEAEKARQ-AEMDR--QAAIYAEQERMAMEREREle 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2688 -IALKEKEAENERLRR---AAEDEAYQR-KALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEE--- 2759
Cdd:pfam17380 352 rIRQEERKRELERIRQeeiAMEISRMRElERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEqee 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2760 --EIRILKLNFEKASsgkldlELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEE----- 2832
Cdd:pfam17380 432 arQREVRRLEEERAR------EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEleerk 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2833 ----EAARQRKIAQDELE-RLKKKAEEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKEDSIMHKKLKQE 2907
Cdd:pfam17380 506 qamiEEERKRKLLEKEMEeRQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2420-2806 |
9.09e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 62.66 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2420 VEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDainaREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQ 2499
Cdd:COG3096 284 SERALELRRELFGARRQLAEEQYRLVEMARELEE----LSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLEEL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2500 KEEAEREAKKRAKAEEsalkQKDMAEKELERQRKVADSTA------QQKLTAEQEliR-------LRAdFDNAEQQRSLL 2566
Cdd:COG3096 360 TERLEEQEEVVEEAAE----QLAEAEARLEAAEEEVDSLKsqladyQQALDVQQT--RaiqyqqaVQA-LEKARALCGLP 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2567 EDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDIliqlkSKAEKetmSNTEKSKQLLEAEA---------TKMRDVAEEA 2637
Cdd:COG3096 433 DLTPENAEDYLAAFRAKEQQATEEVLELEQKLSV-----ADAAR---RQFEKAYELVCKIAgeversqawQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2638 GKLRAIAEEAKH-QRQVAE-EEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALE 2715
Cdd:COG3096 505 RSQQALAQRLQQlRAQLAElEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELR 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2716 deanQHKKEIEEKIVQLKKS------SDAEMERQKAMVDDTLKQRRVVEEEIRILklnfekassgkLDLELELNKLKnia 2789
Cdd:COG3096 585 ----QQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEVTAAMQQL-----------LEREREATVER--- 646
|
410
....*....|....*..
gi 1678729579 2790 EETQQSKLRAEEEAEKL 2806
Cdd:COG3096 647 DELAARKQALESQIERL 663
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2304-2540 |
9.62e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2304 TAESELKQLRERAAEAERLRKVAQEEAEKLHKQVieetqkkriaekelqhkseaeKEAAKQKQKALDDLENLKKQAEEAE 2383
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAEL---------------------EELNEEYNELQAELEALQAEIDKLQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2384 RQVKQAEVE-KERQIKVAHVA--AQKSAAAE------LQSKH-SSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQED 2453
Cdd:COG3883 72 AEIAEAEAEiEERREELGERAraLYRSGGSVsyldvlLGSESfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2454 AINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRK 2533
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
....*..
gi 1678729579 2534 VADSTAQ 2540
Cdd:COG3883 232 AAAAAAA 238
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3061-3419 |
1.16e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 60.70 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3061 QMEELLKLKLRIEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDAARlsvesqeaarlrqiaeddliQQRALADKMLKEK 3140
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKR--------------------YRQELEEQIEERE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3141 MQAIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKslEAERRRQLEIVAEAEKLKLQVSQLSEA 3220
Cdd:pfam13868 87 QKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNE--EQAEWKELEKEEEREEDERILEYLKEK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3221 QtkAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNtskeagDLRDAIADLEKDKARLKKEAEELQNKSKE 3300
Cdd:pfam13868 165 A--EREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELR------AKLYQEEQERKERQKEREEAEKKARQRQE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3301 MADAQQKQIEHEKTLLQQTFLTEREmllkkeklieeekkklesqFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEA 3380
Cdd:pfam13868 237 LQQAREEQIELKERRLAEEAEREEE-------------------EFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK 297
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1678729579 3381 LSKQKEAEK--EMLSKQKEMQELEKKRLEQEIILADENQKL 3419
Cdd:pfam13868 298 QIEEREEQRaaEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2265-2907 |
1.26e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.90 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2265 QQIKDKGQLVDEALQSRTKIE---EEIYLIRIQLETtvkqkstAESELKQLRERAAEAERLRKVAQEEAEKLHKQV---- 2337
Cdd:PRK04863 331 QAASDHLNLVQTALRQQEKIEryqADLEELEERLEE-------QNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyq 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2338 --IEETQKKRIAekeLQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAE---VEKERQIKVAHVAA-QKSAAAE 2411
Cdd:PRK04863 404 qaLDVQQTRAIQ---YQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATeelLSLEQKLSVAQAAHsQFEQAYQ 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2412 LQSK----------HSSFVEKTSKLEEsLKQEHGAVLQLQQEAAHLKK---QQEDAINAREEAEKELEkwRQKANEALRL 2478
Cdd:PRK04863 481 LVRKiagevsrseaWDVARELLRRLRE-QRHLAEQLQQLRMRLSELEQrlrQQQRAERLLAEFCKRLG--KNLDDEDELE 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2479 RLQAEEEAhkkslAQEDAEKQKEEAereakkraKAEESALKQKdmaEKELERQRKVADSTAQQKLTAEQELIRLR----A 2554
Cdd:PRK04863 558 QLQEELEA-----RLESLSESVSEA--------RERRMALRQQ---LEQLQARIQRLAARAPAWLAAQDALARLReqsgE 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2555 DFDNAEQQRSLLEDELYRLKN---EVIAAQQQRKQLEDELAKVR----SEMDILIQLKSKAEKETMSNTEKSKQLLEA-- 2625
Cdd:PRK04863 622 EFEDSQDVTEYMQQLLEREREltvERDELAARKQALDEEIERLSqpggSEDPRLNALAERFGGVLLSEIYDDVSLEDApy 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2626 ---------EATKMRDVAEEAGKLRAI-----------------------AEEakHQRQVAEEEAARQ------------ 2661
Cdd:PRK04863 702 fsalygparHAIVVPDLSDAAEQLAGLedcpedlyliegdpdsfddsvfsVEE--LEKAVVVKIADRQwrysrfpevplf 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2662 --RAEAERI--LKEKLAAISEAtHLKTEAEI--------ALKEKEAENERLRRAAEDEAYQRKALE--DEANQHKKEIEE 2727
Cdd:PRK04863 780 grAAREKRIeqLRAEREELAER-YATLSFDVqklqrlhqAFSRFIGSHLAVAFEADPEAELRQLNRrrVELERALADHES 858
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2728 KIVQLKKSSDAEMERQKAM----------VDDTLKQR-RVVEEEIrilklnfEKASSGKLDLELELNKLKNIaeETQQSK 2796
Cdd:PRK04863 859 QEQQQRSQLEQAKEGLSALnrllprlnllADETLADRvEEIREQL-------DEAEEAKRFVQQHGNALAQL--EPIVSV 929
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2797 LRAEEEA-EKLRKLALEEEKRRREAEEKVKKITA--------AEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEae 2867
Cdd:PRK04863 930 LQSDPEQfEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQ-- 1007
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1678729579 2868 vqivaAQQAALKCSTAeHQVQSVL---AQQKEDsiMHKKLKQE 2907
Cdd:PRK04863 1008 -----LRQAQAQLAQY-NQVLASLkssYDAKRQ--MLQELKQE 1042
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2308-2547 |
1.30e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 61.50 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2308 ELKQLR---ERAAEAERLRKVAQEEAEKLHKQVIE--ETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEA 2382
Cdd:PRK05035 456 EARQARlerEKAAREARHKKAAEARAAKDKDAVAAalARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQA 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2383 ERQVKQAEVEKERQIK--VAHVAAQKSAAAELQSKHSSFVEKTSkleeslkqehgAVLQLQQEAAHLKKQQEDAINAREE 2460
Cdd:PRK05035 536 EKQAAAAADPKKAAVAaaIARAKAKKAAQQAANAEAEEEVDPKK-----------AAVAAAIARAKAKKAAQQAASAEPE 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2461 AEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTA- 2539
Cdd:PRK05035 605 EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAi 684
|
250
....*....|.
gi 1678729579 2540 ---QQKLTAEQ 2547
Cdd:PRK05035 685 araKAKKAAQQ 695
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2500-2968 |
1.53e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2500 KEEAEREAKKRAKAEESALKQKdmaeKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIA 2579
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKEL----KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2580 AQ--QQRKQLEDELAKVRSEMDILiqlksKAEKETMSNTEKSKQLLEAEATKMRdvaeeagklRAIAEEAKHQRQVAEEE 2657
Cdd:COG4717 128 LPlyQELEALEAELAELPERLEEL-----EERLEELRELEEELEELEAELAELQ---------EELEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2658 AARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRK--------------ALEDEANQHKK 2723
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallallGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2724 EIEEKI----------VQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDlelELNKLKNIAEETQ 2793
Cdd:COG4717 274 TIAGVLflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE---ELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2794 QSKLRAEEEAEKLRKLALEEEKRRReaeekVKKITAAEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEAEVQIVAA 2873
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAAL-----LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2874 QQAALkcstaEHQVQSVLAQQKEDSIMHKKLKQEYEKAKKLAKEAEAAKEKAEreaalLRQQAEEAERQKAAAEQEAAIQ 2953
Cdd:COG4717 426 DEEEL-----EEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE-----LLQELEELKAELRELAEEWAAL 495
|
490
....*....|....*
gi 1678729579 2954 AKAQEDAERLRKEAE 2968
Cdd:COG4717 496 KLALELLEEAREEYR 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3218-3433 |
1.57e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3218 SEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNK 3297
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3298 SK-------EMADAQQK--QIEHEKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQQMEE 3368
Cdd:COG4942 99 LEaqkeelaELLRALYRlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678729579 3369 EKKKLhATMHEALSKQKEAEKEMLSKQKEMQELEKKRLEQeiiLADENQKLREKLQQLEEAQKEQ 3433
Cdd:COG4942 179 LLAEL-EEERAALEALKAERQKLLARLEKELAELAAELAE---LQQEAEELEALIARLEAEAAAA 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2994-3432 |
2.02e-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: 61.19 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2994 KHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLL---DDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKL 3070
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3071 RIEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDaarlsVESQEAARLRQIaeDDLIQQRAladKMLKEKMQAIQESSRL 3150
Cdd:TIGR04523 292 QLKSEISDLNNQKEQDWNKELKSELKNQEKKLEE-----IQNQISQNNKII--SQLNEQIS---QLKKELTNSESENSEK 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3151 KAEAEMLQRQ-KDLAQEQAQKLLEDKQLMQRRLEEETE-EYQKSLEAERRRQLEIV-AEAEKLKLQVSQLSEAQTKAEEE 3227
Cdd:TIGR04523 362 QRELEEKQNEiEKLKKENQSYKQEIKNLESQINDLESKiQNQEKLNQQKDEQIKKLqQEKELLEKEIERLKETIIKNNSE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3228 AKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMADAQQK 3307
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3308 QIEHEKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEEEakkskalKDEQERQKQQMEEEKKKLHATMHEA--LSKQK 3385
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE-------IDEKNKEIEELKQTQKSLKKKQEEKqeLIDQK 594
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1678729579 3386 EAEKEMLSKQKEMQELEKKRLEQEIILAD-ENQKLREKLQQLEEAQKE 3432
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKELEKAKkENEKLSSIIKNIKSKKNK 642
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2176-2585 |
2.60e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 59.55 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2176 RRLEDEEKAAKklkaeeqkkmaeMQAELDKQKQlaaahakaiakaekEAQELKLMMKEEvnRREIAAVDAEKQKQNIQLE 2255
Cdd:pfam13868 9 RELNSKLLAAK------------CNKERDAQIA--------------EKKRIKAEEKEE--ERRLDEMMEEERERALEEE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2256 LHELKNLSEQQIKDKGQLVDEALQSRTKIEEEiyliriqlettvkqkstaesELKQLRERAAEAERLRKVAQEEAEKLhk 2335
Cdd:pfam13868 61 EEKEEERKEERKRYRQELEEQIEEREQKRQEE--------------------YEEKLQEREQMDEIVERIQEEDQAEA-- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2336 qviEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLK-------KQAEEAERQVKQAEVEKERQIKVAHVAAQKSA 2408
Cdd:pfam13868 119 ---EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERileylkeKAEREEEREAEREEIEEEKEREIARLRAQQEK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2409 AAELQSkhssfvektskleeslkqehgavlqlQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEEEAHK 2488
Cdd:pfam13868 196 AQDEKA--------------------------ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2489 KSLAqedAEKQKEEAEREAKKRAKAEEsalKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLED 2568
Cdd:pfam13868 250 RRLA---EEAEREEEEFERMLRKQAED---EEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREE 323
|
410
....*....|....*..
gi 1678729579 2569 ELYRlkNEVIAAQQQRK 2585
Cdd:pfam13868 324 EAER--RERIEEERQKK 338
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3091-3300 |
2.78e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3091 LAEEAENMKRLAEDAARLS-----VESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQ 3165
Cdd:COG4913 257 IRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3166 ----EQAQKLLEDKQLMQRRLEEETEEYQKSLeaeRRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAAR 3241
Cdd:COG4913 337 gdrlEQLEREIERLERELEERERRRARLEALL---AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAA 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3242 LHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIAD-LEKDKARLKKEAEELQNKSKE 3300
Cdd:COG4913 414 LRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3071-3307 |
3.25e-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: 59.39 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3071 RIEDENQRL--LKKDKDNSQKFLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESS 3148
Cdd:COG4942 21 AAAEAEAELeqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3149 RLKAE-AEMLQRQKDLAQEQAQKLL---EDKQLMQRRLEeeteeYQKSLEAERRRQleivaeAEKLKLQVSQLSEAQTKA 3224
Cdd:COG4942 101 AQKEElAELLRALYRLGRQPPLALLlspEDFLDAVRRLQ-----YLKYLAPARREQ------AEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3225 EEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMADA 3304
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 1678729579 3305 QQK 3307
Cdd:COG4942 250 ALK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2314-3043 |
3.53e-08 |
|
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: 60.12 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2314 ERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKseaeKEAAKQKQKALDDLenlkkQAEEAERQVKQAEVEK 2393
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQEN----RKIIEAQRKAIQEL-----QFENEKVSLKLEEEIQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2394 ERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEhgavlqlQQEAAHLKKQQEDAINAREEAEKELEKWRQKAN 2473
Cdd:pfam05483 142 ENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREET-------RQVYMDLNNNIEKMILAFEELRVQAENARLEMH 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2474 EALRL---RLQAEEEAHKKSLaqEDAEKQK-----EEAEREAKKRAKA---EESALKQKDMAEK-ELERQRKVADSTAQQ 2541
Cdd:pfam05483 215 FKLKEdheKIQHLEEEYKKEI--NDKEKQVsllliQITEKENKMKDLTfllEESRDKANQLEEKtKLQDENLKELIEKKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2542 KLTAEQELIRLRADfDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEdELAKVRSEMDILI-QLKS---------KAEKE 2611
Cdd:pfam05483 293 HLTKELEDIKMSLQ-RSMSTQKALEEDLQIATKTICQLTEEKEAQME-ELNKAKAAHSFVVtEFEAttcsleellRTEQQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2612 TMSNTEKSKQLLEAEATKMRDVAEEAGKLraiaeeaKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLK-TEAEIAL 2690
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTKF-------KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgKEQELIF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2691 KEKEAENErlrraAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRI---LKLN 2767
Cdd:pfam05483 444 LLQAREKE-----IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMtleLKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2768 FEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRKIAQDELER 2847
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2848 LKKKAEEARKQKDEADVEaevqivaaQQAALKCSTAEHQvqsvlaQQKEDSIMHKKLKQEYekakklakeaeaaKEKAER 2927
Cdd:pfam05483 599 LKKQIENKNKNIEELHQE--------NKALKKKGSAENK------QLNAYEIKVNKLELEL-------------ASAKQK 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2928 EAALLRQQAEEAERQKAAAEQEAAIQAKAQ---EDAERLRKEAEFEAAKRAqAEGAALKQK---------QQADAEMAKH 2995
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKISEEKLLEEVEKAKaiaDEAVKLQKEIDKRCQHKI-AEMVALMEKhkhqydkiiEERDSELGLY 730
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1678729579 2996 KKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDD 3043
Cdd:pfam05483 731 KNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2727-3428 |
3.60e-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: 60.62 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2727 EKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRILK-----------------------LNFEKASSGKLDLELELN 2783
Cdd:pfam12128 182 DKIAKAMHSKEGKFRDVKSMIVAILEDDGVVPPKSRLNRqqvehwirdiqaiagimkirpefTKLQQEFNTLESAELRLS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2784 KLK------NIAEETQQsKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARqrkiAQDELERLkkkaEEARK 2857
Cdd:pfam12128 262 HLHfgyksdETLIASRQ-EERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAK----DRSELEAL----EDQHG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2858 QKDEADVEAevqiVAAQQAALKCSTAEHQVQSVLAQQKEDSimHKKLKQEYEKAKKLAKEAEAAKEKAEREAalLRQQAE 2937
Cdd:pfam12128 333 AFLDADIET----AAADQEQLPSWQSELENLEERLKALTGK--HQDVTAKYNRRRSKIKEQNNRDIAGIKDK--LAKIRE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2938 EAERQKaaaeQEAAIQAKAQEDAERLRKEA---EFEAAKRAQAEGAALKQKQQADAEMakhkklAEQTLKQKFQVEQELT 3014
Cdd:pfam12128 405 ARDRQL----AVAEDDLQALESELREQLEAgklEFNEEEYRLKSRLGELKLRLNQATA------TPELLLQLENFDERIE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3015 KVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLLKKD----KDNSQKF 3090
Cdd:pfam12128 475 RAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEapdwEQSIGKV 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3091 LAEE------------------AENMKRLAEDAARLSVES-----QEAARLRQIAEDDLIQQRALADKMLKEKMQAIQES 3147
Cdd:pfam12128 555 ISPEllhrtdldpevwdgsvggELNLYGVKLDLKRIDVPEwaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGEL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3148 SRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEaERRRQLEivAEAEKLKLQVSQLSEAQTKAEEE 3227
Cdd:pfam12128 635 EKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN-ERLNSLE--AQLKQLDKKHQAWLEEQKEQKRE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3228 AKKFKKQADKIAARLHETEIA----TKEKMTVVEKLEFERLNTSKeAGDLRDAIADLEKDkARLKKEAEELQNKSKEMAD 3303
Cdd:pfam12128 712 ARTEKQAYWQVVEGALDAQLAllkaAIAARRSGAKAELKALETWY-KRDLASLGVDPDVI-AKLKREIRTLERKIERIAV 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3304 AQQKQIEHEKtLLQQTFLTEREmllkkeklieeekkKLESQFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHeALSK 3383
Cdd:pfam12128 790 RRQEVLRYFD-WYQETWLQRRP--------------RLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERK-ASEK 853
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1678729579 3384 QKEAEKEMLSKQK-EMQELEKKRLEQEIILADenQKLREKLQQLEE 3428
Cdd:pfam12128 854 QQVRLSENLRGLRcEMSKLATLKEDANSEQAQ--GSIGERLAQLED 897
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
3036-3431 |
3.74e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 60.61 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3036 RLKDEV-DDAVKQRGQVEEELFKVKVQMEELL--------KLKLRIEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDAA 3106
Cdd:NF041483 116 RLQAELhTEAVQRRQQLDQELAERRQTVESHVnenvawaeQLRARTESQARRLLDESRAEAEQALAAARAEAERLAEEAR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3107 RLSVESQEAARlrqiAEDDLIQQRALADKmlkekmqaiqessrlkaeaemlQRQKDLAQEQAQKLLEDKQLMQRRLEEET 3186
Cdd:NF041483 196 QRLGSEAESAR----AEAEAILRRARKDA----------------------ERLLNAASTQAQEATDHAEQLRSSTAAES 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3187 EEyqksleaERRRQLEIVAEAEKlklQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERL-- 3264
Cdd:NF041483 250 DQ-------ARRQAAELSRAAEQ---RMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLvg 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3265 NTSKEAGDLRdaiADLEKDKARLKKEAEELQNKSKEmaDAQQKQIEHEKTLLQQTFLTEREMLlkkeklieeekkkleSQ 3344
Cdd:NF041483 320 EATKEAEALK---AEAEQALADARAEAEKLVAEAAE--KARTVAAEDTAAQLAKAARTAEEVL---------------TK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3345 FEEEAKKS-KALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEK----EMLSKQKEMQElEKKRL--EQEIILAD--- 3414
Cdd:NF041483 380 ASEDAKATtRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKddtkEYRAKTVELQE-EARRLrgEAEQLRAEava 458
|
410 420
....*....|....*....|..
gi 1678729579 3415 ENQKLR-----EKLQQLEEAQK 3431
Cdd:NF041483 459 EGERIRgearrEAVQQIEEAAR 480
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2933-3436 |
4.26e-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: 60.24 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2933 RQQAEEAERQKAAAEQEAAIQAKAQE--DAERLRKEAEFEAAKRAQAEGAAL----KQKQQADAEMAKhkklAEQTLKQK 3006
Cdd:pfam12128 276 SRQEERQETSAELNQLLRTLDDQWKEkrDELNGELSAADAAVAKDRSELEALedqhGAFLDADIETAA----ADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3007 FQVEQELTKVKLKLDDTDKQKslLDDELQRLKDEVD-DAVKQRGQVEEELFKVKvqmEELLKLKLRIEDENQRLLKKDKD 3085
Cdd:pfam12128 352 WQSELENLEERLKALTGKHQD--VTAKYNRRRSKIKeQNNRDIAGIKDKLAKIR---EARDRQLAVAEDDLQALESELRE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3086 NSQKFLAEEAENMKRLAEDAARLSVESQEAarlrQIAEDDLIQQRALADKMlkEKMQAIQESSRlkAEAEMLQRQKDLAQ 3165
Cdd:pfam12128 427 QLEAGKLEFNEEEYRLKSRLGELKLRLNQA----TATPELLLQLENFDERI--ERAREEQEAAN--AEVERLQSELRQAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3166 EQAQKLLEDKQLMQRRLEEETEEYQK----------SLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQA 3235
Cdd:pfam12128 499 KRRDQASEALRQASRRLEERQSALDElelqlfpqagTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGEL 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3236 DKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQnksKEMADAQQKqIEHEKTL 3315
Cdd:pfam12128 579 NLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS---REETFARTA-LKNARLD 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3316 LQQTFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHE-------ALSKQKEAE 3388
Cdd:pfam12128 655 LRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAywqvvegALDAQLALL 734
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3389 KEMLSKQKEMQELEKKRLEQ------------EIILADENQKLREKLQQLEEAQKEQHTV 3436
Cdd:pfam12128 735 KAAIAARRSGAKAELKALETwykrdlaslgvdPDVIAKLKREIRTLERKIERIAVRRQEV 794
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2840-3231 |
4.58e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 60.07 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2840 IAQDElERLKKKAEEARKQKDEADVEaevqIVAAQQAALKcSTAEHQVQSVLAQQKEDSI-----MHKKLKQEYEKAKKL 2914
Cdd:PRK10929 21 TAPDE-KQITQELEQAKAAKTPAQAE----IVEALQSALN-WLEERKGSLERAKQYQQVIdnfpkLSAELRQQLNNERDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2915 AKEAEAAKEKAEREAALL----------RQQAEEAERQKAAAEQEAAIQAKaQEDAERLRKEAEfeaaKRAQAEGA---A 2981
Cdd:PRK10929 95 PRSVPPNMSTDALEQEILqvssqlleksRQAQQEQDRAREISDSLSQLPQQ-QTEARRQLNEIE----RRLQTLGTpntP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2982 LKQKQ--QADAEMAKHK-KLAEQTLKQ-KFQVEQELTKVKLKLddTDKQKSLLDDELQRLKDEVDDavkQRGQVEEELFk 3057
Cdd:PRK10929 170 LAQAQltALQAESAALKaLVDELELAQlSANNRQELARLRSEL--AKKRSQQLDAYLQALRNQLNS---QRQREAERAL- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3058 vkvqmeellklklriedENQRLLKKDKDNSQKFLAEEAENMKRLAEDaarLSVESQE----AARLRQIAEDdlIQQRALA 3133
Cdd:PRK10929 244 -----------------ESTELLAEQSGDLPKSIVAQFKINRELSQA---LNQQAQRmdliASQQRQAASQ--TLQVRQA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3134 DKMLKEKMQAIQESSRLkAEA---------EMLQRQK---DLAQEQAQKL----LEDKQLMQRRLEEE-----TEEYQKS 3192
Cdd:PRK10929 302 LNTLREQSQWLGVSNAL-GEAlraqvarlpEMPKPQQldtEMAQLRVQRLryedLLNKQPQLRQIRQAdgqplTAEQNRI 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3193 LEAERRRQLEI-----------VAEAEKLKLQVSQLSEAQTKAEEEAKKF 3231
Cdd:PRK10929 381 LDAQLRTQRELlnsllsggdtlILELTKLKVANSQLEDALKEVNEATHRY 430
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2521-3217 |
4.65e-08 |
|
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: 59.77 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2521 KDMAEKELERQRKVADSTAQQKLTAEQELIR----LRADFDNAEQQRSlledelyrlknEVIAAQ-QQRKQLEDELAKVR 2595
Cdd:pfam07111 18 QDVLERRLDTQRPTVTMWEQDVSGDGQGPGRrgrsLELEGSQALSQQA-----------ELISRQlQELRRLEEEVRLLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2596 -SEMDILIQLKSKA-EKETMSNTEKSKQlleAEATKMRDVAEEAGKLRAIAEEAKHqrqvaeeeaaRQRAEAERILKEKL 2673
Cdd:pfam07111 87 eTSLQQKMRLEAQAmELDALAVAEKAGQ---AEAEGLRAALAGAEMVRKNLEEGSQ----------RELEEIQRLHQEQL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2674 AAISEAthlkteAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDaEMERQKAMVDDTlkq 2753
Cdd:pfam07111 154 SSLTQA------HEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQE-ELEAQVTLVESL--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2754 RRVVEEEIrilkLNFEKASSGKLDLELELNKLKNIAEEtqQSKLRAEEEAEKLRKLALEeekrrreaeekvkKITAAEEE 2833
Cdd:pfam07111 224 RKYVGEQV----PPEVHSQTWELERQELLDTMQHLQED--RADLQATVELLQVRVQSLT-------------HMLALQEE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2834 AARQRKIAQDELE-RLKKKAEEARKQKDEADVEAEVQIVAAQ------QAALKCSTAEHQVQsVLAQQKEDSIMHKKLKQ 2906
Cdd:pfam07111 285 ELTRKIQPSDSLEpEFPKKCRSLLNRWREKVFALMVQLKAQDlehrdsVKQLRGQVAELQEQ-VTSQSQEQAILQRALQD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2907 EYEKAKKLAKEAEAAKEKAEREAALLR---QQAEEAERQ-KAAAEQEAAIQAKAQEDAERLrKEAEFEAAKRAQAEGAAL 2982
Cdd:pfam07111 364 KAAEVEVERMSAKGLQMELSRAQEARRrqqQQTASAEEQlKFVVNAMSSTQIWLETTMTRV-EQAVARIPSLSNRLSYAV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2983 KQKQQADAEMAKHKKLAE---QTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQR----LKDEVDDAvKQRGQVEEel 3055
Cdd:pfam07111 443 RKVHTIKGLMARKVALAQlrqESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLsahlIQQEVGRA-REQGEAER-- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3056 fkvkvqmEELLKLKLRIEDENQRllkkdkdnSQKFLAEEAENMkrlaEDAARLSVES-QEAARLRQiaedDLIQQRALAD 3134
Cdd:pfam07111 520 -------QQLSEVAQQLEQELQR--------AQESLASVGQQL----EVARQGQQEStEEAASLRQ----ELTQQQEIYG 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3135 KMLKEKMQAIQesSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQ--KSLEAERRRQleivaEAEKLKL 3212
Cdd:pfam07111 577 QALQEKVAEVE--TRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQelRRLQDEARKE-----EGQRLAR 649
|
....*
gi 1678729579 3213 QVSQL 3217
Cdd:pfam07111 650 RVQEL 654
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2441-2748 |
5.26e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 59.14 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2441 QQEAAHLKKQQEdAINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQ 2520
Cdd:pfam07888 40 LQERAELLQAQE-AANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2521 KDMAEKELERQR-----KVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVR 2595
Cdd:pfam07888 119 ALLAQRAAHEARireleEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2596 SEMD----ILIQLKSKAEKETMSNTEKSKQLLEAEATK--MRDVAEEAGKLRAIAEEAKhqRQVAEEEAARQRAEAEriL 2669
Cdd:pfam07888 199 NSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLeeLRSLQERLNASERKVEGLG--EELSSMAAQRDRTQAE--L 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2670 KEKLAAISEATHLKTEAEIALKEKEA----ENERLRRAAEDEAYQRKALEDEANQHKKEIEEkivqlkkssdAEMERQKA 2745
Cdd:pfam07888 275 HQARLQAAQLTLQLADASLALREGRArwaqERETLQQSAEADKDRIEKLSAELQRLEERLQE----------ERMEREKL 344
|
...
gi 1678729579 2746 MVD 2748
Cdd:pfam07888 345 EVE 347
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5212-5250 |
6.32e-08 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 51.56 E-value: 6.32e-08
10 20 30
....*....|....*....|....*....|....*....
gi 1678729579 5212 FLEVQYLTGGLIEPDVESRVSLDESIKKGSIDARTAQKL 5250
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2605-3125 |
7.62e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2605 KSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEE-AKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLK 2683
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2684 TEAEIALKEKEAENERLRRAAEDEAYQRKALEdEANQHKKEIEEKIVQLKKSSDAEMERQkamVDDTLKQRRVVEEEIRI 2763
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2764 LKLNFEKASSGKLDLELELNKLKNIAEETQQSKlRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRkIAQD 2843
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG-LLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2844 ELERLKKKAEEARKQKDEADVEAEVQIVAAQQaalkcstaehqvqsvlaqqkedsimHKKLKQEYEKAKKLAKEAEAAKE 2923
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEE-------------------------LEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2924 KAEREAALLRQQAEEAERQkaaaeqeaaiqakAQEDAERLRKEAEFEAAKRAQAEG--AALKQKQQADAEMAKHKKLAEq 3001
Cdd:COG4717 344 DRIEELQELLREAEELEEE-------------LQLEELEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEE- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3002 tlkqkfQVEQELTKVKLKLDDTDKQKslLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKlklriEDENQRLLK 3081
Cdd:COG4717 410 ------QLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQ 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1678729579 3082 KdkdnsqkfLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDD 3125
Cdd:COG4717 477 E--------LEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4860-4896 |
7.91e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 51.33 E-value: 7.91e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1678729579 4860 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGFFDEEM 4896
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2076-2727 |
8.12e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.88 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2076 KTLKEQLSQEKKLLEEIENN-------KDNVDECQKYAKAYINSIKDyelQLVAYNAQADPLASPLKKTKLDSASDNiiq 2148
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNlnkdeekINNSNNKIKILEQQIKDLND---KLKKNKDKINKLNSDLSKINSEIKNDK--- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2149 eyvtlrtryselmtltsqyikfitETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELK 2228
Cdd:TIGR04523 117 ------------------------EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2229 LMMKEevnrreiaavdAEKQKQNIQlelHELKNLSEQQIKDKGQL--VDEALQSRTKIEEEIYLIRIQLETTVKQKSTAE 2306
Cdd:TIGR04523 173 NELNL-----------LEKEKLNIQ---KNIDKIKNKLLKLELLLsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2307 SELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETqkkriaeKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEA-ERQ 2385
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ-------KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwNKE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2386 VKQAEVEKERQIKVAhvaaqKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKEL 2465
Cdd:TIGR04523 312 LKSELKNQEKKLEEI-----QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2466 EKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKK------RAKAEESALKQKDMA-EKELERQRKVADST 2538
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlketiiKNNSEIKDLTNQDSVkELIIKNLDNTRESL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2539 AQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMS---- 2614
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDlede 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2615 ----NTEKSKQLLEAEatkMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEklaaISEATHLKTEAEIAL 2690
Cdd:TIGR04523 547 lnkdDFELKKENLEKE---IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE----IEEKEKKISSLEKEL 619
|
650 660 670
....*....|....*....|....*....|....*..
gi 1678729579 2691 KEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEE 2727
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
861-970 |
8.15e-08 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 53.66 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 861 EDERDrvqKKTFTKWVNKHLIKRaesqhHVTDLYEDLRDGHNLISLLEVLSGDTLPREKG-----RMRFHKLQNVQIALD 935
Cdd:cd21299 1 ETSRE---ERCFRLWINSLGIDT-----YVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVK 72
|
90 100 110
....*....|....*....|....*....|....*
gi 1678729579 936 FLRHRQVKLVNIRNDDIADGNPKLTLGLIWTVILH 970
Cdd:cd21299 73 IGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2932-3321 |
9.03e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2932 LRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAA------------KRAQAEGAALKQKQQADAEMAKHKKLA 2999
Cdd:COG4717 100 LEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaelperleeleERLEELRELEEELEELEAELAELQEEL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3000 EQTLKQK-FQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQmEELLKLKLRIEDENQR 3078
Cdd:COG4717 180 EELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAAAL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3079 LLKKDKDNSQKFLAEE---------------AENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRA-------LADKM 3136
Cdd:COG4717 259 LALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalglppdLSPEE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3137 LKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQKlledKQLMQRRLEEETEEYQKSLEAERRRQlEIVAEAEKLKLQVSQ 3216
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEELQLEELEQEI----AALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3217 LSEaqtkaEEEAKKFKKQADKIAARLHETEIAtkekmtvVEKLEFERLNTSKEAGDLRDAIADLEKDK--ARLKKEAEEL 3294
Cdd:COG4717 414 LLG-----ELEELLEALDEEELEEELEELEEE-------LEELEEELEELREELAELEAELEQLEEDGelAELLQELEEL 481
|
410 420 430
....*....|....*....|....*....|...
gi 1678729579 3295 QNKSKEMA------DAQQKQIEHEKTLLQQTFL 3321
Cdd:COG4717 482 KAELRELAeewaalKLALELLEEAREEYREERL 514
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
860-961 |
9.19e-08 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 53.75 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 860 IEDERDRVQ--KKTFTKWVNKHLikrAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLP----REKGRMRFHKLQNVQIA 933
Cdd:cd21222 7 FDEAPEKLAevKELLLQFVNKHL---AKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLA 83
|
90 100
....*....|....*....|....*...
gi 1678729579 934 LDFLRHRQVKLVNIRNDDIADGNPKLTL 961
Cdd:cd21222 84 LELMEDAGISTPKIRPEDIVNGDLKSIL 111
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2457-3177 |
9.54e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.98 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2457 AREEAEKELEKWRQKANEaLRLRLQAEEEAHKK-------SLAQEDAEKQKEEAEREA-----KKRAKAEESALKQKDMA 2524
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKD-LQRRLNESNELHEKqkfylrqSVIDLQTKLQEMQMERDAmadirRRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2525 EKELE-----RQRKVADSTAQ------QKLTAE---QELIRLRADFDNAEQQRSLLEDELYRL--KNEVIAAQQQRKQLE 2588
Cdd:pfam15921 151 VHELEaakclKEDMLEDSNTQieqlrkMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2589 DELAKVRSEM----DILIQLKSKAEKET----MSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAAR 2660
Cdd:pfam15921 231 TEISYLKGRIfpveDQLEALKSESQNKIelllQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2661 QRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQL-------K 2733
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhkrE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2734 KSSDAEMERQKAMVD-DT------------LKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEEtQQSKLRAE 2800
Cdd:pfam15921 391 KELSLEKEQNKRLWDrDTgnsitidhlrreLDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLE-KVSSLTAQ 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2801 EEAEK--LRKLA---LEEEKRRREAEEKVKKITAAEEEAARQRKIAQDELERLKK----KAEEARKQKDEADveaEVQIV 2871
Cdd:pfam15921 470 LESTKemLRKVVeelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSrvdlKLQELQHLKNEGD---HLRNV 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2872 AAQQAALKCSTAEH-QVQSVLAQQKEDsiMHKKLKQEyekakklakeaeaakeKAEREAALLRQQAEEAERQKAAAEQEA 2950
Cdd:pfam15921 547 QTECEALKLQMAEKdKVIEILRQQIEN--MTQLVGQH----------------GRTAGAMQVEKAQLEKEINDRRLELQE 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2951 AIQAKAQEDAERLRKEA-----EFEAAKRAQAEGAALKQ----KQQADAEMAKHK-------KLAE--QTLKQKFQ---V 3009
Cdd:pfam15921 609 FKILKDKKDAKIRELEArvsdlELEKVKLVNAGSERLRAvkdiKQERDQLLNEVKtsrnelnSLSEdyEVLKRNFRnksE 688
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3010 EQELTKVKLKLDDTDKQKSL--LDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEElLKLKLRIEDENQRLLKKDKdns 3087
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQSELeqTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKEK--- 764
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3088 qKFLAEEAenmKRLAEDAARLSVESQEAARLRQIAEDdliQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQ-KDLAQE 3166
Cdd:pfam15921 765 -HFLKEEK---NKLSQELSTVATEKNKMAGELEVLRS---QERRLKEKVANMEVALDKASLQFAECQDIIQRQeQESVRL 837
|
810
....*....|.
gi 1678729579 3167 QAQKLLEDKQL 3177
Cdd:pfam15921 838 KLQHTLDVKEL 848
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2259-2740 |
9.98e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 58.68 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2259 LKNLSEQqIKDKGQLVDEaLQSRTKieeeiyliriQLETtvkQKSTAESELKQLRERAAEAERlrkvaqeeaeklhkqVI 2338
Cdd:pfam10174 403 IENLQEQ-LRDKDKQLAG-LKERVK----------SLQT---DSSNTDTALTTLEEALSEKER---------------II 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2339 EETQKKRiaekelqhkseaekeaAKQKQKALDDLENLKKQAEEAERQVKQAEVEKerqikvahvAAQKSAAAELQSKHSS 2418
Cdd:pfam10174 453 ERLKEQR----------------EREDRERLEELESLKKENKDLKEKVSALQPEL---------TEKESSLIDLKEHASS 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2419 FVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAekelekwRQKANEALRLRLQAEEEAHKKslaqEDAEK 2498
Cdd:pfam10174 508 LASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAV-------RTNPEINDRIRLLEQEVARYK----EESGK 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2499 QKEEAER--EAKKRAKAEESaLKQKDMAEKELERQRKVADST--AQQKLTAEQElirlradfdnaEQQRSLLEDELYRLK 2574
Cdd:pfam10174 577 AQAEVERllGILREVENEKN-DKDKKIAELESLTLRQMKEQNkkVANIKHGQQE-----------MKKKGAQLLEEARRR 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2575 NEVIAAQQQRKQLED---ELAKVRSEMDiliqlkskAEKETMSNTEKSKQLLEAEATKMRdvaeeagklraiaeeakHQR 2651
Cdd:pfam10174 645 EDNLADNSQQLQLEElmgALEKTRQELD--------ATKARLSSTQQSLAEKDGHLTNLR-----------------AER 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2652 QVAEEEAARQRAEAerilkeKLAAISEathlkTEAEIALKEKEAENerlrraaedeayqRKALEDEANQHKKEIEEKIVQ 2731
Cdd:pfam10174 700 RKQLEEILEMKQEA------LLAAISE-----KDANIALLELSSSK-------------KKKTQEEVMALKREKDRLVHQ 755
|
....*....
gi 1678729579 2732 LKKSSDAEM 2740
Cdd:pfam10174 756 LKQQTQNRM 764
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2381-2712 |
1.11e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 57.62 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2381 EAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSK--LEESLKQEHGAVLQLQQEAAHLKKQ----QEDA 2454
Cdd:pfam13868 10 ELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEEREraLEEEEEKEEERKEERKRYRQELEEQieerEQKR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2455 INAREEAEKE----LEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALK--QKDMAEKEL 2528
Cdd:pfam13868 90 QEEYEEKLQEreqmDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILeyLKEKAEREE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2529 ERQRKVadstAQQKLTAEQELIRLRADFDNAEQQRslleDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKsKA 2608
Cdd:pfam13868 170 EREAER----EEIEEEKEREIARLRAQQEKAQDEK----AERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQ-QA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2609 EKETMSNTEKSKQlleaeATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEkLAAISEATHLKTEAEI 2688
Cdd:pfam13868 241 REEQIELKERRLA-----EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ-IEEREEQRAAEREEEL 314
|
330 340
....*....|....*....|....
gi 1678729579 2689 ALKEKEAENERLRRAAEDEAYQRK 2712
Cdd:pfam13868 315 EEGERLREEEAERRERIEEERQKK 338
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2178-2573 |
1.14e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.81 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2178 LEDEEKAAKKLKAEEQKKMAEMQAELDkqkQLAAAHAKAIAKAEKEAQELKLMM-----KEEVNRR----EIAAVDAEKQ 2248
Cdd:COG3096 290 LRRELFGARRQLAEEQYRLVEMARELE---ELSARESDLEQDYQAASDHLNLVQtalrqQEKIERYqedlEELTERLEEQ 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2249 KQNI------QLELHELKNLSEQQIKD-KGQLVD-----EALQSRTkieeeiylirIQLETTVKQKSTAEsELKQLRERA 2316
Cdd:COG3096 367 EEVVeeaaeqLAEAEARLEAAEEEVDSlKSQLADyqqalDVQQTRA----------IQYQQAVQALEKAR-ALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2317 AE-AERLRKVAQEEAEKLHKQVIEETQKKRIAEkelqhkseaekEAAKQKQKAlddLENLKKQAEEAER----QVKQAEV 2391
Cdd:COG3096 436 PEnAEDYLAAFRAKEQQATEEVLELEQKLSVAD-----------AARRQFEKA---YELVCKIAGEVERsqawQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2392 EKERQIKvaHVAAQKSAaaeLQSKHssfvektSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINA---REEAEKELEKW 2468
Cdd:COG3096 502 RRYRSQQ--ALAQRLQQ---LRAQL-------AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELeelLAELEAQLEEL 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2469 RQKANEAL--RLRLQAEEEAHKkslaqedaEKQKEEAEREAKKRAkAEESALKQKDMAEKELERQRKVaDSTAQQKLTAE 2546
Cdd:COG3096 570 EEQAAEAVeqRSELRQQLEQLR--------ARIKELAARAPAWLA-AQDALERLREQSGEALADSQEV-TAAMQQLLERE 639
|
410 420
....*....|....*....|....*..
gi 1678729579 2547 QELIRLRadfDNAEQQRSLLEDELYRL 2573
Cdd:COG3096 640 REATVER---DELAARKQALESQIERL 663
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2727-3408 |
1.14e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.58 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2727 EKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASsgkLDLELELNKLKNIAEETQQSklraeeeaekl 2806
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVS---LKLEEEIQENKDLIKENNAT----------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2807 RKLALEEEKRRREAEEKVKKITAAEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEaevqivaaqqaalkcstaehq 2886
Cdd:pfam05483 154 RHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLE--------------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2887 vqsvlaqqkedsiMHKKLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAE-RQKAAAEQEAAIQAKAQEDAERLRK 2965
Cdd:pfam05483 213 -------------MHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKEnKMKDLTFLLEESRDKANQLEEKTKL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2966 EAEfeaAKRAQAEGAALKQKQQADAEMAKHKKLAEQ-TLKQKFQVEQ----ELTKVK-LKLDDTDKQKS----------- 3028
Cdd:pfam05483 280 QDE---NLKELIEKKDHLTKELEDIKMSLQRSMSTQkALEEDLQIATkticQLTEEKeAQMEELNKAKAahsfvvtefea 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3029 -------LLDDELQRLKDEVDdavkQRGQVEEELFKVKVQMEELLKLKLRIEDENQRlLKKDKDNSQKFLaEEAENMKRL 3101
Cdd:pfam05483 357 ttcsleeLLRTEQQRLEKNED----QLKIITMELQKKSSELEEMTKFKNNKEVELEE-LKKILAEDEKLL-DEKKQFEKI 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3102 AEDaarLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQ-RQKDLAQEQAQKLLEDKQLMQr 3180
Cdd:pfam05483 431 AEE---LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHCDKLLLENKELTQ- 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3181 rleeETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEE----AKKFKKQADKIAARLHETEIATKEKMTVV 3256
Cdd:pfam05483 507 ----EASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDElesvREEFIQKGDEVKCKLDKSEENARSIEYEV 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3257 EKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKemadAQQKQIEHEKTLLQQTFLteremllkkekliee 3336
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS----AENKQLNAYEIKVNKLEL--------------- 643
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678729579 3337 EKKKLESQFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMLSKQKEMQELEKKRLEQ 3408
Cdd:pfam05483 644 ELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2516-2720 |
1.17e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2516 SALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAK-- 2593
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2594 --------VRSEMDILiqLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEeagkLRAIAEEAKHQRQVAEEEAARQRAEA 2665
Cdd:COG3883 93 ralyrsggSVSYLDVL--LGSESFSDFLDRLSALSKIADADADLLEELKA----DKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678729579 2666 ERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQ 2720
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2318-2675 |
1.18e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 58.04 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2318 EAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKERQi 2397
Cdd:pfam15709 164 TPASISHAERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERN- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2398 kvAHVAAQKSAAAELQSKHS-------SFVEKTSKLEESLKQEHGAvlQLQQEAAHLKKQQEDAINAREEAEKELEKWRQ 2470
Cdd:pfam15709 243 --LEVAAELSGPDVINSKETedasergAFSSDSVVEDPWLSSKYDA--EESQVSIDGRSSPTQTFVVTGNMESEEERSEE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2471 KANEALRLRLQAEEEAHKKsLAQEDAEKQKEEAEReaKKRAKAEESALKQK-----DMAEKELERQrkvadstaQQKLTA 2545
Cdd:pfam15709 319 DPSKALLEKREQEKASRDR-LRAERAEMRRLEVER--KRREQEEQRRLQQEqleraEKMREELELE--------QQRRFE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2546 EqelIRLRADFDNAEQQRSLLEDELYRLKNEviAAQQQRKQLEDELAKVrsemdiLIQLKSKAEKETMSNTEKSKQLLEA 2625
Cdd:pfam15709 388 E---IRLRKQRLEEERQRQEEEERKQRLQLQ--AAQERARQQQEEFRRK------LQELQRKKQQEEAERAEAEKQRQKE 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1678729579 2626 EATKMrdvAEEAGKLRAIAEEAK--HQRQVAEEEAARQRAEAERILKEKLAA 2675
Cdd:pfam15709 457 LEMQL---AEEQKRLMEMAEEERleYQRQKQEAEEKARLEAEERRQKEEEAA 505
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2053-2753 |
1.28e-07 |
|
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: 58.91 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2053 LIHWITDAKERQEKIQAVSITDSKTLKEQLSQE---------KKLLEEIENNKDNVDECQKYAKAY-------------- 2109
Cdd:TIGR01612 1031 IEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEigkniellnKEILEEAEINITNFNEIKEKLKHYnfddfgkeenikya 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2110 --INSIKDyelQLVAYNAQADPLASPLKKTKldSASDNIIQEyvtLRTRYSELMTLTSQYI--KFITETQRRLED--EEK 2183
Cdd:TIGR01612 1111 deINKIKD---DIKNLDQKIDHHIKALEEIK--KKSENYIDE---IKAQINDLEDVADKAIsnDDPEEIEKKIENivTKI 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2184 AAKKLKAEEQKKMAEMQAELDKQKqlaaahakaiaKAEKEAQELKLMMKEEVNRREIAAVDAEKQKQNIQLELHE--LKN 2261
Cdd:TIGR01612 1183 DKKKNIYDEIKKLLNEIAEIEKDK-----------TSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEayIED 1251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2262 LSEqqIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLRERAaeaERLRKVAQEEAEKLHKQVIEET 2341
Cdd:TIGR01612 1252 LDE--IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIR---EKSLKIIEDFSEESDINDIKKE 1326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2342 QKKRIAEKElQHKSEAEKEAAK-----------QKQKALDDLENLKKQAEEAERQVKQAEVEKERQIKVAhvaaqksaaa 2410
Cdd:TIGR01612 1327 LQKNLLDAQ-KHNSDINLYLNEianiynilklnKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKI---------- 1395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2411 elqSKHSSFVEKTSKLEESL--KQEHGAVLQLQQEAAHLKKQQEDA----INAREEAE------KELEKWRQKANEALRL 2478
Cdd:TIGR01612 1396 ---KDDINLEECKSKIESTLddKDIDECIKKIKELKNHILSEESNIdtyfKNADENNEnvlllfKNIEMADNKSQHILKI 1472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2479 RLQAEEEAHKKSLAQEDAEKQKEEAER-EAKKRAKAEESalkqkdmaEKELERQRKVADSTAQQKLTAeqelIRLRADFD 2557
Cdd:TIGR01612 1473 KKDNATNDHDFNINELKEHIDKSKGCKdEADKNAKAIEK--------NKELFEQYKKDVTELLNKYSA----LAIKNKFA 1540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2558 NAEQQRSLLEDELYRLKNEVIAaqqQRKQLEDELAKVRSEMdilIQLKSKAEKETMSNT-----EKSKQLLEAEATKMRD 2632
Cdd:TIGR01612 1541 KTKKDSEIIIKEIKDAHKKFIL---EAEKSEQKIKEIKKEK---FRIEDDAAKNDKSNKaaidiQLSLENFENKFLKISD 1614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2633 VAEEAGKlrAIAEEAKHQRQVAEEEAARQRAEaeriLKEKLAAISEathLKTEAEiALKEKEAENERLRRAAEDEAYQRK 2712
Cdd:TIGR01612 1615 IKKKIND--CLKETESIEKKISSFSIDSQDTE----LKENGDNLNS---LQEFLE-SLKDQKKNIEDKKKELDELDSEIE 1684
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1678729579 2713 ALEDEANQHKKEIE----EKIVQLKKSSDAEMERQKAMVDDTLKQ 2753
Cdd:TIGR01612 1685 KIEIDVDQHKKNYEigiiEKIKEIAIANKEEIESIKELIEPTIEN 1729
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2440-3015 |
1.40e-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: 58.12 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2440 LQQEAAHLKKQQEDAINAREEAEKELEKWRqKANEALRLRLQ-AEEEAHKkslAQEDAEKQKEEAErEAKKRAKAEESAL 2518
Cdd:pfam05701 47 VQEEIPEYKKQSEAAEAAKAQVLEELESTK-RLIEELKLNLErAQTEEAQ---AKQDSELAKLRVE-EMEQGIADEASVA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2519 KQkdmAEKELERQRKVAdstaqqkltAEQELIRLRADFDNAEQQRSLLEDE----LYRLKNEVIAAQQQRKQLEDELAKV 2594
Cdd:pfam05701 122 AK---AQLEVAKARHAA---------AVAELKSVKEELESLRKEYASLVSErdiaIKRAEEAVSASKEIEKTVEELTIEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2595 rsemdiliqLKSKAEKETMSNTEkskqlLEAEATKMRDV-AEEAGKLRAIAEeakhqRQVAEEEAARQRAE--AERILKE 2671
Cdd:pfam05701 190 ---------IATKESLESAHAAH-----LEAEEHRIGAAlAREQDKLNWEKE-----LKQAEEELQRLNQQllSAKDLKS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2672 KLAAISEATH-LKTE----AEIALKEKEAENERLRRAAEDE----AYQRKALED-EANQHKKEIEEKIVQLKKSS-DAEM 2740
Cdd:pfam05701 251 KLETASALLLdLKAElaayMESKLKEEADGEGNEKKTSTSIqaalASAKKELEEvKANIEKAKDEVNCLRVAAASlRSEL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2741 ERQKAMVdDTLKQRRvveeeirilklnfEKASSGKLDLELELNKLKniaEETQQSKLRAEEEAEKLRKLAleeekrrrea 2820
Cdd:pfam05701 331 EKEKAEL-ASLRQRE-------------GMASIAVSSLEAELNRTK---SEIALVQAKEKEAREKMVELP---------- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2821 eekvKKITAAEEEAARQRKIAQDELERLKKKAEEARKQKDEAD-VEAEVQIV--------AAQQAALKCSTA-EHQVQSV 2890
Cdd:pfam05701 384 ----KQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAAStVESRLEAVlkeieaakASEKLALAAIKAlQESESSA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2891 LAQQKEDSIMHKKLK-QEYEKakklakeaeaakekaereaalLRQQAEEAERQKAAAEQEAAIQAKAQEDAE-----RLr 2964
Cdd:pfam05701 460 ESTNQEDSPRGVTLSlEEYYE---------------------LSKRAHEAEELANKRVAEAVSQIEEAKESElrsleKL- 517
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 2965 KEAEFEAAKRAQAEGAALKQkqqadAEMAKHKKLAeqtlkqkfqVEQELTK 3015
Cdd:pfam05701 518 EEVNREMEERKEALKIALEK-----AEKAKEGKLA---------AEQELRK 554
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2425-2786 |
1.40e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 58.53 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2425 KLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRL--RLQAEEEAHKKSLAQEDAEKQKEE 2502
Cdd:PRK10929 27 QITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNFPKLsaELRQQLNNERDEPRSVPPNMSTDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2503 AEREAkkrAKAEESALKQKDMAEKELERQRKVADSTAQqkLTAEQ-ELIRLRADFDN------------AEQQRSLLEDE 2569
Cdd:PRK10929 107 LEQEI---LQVSSQLLEKSRQAQQEQDRAREISDSLSQ--LPQQQtEARRQLNEIERrlqtlgtpntplAQAQLTALQAE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2570 LYRLK---NEVIAAQ------QQRKQLEDELAKVRSE-MDILIQ-----LKSKAEKETMSNTEKSKQLLEAEATKMRDVA 2634
Cdd:PRK10929 182 SAALKalvDELELAQlsannrQELARLRSELAKKRSQqLDAYLQalrnqLNSQRQREAERALESTELLAEQSGDLPKSIV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2635 EEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAaiseathLKTEAEIA--LKEKEAENERLR----RAAEDEA 2708
Cdd:PRK10929 262 AQFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQA-------LNTLREQSqwLGVSNALGEALRaqvaRLPEMPK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2709 YQRkaLEDEANQ------HKKEIEEKIVQLKKSsdaemeRQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELEL 2782
Cdd:PRK10929 335 PQQ--LDTEMAQlrvqrlRYEDLLNKQPQLRQI------RQADGQPLTAEQNRILDAQLRTQRELLNSLLSGGDTLILEL 406
|
....
gi 1678729579 2783 NKLK 2786
Cdd:PRK10929 407 TKLK 410
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2524-2746 |
1.41e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2524 AEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQ 2603
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2604 lkskAEKETMSNTEKSKQLLEAEatkmrDVAEEAGKLRAIAEEAKHQRQV------AEEEAARQRAEAERILKEKLAAIS 2677
Cdd:COG3883 94 ----ALYRSGGSVSYLDVLLGSE-----SFSDFLDRLSALSKIADADADLleelkaDKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678729579 2678 EATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAM 2746
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2303-2545 |
1.71e-07 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 57.30 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2303 STAESELKQLRERAAEaeRLRKVAQEE-AEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQK--QKALDDLENLKKQA 2379
Cdd:PRK07735 1 MDPEKDLEDLKKEAAR--RAKEEARKRlVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRaaAAAKAKAAALAKQK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2380 EEAERQVKQAEVEKErqiKVAHVAAQKSAAAELQSKHSSFVEKTSKlEESLKQEHGAVLQLQQEAAHLKKQQEDAIN--A 2457
Cdd:PRK07735 79 REGTEEVTEEEKAKA---KAKAAAAAKAKAAALAKQKREGTEEVTE-EEKAAAKAKAAAAAKAKAAALAKQKREGTEevT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2458 REEAEKELEKWRQKANEALRLRLQAeEEAHKKSLAQEDAEKQKEEAEREAKKR----AKAEESAL-KQK-----DMAEKE 2527
Cdd:PRK07735 155 EEEEETDKEKAKAKAAAAAKAKAAA-LAKQKAAEAGEGTEEVTEEEKAKAKAKaaaaAKAKAAALaKQKasqgnGDSGDE 233
|
250
....*....|....*...
gi 1678729579 2528 LERQRKVADSTAQQKLTA 2545
Cdd:PRK07735 234 DAKAKAIAAAKAKAAAAA 251
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2167-2728 |
1.90e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.99 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2167 YIKFITETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLaaahakaiakaekeAQELKLMM--KEEVNRREIAAVD 2244
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNL--------------KSALNELSslEDMKNRYESEIKT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2245 AEKQKQNIQLELHELKNLSEQQIKDKGqlvDEALQSRTKIEEEIYLIRiQLETTVKQKSTAESELKQLRERAAEAERLrk 2324
Cdd:PRK01156 261 AESDLSMELEKNNYYKELEERHMKIIN---DPVYKNRNYINDYFKYKN-DIENKKQILSNIDAEINKYHAIIKKLSVL-- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2325 vaqeeaEKLHKQVIEETQKKriaeKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKERQIKVAHVAA 2404
Cdd:PRK01156 335 ------QKDYNDYIKKKSRY----DDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2405 Q--KSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAA---------------------HLKKQQEDAINAREEA 2461
Cdd:PRK01156 405 DaiKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeeksnHIINHYNEKKSRLEEK 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2462 EKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADStaqq 2541
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKL---- 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2542 kltaeQELIRLRADFDNAEQQRSLLEDELYRLKNEVIaaQQQRKQLEDELAKVRSEMDiliqlkskaekETMSNTEKSKQ 2621
Cdd:PRK01156 561 -----EDLDSKRTSWLNALAVISLIDIETNRSRSNEI--KKQLNDLESRLQEIEIGFP-----------DDKSYIDKSIR 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2622 LLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRaEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLR 2701
Cdd:PRK01156 623 EIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLE 701
|
570 580
....*....|....*....|....*..
gi 1678729579 2702 RAAEDEAYQRKALEDEANQHKKEIEEK 2728
Cdd:PRK01156 702 STIEILRTRINELSDRINDINETLESM 728
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2306-2808 |
1.90e-07 |
|
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: 57.99 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2306 ESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKS----------EAEKEAAKQKQKALDDLENL 2375
Cdd:pfam15964 127 EAEVKFCKEELSEMKQRVQVVVLENEKLQQELKSQTQEETLREQTLLDSSgnmqnswctpEDSRVHQTSKRPASHNLAER 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2376 KKQAEEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQ---------------------EH 2434
Cdd:pfam15964 207 LKSATTGEDEKWRLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDLKERLKHkeslvaastssrvgglclkcaQH 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2435 GAVLQLQQEAAH------LKKQQEDAINAREEAEKELEKWRQK---ANEALRLRLQAEEEAH-KKSLAQEDAEKQKEEAE 2504
Cdd:pfam15964 287 EAVLAQTHTNVHmqtierLTKERDDLMSALVSVRSSLAEAQQRessAYEQVKQAVQMTEEANfEKTKALIQCEQLKSELE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2505 REA----KKRAKAEESALKQKDMAEKELERQRKVADSTAqqkLTAEQELIRLRADFDNAEQQRSlledelyRLKNEVIAA 2580
Cdd:pfam15964 367 RQKerleKELASQQEKRAQEKEALRKEMKKEREELGATM---LALSQNVAQLEAQVEKVTREKN-------SLVSQLEEA 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2581 QQQRKQLEDELAKVRSEMDILIQlKSKAEKEtmsntEKSKQLLEAEATKMRDVA---EEAGKLRAIAEEAKHQRQVAEEE 2657
Cdd:pfam15964 437 QKQLASQEMDVTKVCGEMRYQLN-QTKMKKD-----EAEKEHREYRTKTGRQLEikdQEIEKLGLELSESKQRLEQAQQD 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2658 AARQRAEAERIlkeklaaiseaTHLKTEAEIALKEKEAENERLRRAAEDEAyqrKALEDEANQHKKEIEEKIVQLKKSSD 2737
Cdd:pfam15964 511 AARAREECLKL-----------TELLGESEHQLHLTRLEKESIQQSFSNEA---KAQALQAQQREQELTQKMQQMEAQHD 576
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 2738 AEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASsgkldlelelNKLKNIAEETQQSKLRAEEEAEKLRK 2808
Cdd:pfam15964 577 KTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEIT----------QKSRSEVEQLSQEKEYLQDRLEKLQK 637
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2831-3022 |
2.02e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.12 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2831 EEEAARQRKIAQDELERL-----KKKAEEARKQKDEADVEA-EVQIVAAQQAALKCSTAEHQVQSVLAQQKEDSimhKKL 2904
Cdd:PRK09510 94 QKQAAEQERLKQLEKERLaaqeqKKQAEEAAKQAALKQKQAeEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEA---KKK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2905 KQEYEKAKKLAKEaeaakekaereaallRQQAEEAERQKaaaeQEAAIQAKAQEDAErlrKEAEFEAAKRAQAEGAALKQ 2984
Cdd:PRK09510 171 AEAEAAKKAAAEA---------------KKKAEAEAAAK----AAAEAKKKAEAEAK---KKAAAEAKKKAAAEAKAAAA 228
|
170 180 190
....*....|....*....|....*....|....*...
gi 1678729579 2985 KQQADAemakhKKLAEQTLKQKFQVEQELTKVKLKLDD 3022
Cdd:PRK09510 229 KAAAEA-----KAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2246-2415 |
2.03e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.12 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2246 EKQKQNIQLELHELKNLSEQQIKdkgQLVDEALQSRTKIEEEIYLIRIQLEttvKQKSTAESELKQLRERAAEAERLRKV 2325
Cdd:PRK09510 82 KKKEQQQAEELQQKQAAEQERLK---QLEKERLAAQEQKKQAEEAAKQAAL---KQKQAEEAAAKAAAAAKAKAEAEAKR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2326 AQEEAeklhKQVIEETQKKRIAEKELQHKSEAEKEA-AKQKQKALDDLEnlKKQAEEAERQVKQAEVEK---ERQIKVAH 2401
Cdd:PRK09510 156 AAAAA----KKAAAEAKKKAEAEAAKKAAAEAKKKAeAEAAAKAAAEAK--KKAEAEAKKKAAAEAKKKaaaEAKAAAAK 229
|
170
....*....|....
gi 1678729579 2402 VAAQKSAAAELQSK 2415
Cdd:PRK09510 230 AAAEAKAAAEKAAA 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2762-3242 |
2.04e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2762 RILKLNFEKASSGKLDLELELNKLKNIAEETQQ-SKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRKI 2840
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2841 AQDELERLKKKAEEARkqkdeadvEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKEDSImhKKLKQEYEKAKKLAKEAEA 2920
Cdd:COG4717 144 LPERLEELEERLEELR--------ELEEELEELEAELAELQEELEELLEQLSLATEEEL--QDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2921 AKEKAEREAALLRQQAEEAERQKAaaeqeaaiqakAQEDAERLRKEAEFEAAKRAQAEGAAL------------------ 2982
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELE-----------AAALEERLKEARLLLLIAAALLALLGLggsllsliltiagvlflv 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2983 ------------KQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQ 3050
Cdd:COG4717 283 lgllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3051 VEEElfkvkvqmeellklklRIEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDAARLsveSQEAARLRQIAEDDLIQQR 3130
Cdd:COG4717 363 LQLE----------------ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3131 ALADKMLKEKMQAIQES-SRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAek 3209
Cdd:COG4717 424 ALDEEELEEELEELEEElEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALEL-- 501
|
490 500 510
....*....|....*....|....*....|....
gi 1678729579 3210 lklqvsqLSEAQTKAEEE-AKKFKKQADKIAARL 3242
Cdd:COG4717 502 -------LEEAREEYREErLPPVLERASEYFSRL 528
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2833-3188 |
2.04e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 57.21 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2833 EAARQRKIAQDELERLKKKAEEARKQKDEADVEAEVQIvAAQQAALKCSTAEHQvqSVLAQQKEDSIMHKKLKQEyekak 2912
Cdd:pfam07888 45 ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRV-AELKEELRQSREKHE--ELEEKYKELSASSEELSEE----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2913 klakeaeaakekaerEAALLRQQAEEAERQKAAAEQEAAIQAKAQE---DAERLRKEAEFEAAKRA--QAEGAALKQKQQ 2987
Cdd:pfam07888 117 ---------------KDALLAQRAAHEARIRELEEDIKTLTQRVLEretELERMKERAKKAGAQRKeeEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2988 ADAEMAKHKKLAEQTLK--------QKFQVEQELTKVKLKLDDTDKQKSLLDDELQR-----------------LKDEVD 3042
Cdd:pfam07888 182 QTEEELRSLSKEFQELRnslaqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrslqerlnaserkvegLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3043 DAVKQRGQVEEELFKVKVQMEEL------LKLKLRiedENQRLLKKDKDNSQKFLAEEAENMKRLAEDAARLSVESQEAA 3116
Cdd:pfam07888 262 SMAAQRDRTQAELHQARLQAAQLtlqladASLALR---EGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEER 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678729579 3117 RLRQIAEDDLIQQRALADKMLKEKMQAIQEssrLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEE 3188
Cdd:pfam07888 339 MEREKLEVELGREKDCNRVQLSESRRELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2442-2679 |
2.05e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.12 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2442 QEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAK-AEESALKQ 2520
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKqAEEAAAKA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2521 KDMAEKELERQRKVADSTAQQkltAEQElirlradfdnaeqqrslledelyrlKNEVIAAQQQRKQLEDELAKVRSEMdi 2600
Cdd:PRK09510 142 AAAAKAKAEAEAKRAAAAAKK---AAAE-------------------------AKKKAEAEAAKKAAAEAKKKAEAEA-- 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678729579 2601 liqlKSKAEKEtmsntekSKQLLEAEATKMrdvAEEAGKLRAIAEEAKhqrqVAEEEAARQRAEAERILKEKLAAISEA 2679
Cdd:PRK09510 192 ----AAKAAAE-------AKKKAEAEAKKK---AAAEAKKKAAAEAKA----AAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2932-3294 |
2.36e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 57.21 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2932 LRQQAE---EAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAkRAQAEGAALKQKQQADAEMAKHKKLAEQTLKQKFQ 3008
Cdd:pfam07888 40 LQERAEllqAQEAANRQREKEKERYKRDREQWERQRRELESRVA-ELKEELRQSREKHEELEEKYKELSASSEELSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3009 V---EQELTKVKLKLDDTD-----KQKSLLDDELQRLKDEVDDAVKQRGQVEEElfkvkvqmEELLKLKLRIEDENQRLL 3080
Cdd:pfam07888 119 AllaQRAAHEARIRELEEDiktltQRVLERETELERMKERAKKAGAQRKEEEAE--------RKQLQAKLQQTEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3081 KKDKDNSQKFLAEEAENMKRLAEDAARLSVESQEAarlrqiaeddliQQRALADKMLKEKMQAIQE---SSRLKAEAeml 3157
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA------------HRKEAENEALLEELRSLQErlnASERKVEG--- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3158 qRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQ-----------KSLEAERRRQLEIVAEAEKLKLQvsQLSEAQTKAEE 3226
Cdd:pfam07888 256 -LGEELSSMAAQRDRTQAELHQARLQAAQLTLQladaslalregRARWAQERETLQQSAEADKDRIE--KLSAELQRLEE 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678729579 3227 EAKKFKKQADKIaarlhETEIATKEKMTVVEKLEferlnTSKEAGDLRDAIADLEKDKARLKKEAEEL 3294
Cdd:pfam07888 333 RLQEERMEREKL-----EVELGREKDCNRVQLSE-----SRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
870-967 |
2.39e-07 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 51.95 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 870 KTFTKWVNkHLIKRAESQHHVTDLYEDLRDGHNLISLLEVLSGDTL------PREKGRMrfhkLQNVQIALDFLRHRQVK 943
Cdd:cd21286 3 KIYTDWAN-HYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVN 77
|
90 100
....*....|....*....|....
gi 1678729579 944 LVNIRNDDIADGNPKLTLGLIWTV 967
Cdd:cd21286 78 VQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2361-2551 |
2.94e-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: 54.93 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2361 AAKQKQKALDDLENLKKQAEEAERQVKQAEvekerqikvAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQL 2440
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELP---------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2441 QQEAAHLKKQQEDAINARE----EAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEEs 2516
Cdd:COG1579 72 EARIKKYEEQLGNVRNNKEyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE- 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1678729579 2517 aLKQKDMAEKELERQRKVADSTAQQKLTAEQELIR 2551
Cdd:COG1579 151 -LAELEAELEELEAEREELAAKIPPELLALYERIR 184
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2400-2641 |
3.23e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2400 AHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAahlkKQQEDAINAREEAEKELEKWRQKANEALRlR 2479
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL----AALERRIAALARRIRALEQELAALEAELA-E 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2480 LQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAE----------------KELERQRKVADSTAQQKL 2543
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavrrlqylkylaparrEQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2544 TAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSntekskqll 2623
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA--------- 238
|
250
....*....|....*...
gi 1678729579 2624 EAEATKMRDVAEEAGKLR 2641
Cdd:COG4942 239 AAERTPAAGFAALKGKLP 256
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2452-2682 |
3.26e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 56.42 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2452 EDAINAREEAEKELEKwrqkanealrlrlqaeeeahKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQ 2531
Cdd:COG2268 199 RDARIAEAEAERETEI--------------------AIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2532 RKvadstaqqKLTAEQELIrlradfdnaeqqrslledelyrlknevIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKE 2611
Cdd:COG2268 259 TA--------RAEAEAAYE---------------------------IAEANAEREVQRQLEIAEREREIELQEKEAEREE 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 2612 tmsNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKhqrqvAEEEAARQRAEAERILKEKLAAISEATHL 2682
Cdd:COG2268 304 ---AELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGL-----AEAEGKRALAEAWNKLGDAAILLMLIEKL 366
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2958-3432 |
3.42e-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: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2958 EDAERLRKEaeFEAAKRAQAegAALKQKQQADA--EMAKHKKLAEQTLKQKFQVEQELTKVKL-----KLDDTDKQKSLL 3030
Cdd:COG4913 225 EAADALVEH--FDDLERAHE--ALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3031 DDELQRLKDEVDDAVKQRGQVEEELFKVKVQM-----EELLKLKLRIEDENQRLlkKDKDNSQKFLAEEAENMK-RLAED 3104
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIrgnggDRLEQLEREIERLEREL--EERERRRARLEALLAALGlPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3105 AARLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQK---DLAQEQAQKLLEDK------ 3175
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDALAEAlgldea 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3176 ------QLMQRRLEEEteEYQKSLE-------------AERRRQ-LEIVaEAEKLKLQVSQLSEAQTKAEEEAKKFKKQ- 3234
Cdd:COG4913 459 elpfvgELIEVRPEEE--RWRGAIErvlggfaltllvpPEHYAAaLRWV-NRLHLRGRLVYERVRTGLPDPERPRLDPDs 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3235 -ADKIAARLH------ETEIATKEKMTVVEKLE-FERLNTS-------KEAGDL-------------------RDAIADL 3280
Cdd:COG4913 536 lAGKLDFKPHpfrawlEAELGRRFDYVCVDSPEeLRRHPRAitragqvKGNGTRhekddrrrirsryvlgfdnRAKLAAL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3281 EKDKARLKKEAEELQNKSKEMA---DAQQKQIEHEKTLLQQTFL------TEREMLLKKEKLIEEEKKKLE-SQFEEEAK 3350
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEaelDALQERREALQRLAEYSWDeidvasAEREIAELEAELERLDASSDDlAALEEQLE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3351 KSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQLEEAQ 3430
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
..
gi 1678729579 3431 KE 3432
Cdd:COG4913 776 DA 777
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3023-3432 |
3.59e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3023 TDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELlklklrieDENQRLLKKDKDNSQKFLAEEAEN---MK 3099
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERY--------EEQREQARETRDEADEVLEEHEERreeLE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3100 RLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDlaqeqaqklledkqlmq 3179
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE----------------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3180 rRLEEETEEYQKSLEAERRRQLEIVAEAEKLKlqvsqlsEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKL 3259
Cdd:PRK02224 318 -ELEDRDEELRDRLEECRVAAQAHNEEAESLR-------EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3260 EferlntsKEAGDLRDAIADLEKDKARLKKEAEELQnksKEMADAQQKQIEHEKTLlqqtfLTEREMLLKKEKLIEEEKK 3339
Cdd:PRK02224 390 E-------EEIEELRERFGDAPVDLGNAEDFLEELR---EERDELREREAELEATL-----RTARERVEEAEALLEAGKC 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3340 KLESQFEEEAKKSKALkDEQERQKQQMEEEKKKLHATmHEALSKQKEAEKEMLSKQKEMQELEKKRLEQEIILADENQKL 3419
Cdd:PRK02224 455 PECGQPVEGSPHVETI-EEDRERVEELEAELEDLEEE-VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETI 532
|
410
....*....|...
gi 1678729579 3420 REKLQQLEEAQKE 3432
Cdd:PRK02224 533 EEKRERAEELRER 545
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2176-2597 |
3.97e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2176 RRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQ---------ELKLMMKEEVN-RREIAAVDA 2245
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaelperleELEERLEELRElEEELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2246 EKQKQNIQLE--LHELKNLSEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAESEL--KQLRERAAEAER 2321
Cdd:COG4717 171 ELAELQEELEelLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEARL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2322 LRKVAQEEAEKLHKQVIEETQKKRIAE------------KELQHKSEAEKEAAKQKQKALDDLENLkkQAEEAERQVKQA 2389
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallFLLLAREKASLGKEAEELQALPALEEL--EEEELEELLAAL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2390 EVEKErqIKVAHVAAQKSAAAELQSKHSsfveKTSKLEESLKQEHgAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWR 2469
Cdd:COG4717 329 GLPPD--LSPEELLELLDRIEELQELLR----EAEELEEELQLEE-LEQEIAALLAEAGVEDEEELRAALEQAEEYQELK 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2470 QKANEaLRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEEsalkqkdmaekELERQRKvadstAQQKLTAEQEL 2549
Cdd:COG4717 402 EELEE-LEEQLEELLGELEELLEALDEEELEEELEELEEELEELEE-----------ELEELRE-----ELAELEAELEQ 464
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1678729579 2550 IRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSE 2597
Cdd:COG4717 465 LEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3119-3431 |
4.36e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 55.70 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3119 RQIAEDDLIQQRALADKMLKEKMQAIQEssRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERR 3198
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEE--EEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3199 RQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQaDKIAARLHETEIA--TKEKMTVVEKLEFERLNTSKEAGDLRDA 3276
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKEL-EKEEEREEDERILeyLKEKAEREEEREAEREEIEEEKEREIAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3277 IADL---------EKDKARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQQTFLTEREMLLKKEKLIEEEKKklesQFEE 3347
Cdd:pfam13868 189 LRAQqekaqdekaERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREE----EEFE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3348 EAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEaekemlskqkEMQELEKKRLEQEIILADENQKLREKLQQLE 3427
Cdd:pfam13868 265 RMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEERE----------EQRAAEREEELEEGERLREEEAERRERIEEE 334
|
....
gi 1678729579 3428 EAQK 3431
Cdd:pfam13868 335 RQKK 338
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2554-3005 |
5.37e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 56.07 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2554 ADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKE---TMSNTEKSKQLLEAeatkM 2630
Cdd:COG5278 79 EPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEaalALVRSGEGKALMDE----I 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2631 RDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQ 2710
Cdd:COG5278 155 RARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2711 RKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAE 2790
Cdd:COG5278 235 LAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2791 ETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEAEVQI 2870
Cdd:COG5278 315 AAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2871 VAAQQAALKCSTAEHQVQSVLAQQKEDSIMHKKLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKAAAEQEA 2950
Cdd:COG5278 395 IAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAAL 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1678729579 2951 AIQAKAQEDAERLRKEAEFEAAKRAQAEGAALKQKQQADAEMAKHKKLAEQTLKQ 3005
Cdd:COG5278 475 AALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAE 529
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2623-2872 |
5.53e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2623 LEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEE-EAARQRAEAERILKEKLAAISEATHLKTeAEIALKEKEAENERLR 2701
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIELLEPiRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2702 RAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRILKlnfEKASSGKLDLELE 2781
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---ALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2782 LNKLKNIAEETQQSKLRAEEEAEKLRKlaleeekrrreaeeKVKKITAAEEEAARQRKIAQDELERLKK-------KAEE 2854
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEE--------------ALAEAEAALRDLRRELRELEAEIASLERrksnipaRLLA 444
|
250 260
....*....|....*....|
gi 1678729579 2855 ARKQ-KDEADV-EAEVQIVA 2872
Cdd:COG4913 445 LRDAlAEALGLdEAELPFVG 464
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4963-4991 |
5.79e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.86 E-value: 5.79e-07
10 20
....*....|....*....|....*....
gi 1678729579 4963 IVDPETGKEMTVYEAYRKGLIDHQTYLEL 4991
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
847-973 |
7.03e-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: 51.54 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 847 SLDQPEEK--TWpHFIEDERDrvQKKTFTKWVNKHLIkraesQHHVTDLYEDLRDGHNLISLLEVL-------SGDTLPR 917
Cdd:cd21331 3 ALTKPENQdiDW-TLLEGETR--EERTFRNWMNSLGV-----NPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPY 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678729579 918 EKGRMRFHKLQNVQIALDFLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTVILHFQI 973
Cdd:cd21331 75 PKLGANMKKLENCNYAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2341-2580 |
7.09e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2341 TQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAevekERQIKvahvaAQKSAAAELQSKHSSFV 2420
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL----ARRIR-----ALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2421 EKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKwRQKANEALRLRLQAEEEAHKKSLAQEDAEKQK 2500
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2501 EEAEREAKKRAKAEESALKQKdmAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAA 2580
Cdd:COG4942 169 LEAERAELEALLAELEEERAA--LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2236-2579 |
7.43e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.29 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2236 NRREIAAVDAEKQKQNIQLELHELKNLsEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLRER 2315
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2316 AAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKER 2395
Cdd:COG4372 96 LAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2396 QIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEA 2475
Cdd:COG4372 176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2476 -LRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRA 2554
Cdd:COG4372 256 iLKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
330 340
....*....|....*....|....*
gi 1678729579 2555 DFDNAEQQRSLLEDELYRLKNEVIA 2579
Cdd:COG4372 336 LAELADLLQLLLVGLLDNDVLELLS 360
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2072-2532 |
7.44e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2072 ITDSKTLKEQLSQEKKLLEEIENNKDNVDECQKYAKAYINSIKDYELQLVAYNAQADPLASPLKKTKLDsasdniiQEYV 2151
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-------AELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2152 TLRTRYSELMtltsQYIKFITETQRRLEDEEKAAKKLKAEEQKKMAemQAELDKQKQLAAAHAKAIAKAEKEAQElklmm 2231
Cdd:COG4717 143 ELPERLEELE----ERLEELRELEEELEELEAELAELQEELEELLE--QLSLATEEELQDLAEELEELQQRLAEL----- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2232 KEEVNRREIAAVDAEKQKQNIQLELHELKNlsEQQIKDKGQL------------VDEALQSRTKIEEEIYLIRIQLettv 2299
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAAL--EERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFLVLGL---- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2300 kqksTAESELKQLRERAAEAERLRKVAQEEAeklhKQVIEETQKKRIAeKELQHKSEAEKEAAKQKQKALDDLENLKKQA 2379
Cdd:COG4717 286 ----LALLFLLLAREKASLGKEAEELQALPA----LEELEEEELEELL-AALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2380 EEAERQVKQAEVEKERQIKVAHVAAQK----SAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQL--QQEAAHLKKQQED 2453
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAEAGVEDeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELleALDEEELEEELEE 436
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678729579 2454 AINAREEAEKELEKWRQKANEaLRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAeESALKQKDMAEKELERQR 2532
Cdd:COG4717 437 LEEELEELEEELEELREELAE-LEAELEQLEEDGELAELLQELEELKAELRELAEEWAAL-KLALELLEEAREEYREER 513
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2356-2751 |
8.19e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 55.26 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2356 EAEKEAAKQK-QKALDDLENLKkQAEEAERQVKQAEVEKERQIkVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEH 2434
Cdd:pfam02029 2 EDEEEAARERrRRAREERRRQK-EEEEPSGQVTESVEPNEHNS-YEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2435 GAVLQLQQEAAHLKKQQEDAINAREEAEKELEK--WRQKANEALRLRLQAEEEAHKKSlaQEDAEKQKEEAEREAKKRAK 2512
Cdd:pfam02029 80 QEALERQKEFDPTIADEKESVAERKENNEEEENssWEKEEKRDSRLGRYKEEETEIRE--KEYQENKWSTEVRQAEEEGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2513 AEEsalkQKDMAEKELERQRKvadstaqqkltaeqelirlradfdNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELA 2592
Cdd:pfam02029 158 EEE----DKSEEAEEVPTENF------------------------AKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2593 KVRSEMDILIQLKSKAEKETMSNT----EKSKQLLEAEATKmrdvaeeagklraiaEEAKHQRQVAEEEaarqraEAERI 2668
Cdd:pfam02029 210 QNGEEEVTKLKVTTKRRQGGLSQSqereEEAEVFLEAEQKL---------------EELRRRRQEKESE------EFEKL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2669 LKEKLAAISEATHLKTEAEIALKEKEAEnERLRRAAEDEayQRKALEDEANQHKKEIEekivqlKKSSDAEMERQKaMVD 2748
Cdd:pfam02029 269 RQKQQEAELELEELKKKREERRKLLEEE-EQRRKQEEAE--RKLREEEEKRRMKEEIE------RRRAEAAEKRQK-LPE 338
|
...
gi 1678729579 2749 DTL 2751
Cdd:pfam02029 339 DSS 341
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2436-2662 |
8.23e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2436 AVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEE 2515
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2516 SALKQKDMAEKELERQRKVADSTAQQK-----------LTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQR 2584
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2585 KQLEDELAKVRSEMDILIQLKsKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKL--RAIAEEAKHQRQVAEEEAARQR 2662
Cdd:COG4942 174 AELEALLAELEEERAALEALK-AERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAAGFAALK 252
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2191-2550 |
8.28e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 55.29 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2191 EEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELKLMMKEEVNRREIAAVDAEKQKQNIQLELHELKNLSEQQIKDK 2270
Cdd:pfam07888 38 ECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2271 GQLVDEALQSRTKIEEeiylIRIQLETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKE 2350
Cdd:pfam07888 118 DALLAQRAAHEARIRE----LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2351 LQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKE--RQIKVAHVAAQKSAAA---ELQSKHSSFVEKTSK 2425
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEelRSLQERLNASERKVEGlgeELSSMAAQRDRTQAE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2426 LEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKAnealrLRLQAEEEAHKKSLAQEDAEKQKEEAEr 2505
Cdd:pfam07888 274 LHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRI-----EKLSAELQRLEERLQEERMEREKLEVE- 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1678729579 2506 eakkRAKAEESALKQKDMAEKELERQR---KVADSTAQQKLTAEQELI 2550
Cdd:pfam07888 348 ----LGREKDCNRVQLSESRRELQELKaslRVAQKEKEQLQAEKQELL 391
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2505-2942 |
8.66e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 55.30 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2505 REAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQR 2584
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2585 KQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAE 2664
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2665 AERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQK 2744
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2745 AMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKV 2824
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2825 KKITAAEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKEDSIMHKKL 2904
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430
....*....|....*....|....*....|....*...
gi 1678729579 2905 KQEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQ 2942
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAA 519
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2481-2704 |
8.79e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 55.72 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2481 QAEEEAHKKSLAQE--DAEKQ---KEEAEREAKKRAKAEESALKQKDMAEKELER-QRKVADSTAQQKLTAEQE------ 2548
Cdd:PRK05035 440 AIEQEKKKAEEAKArfEARQArleREKAAREARHKKAAEARAAKDKDAVAAALARvKAKKAAATQPIVIKAGARpdnsav 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2549 --LIRLRADFDNAEQQRSLLEDELYRLKNEVIAA----QQQRKQLEDELAKVRSEMDiliQLKSKAEKETMSNTEKSKQL 2622
Cdd:PRK05035 520 iaAREARKAQARARQAEKQAAAAADPKKAAVAAAiaraKAKKAAQQAANAEAEEEVD---PKKAAVAAAIARAKAKKAAQ 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2623 LEAEATKMRDVAEEAGKLRAIAEE-AKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLR 2701
Cdd:PRK05035 597 QAASAEPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPK 676
|
...
gi 1678729579 2702 RAA 2704
Cdd:PRK05035 677 KAA 679
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2843-3433 |
9.25e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2843 DELERLKKKAEEARKQKD--EADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKEDsimhkklkqeyekakklakeaea 2920
Cdd:COG4913 235 DDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE----------------------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2921 akekaereaaLLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEfeaAKRAQAEGAALKQ--KQQADAEmakhKKL 2998
Cdd:COG4913 292 ----------LLEAELEELRAELARLEAELERLEARLDALREELDELE---AQIRGNGGDRLEQleREIERLE----REL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2999 AEQTLKQKfQVEQELTKVKLKLDDTDKQkslLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQR 3078
Cdd:COG4913 355 EERERRRA-RLEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3079 LLKKDKDNSQKFLAEEAENMKRLAEDAARLSVesqeAARLRQIAEDDLIQQRAL-------------ADKMLKEKMQAIq 3145
Cdd:COG4913 431 LERRKSNIPARLLALRDALAEALGLDEAELPF----VGELIEVRPEEERWRGAIervlggfaltllvPPEHYAAALRWV- 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3146 ESSRLKAEAEMLQRQKDLAQEQAQKLLED-----------------KQLMQRRL-------EEETEEYQKSLEAER---- 3197
Cdd:COG4913 506 NRLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawlEAELGRRFdyvcvdsPEELRRHPRAITRAGqvkg 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3198 -----------------------RRQLE-IVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIA--ARLHETEIATKE 3251
Cdd:COG4913 586 ngtrhekddrrrirsryvlgfdnRAKLAaLEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3252 KMTVVEKLEFER---LNTSKEAGDLRDAIADLEKDKARLKKEAEELQnksKEMADAQQK--QIEHEKTLLQQTFLTEREM 3326
Cdd:COG4913 666 AEREIAELEAELerlDASSDDLAALEEQLEELEAELEELEEELDELK---GEIGRLEKEleQAEEELDELQDRLEAAEDL 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3327 LLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMLSKQKEMQELEK--K 3404
Cdd:COG4913 743 ARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLAllD 822
|
650 660
....*....|....*....|....*....
gi 1678729579 3405 RLEQEIILADEnQKLREKLQQLEEAQKEQ 3433
Cdd:COG4913 823 RLEEDGLPEYE-ERFKELLNENSIEFVAD 850
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2177-2421 |
9.28e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 9.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2177 RLEDEEKAAKKlKAEEQKKMAEMQAELDKQKQlaaahakaiakaEKEAQELKLMMKEEVNRREIaavdaekQKQNIQlel 2256
Cdd:PRK09510 66 RQQQQQKSAKR-AEEQRKKKEQQQAEELQQKQ------------AAEQERLKQLEKERLAAQEQ-------KKQAEE--- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2257 helknlSEQQIKDKGQLVDEAlqsrtkieeeiyliriQLETTVKQKSTAESELKQLRERAAEAERLRKvAQEEAEKLHKQ 2336
Cdd:PRK09510 123 ------AAKQAALKQKQAEEA----------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEAK-KKAEAEAAKKA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2337 ViEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLEnlKKQAEeAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKH 2416
Cdd:PRK09510 180 A-AEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEA--KKKAA-AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
....*
gi 1678729579 2417 SSFVE 2421
Cdd:PRK09510 256 AAEVD 260
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2172-2519 |
9.47e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 55.26 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2172 TETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHakaiakaekeaQELKLMMKEEVNRREIaavdaekqkqn 2251
Cdd:pfam02029 52 PSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTI-----------ADEKESVAERKENNEE----------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2252 iqlelhELKNLSEQQIKDKGQLVDEalqsrtkiEEEiyliriqlETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAE 2331
Cdd:pfam02029 110 ------EENSSWEKEEKRDSRLGRY--------KEE--------ETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2332 KLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKalddLENLKKQAEEaERQVKQAEVEKERQIKVAHVAAQKSAAAe 2411
Cdd:pfam02029 168 EVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRG----HPEVKSQNGE-EEVTKLKVTTKRRQGGLSQSQEREEEAE- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2412 lqskhsSFVEKTSKLEEsLKQEHGAvlQLQQEAAHLKKQQEDAINAREEAEKELEkWRQKANEALRLRLQAEEEAHKKSL 2491
Cdd:pfam02029 242 ------VFLEAEQKLEE-LRRRRQE--KESEEFEKLRQKQQEAELELEELKKKRE-ERRKLLEEEEQRRKQEEAERKLRE 311
|
330 340
....*....|....*....|....*...
gi 1678729579 2492 aQEDAEKQKEEAEReakKRAKAEESALK 2519
Cdd:pfam02029 312 -EEEKRRMKEEIER---RRAEAAEKRQK 335
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2248-2861 |
9.79e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.73 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2248 QKQNIQLELHELKNLSEQQIKDKGQLvdEALQSRtkIEEEIYLIRIQLETTVKQKSTAESELKQLRERAAEAERLRKV-- 2325
Cdd:PRK04863 531 QQQRAERLLAEFCKRLGKNLDDEDEL--EQLQEE--LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwl 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2326 -AQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKqkalDDLENLKKQAEEAERQVKQAE-VEKERQIKVA--- 2400
Cdd:PRK04863 607 aAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVER----DELAARKQALDEEIERLSQPGgSEDPRLNALAerf 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2401 --------------HVAAQKSAAAElQSKHSSFVEKTSKLEESLKQEHGAvlqlqQEAAHLKKQQEDAI-NAREEAEkEL 2465
Cdd:PRK04863 683 ggvllseiyddvslEDAPYFSALYG-PARHAIVVPDLSDAAEQLAGLEDC-----PEDLYLIEGDPDSFdDSVFSVE-EL 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2466 EK----------WR-----------QKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAE---------- 2514
Cdd:PRK04863 756 EKavvvkiadrqWRysrfpevplfgRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGShlavafeadp 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2515 ESALKQKDMAEKELERQRKVADSTAQQkltaeqelirLRADFDNAEQQRSLLEDELYRLKneVIAaqqqRKQLEDELAKV 2594
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQ----------QRSQLEQAKEGLSALNRLLPRLN--LLA----DETLADRVEEI 899
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2595 RSEMDILiqlkSKAEKETMSNtEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQvaeeeAARQRAEAeriLKEkla 2674
Cdd:PRK04863 900 REQLDEA----EEAKRFVQQH-GNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQR-----DAKQQAFA---LTE--- 963
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2675 AISEATHLKTEAEIALKEKEAE-NERLRRAAEDEAYQRKALEDEANQHKKEIEEKI---VQLKKSSDAEMErqkaMVDDt 2750
Cdd:PRK04863 964 VVQRRAHFSYEDAAEMLAKNSDlNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNqvlASLKSSYDAKRQ----MLQE- 1038
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2751 LKQR------RVVEEEIrilklnfEKASSGKLDLELEL--NKLKNIAEETQQSKLRAEEEA--EKLRKLAleeekrrrea 2820
Cdd:PRK04863 1039 LKQElqdlgvPADSGAE-------ERARARRDELHARLsaNRSRRNQLEKQLTFCEAEMDNltKKLRKLE---------- 1101
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1678729579 2821 eekvKKITAAEEEAARQRKIAQDELERLKKKAEEARKQKDE 2861
Cdd:PRK04863 1102 ----RDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRE 1138
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
868-978 |
1.03e-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: 51.58 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 868 QKKTFTKWVNKHLIKRAESQHHV------TDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHKLQNVQIALDFL 937
Cdd:cd21323 25 EKVAFVNWINKALEGDPDCKHVVpmnptdESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1678729579 938 RHRQVKLVNIRNDDIADGNPKLTLGLIWTVILHFQISDIQI 978
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2617-3434 |
1.11e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.44 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2617 EKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQR-QVAEEEAarQRAEAERILKEKLAAISEathlkteaeiaLKEKEA 2695
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRdQITSKEA--QLESSREIVKSYENELDP-----------LKNRLK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2696 ENERLRRAA---EDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMVDDTL--KQRRVVEEEIRILKLNFEK 2770
Cdd:TIGR00606 256 EIEHNLSKImklDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVreKERELVDCQRELEKLNKER 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2771 A--SSGKLDLELELNKLKNIAEETQ-QSKLRAEEEAEKLRKLALEEEKRRREAEEKVKK-ITAAEEEAARQRKIAQDELE 2846
Cdd:TIGR00606 336 RllNQEKTELLVEQGRLQLQADRHQeHIRARDSLIQSLATRLELDGFERGPFSERQIKNfHTLVIERQEDEAKTAAQLCA 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2847 RLKKKAEEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQ-QKEDSIMHKKLKQEyekakklakeaeaakeka 2925
Cdd:TIGR00606 416 DLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKElQQLEGSSDRILELD------------------ 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2926 ereaallrQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQAegaalkqkqQADAEMAKHKKLAEQTL-- 3003
Cdd:TIGR00606 478 --------QELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLD---------QEMEQLNHHTTTRTQMEml 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3004 -KQKFQVEQELTKVKLKldDTDKQKSLLDD--ELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLL 3080
Cdd:TIGR00606 541 tKDKMDKDEQIRKIKSR--HSDELTSLLGYfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKE 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3081 KKDKDNSQKFLaeEAENMKRLAEDAARLSVESQEAARlrqiaeddliqQRALADKMLKEKMQAIQESSRLKAEAEMLQRQ 3160
Cdd:TIGR00606 619 EQLSSYEDKLF--DVCGSQDEESDLERLKEEIEKSSK-----------QRAMLAGATAVYSQFITQLTDENQSCCPVCQR 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3161 KDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEklkLQVSQLSEAQTKAEEEAKKFKKQADKIAA 3240
Cdd:TIGR00606 686 VFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP---GRQSIIDLKEKEIPELRNKLQKVNRDIQR 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3241 RLHETEIATKEKMTVVEKLEFERLNTSkEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQQTF 3320
Cdd:TIGR00606 763 LKNDIEEQETLLGTIMPEEESAKVCLT-DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTV 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3321 LTEREMLLKKEKLIEEEKKKLESQFEEeAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMLSKQKEMQE 3400
Cdd:TIGR00606 842 VSKIELNRKLIQDQQEQIQHLKSKTNE-LKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK 920
|
810 820 830
....*....|....*....|....*....|....
gi 1678729579 3401 LEKKRLEQEIILADENQKLREKLQQLEEAQKEQH 3434
Cdd:TIGR00606 921 DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIH 954
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2253-2589 |
1.35e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2253 QLELHELKNLSEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLRERAAEAerlrkvaQEEAEK 2332
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQL-------EEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2333 LHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKERQIKVAHVAAQKSAAAEL 2412
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2413 QSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLA 2492
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2493 QEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYR 2572
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330
....*....|....*..
gi 1678729579 2573 LKNEVIAAQQQRKQLED 2589
Cdd:COG4372 325 AKKLELALAILLAELAD 341
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2294-2717 |
1.40e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 54.91 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2294 QLETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLE 2373
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2374 NLKKQAEEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQED 2453
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2454 AINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRK 2533
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2534 VADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDElyrlkNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETM 2613
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAE-----AVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELA 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2614 SNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEK 2693
Cdd:COG5278 426 EALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALAL 505
|
410 420
....*....|....*....|....
gi 1678729579 2694 EAENERLRRAAEDEAYQRKALEDE 2717
Cdd:COG5278 506 AALLLAAAEAALAAALAAALASAE 529
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2077-2693 |
1.49e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.18 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2077 TLKEQLSQEKKLLEEIENNKDNVDECQKYAKAYINSI-KDYELQLVAYNaqadplasplkktKLDSASDNIIQEYVTLRT 2155
Cdd:pfam01576 521 TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALtQQLEEKAAAYD-------------KLEKTKNRLQQELDDLLV 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2156 RYSELMTLTSQYIKfiteTQRRLED---EEKAAKKLKAEEQKKmAEMQAELDKQKQLAaahakaiakaekeaqeLKLMMK 2232
Cdd:pfam01576 588 DLDHQRQLVSNLEK----KQKKFDQmlaEEKAISARYAEERDR-AEAEAREKETRALS----------------LARALE 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2233 EEVNRREiaavDAEKQKQNIQLELHELKNLSEqqikDKGQLVDEALQSRTKIEEEIYLIRIQLETTvkqkstaESELKql 2312
Cdd:pfam01576 647 EALEAKE----ELERTNKQLRAEMEDLVSSKD----DVGKNVHELERSKRALEQQVEEMKTQLEEL-------EDELQ-- 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2313 rerAAEAERLRKVAQEEAEKLHkqvieetqkkriAEKELQHKSEAEKEAAKQKQKALDDLEnlkkqaeeaerqvkqAEVE 2392
Cdd:pfam01576 710 ---ATEDAKLRLEVNMQALKAQ------------FERDLQARDEQGEEKRRQLVKQVRELE---------------AELE 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2393 KERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQehgaVLQLQQEAAHLKKQQEDAINAREEA---EKELEKwR 2469
Cdd:pfam01576 760 DERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQ----LKKLQAQMKDLQRELEEARASRDEIlaqSKESEK-K 834
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2470 QKANEALRLRLQ---AEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMA--EKELE-----------RQRK 2533
Cdd:pfam01576 835 LKNLEAELLQLQedlAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAqlEEELEeeqsntellndRLRK 914
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2534 vadsTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQ--------LEDELAKVRSEMDILIQLK 2605
Cdd:pfam01576 915 ----STLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSkfkssiaaLEAKIAQLEEQLEQESRER 990
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2606 SKAEKETMSNTEKSKQLL---EAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAeAERILKEKLAAISEATHL 2682
Cdd:pfam01576 991 QAANKLVRRTEKKLKEVLlqvEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANA-ARRKLQRELDDATESNES 1069
|
650
....*....|.
gi 1678729579 2683 KTEAEIALKEK 2693
Cdd:pfam01576 1070 MNREVSTLKSK 1080
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2987-3228 |
1.50e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2987 QADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELfkvkVQMEELL 3066
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----EERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3067 KLKLRIEDENQRLLKK-----DKDNSQKFLaEEAENMKRLAEDAARLsVESQEAARlrqiaeDDLIQQRALADKMLKEKM 3141
Cdd:COG3883 89 GERARALYRSGGSVSYldvllGSESFSDFL-DRLSALSKIADADADL-LEELKADK------AELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3142 QAIQESSRLKAEaemLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQ 3221
Cdd:COG3883 161 ALKAELEAAKAE---LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
....*..
gi 1678729579 3222 TKAEEEA 3228
Cdd:COG3883 238 AAAAAAA 244
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2497-2854 |
1.54e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2497 EKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNE 2576
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2577 VIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKH-QRQVAE 2655
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESlQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2656 EEAARQR---AEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQL 2732
Cdd:COG4372 169 LEQELQAlseAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2733 KKSSDAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALE 2812
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1678729579 2813 EEKRRREAEEKVKKITAAEEEAARQRKIAQDELERLKKKAEE 2854
Cdd:COG4372 329 ELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2580-2805 |
1.82e-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: 53.70 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2580 AQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLE-AEATKMRDVAEEAGKLRAI----AEEAKhqRQVA 2654
Cdd:TIGR02794 52 ANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQrAAAEKAAKQAEQAAKQAEEkqkqAEEAK--AKQA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2655 EEEAARQRAEAERILKEKLAAISEATHLKTEAEIAlkEKEAENERLRRAAEDEAyqrkaledeanqhKKEIEEKIVQLKK 2734
Cdd:TIGR02794 130 AEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEA--KKKAEEAKKKAEAEAKA-------------KAEAEAKAKAEEA 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 2735 SSDAEMERQKAMVDDTLKQRRvvEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEK 2805
Cdd:TIGR02794 195 KAKAEAAKAKAAAEAAAKAEA--EAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2237-2543 |
1.97e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.38 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2237 RREIAAVDAEKQKQNIQLELHELKNLSEQQIKDKGQLVDEALQSRTKIEEeiyliriQLETTVKQKstAESELKQLRERA 2316
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEE-------QIEEREQKR--QEEYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2317 AEAERLRKVAQEEAEKLhkqviEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLK-------KQAEEAERQVKQA 2389
Cdd:pfam13868 102 QMDEIVERIQEEDQAEA-----EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERileylkeKAEREEEREAERE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2390 EVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKT---SKLEESLKQEHGAVLQLQQEAAHLKKQQEDAIN------AREE 2460
Cdd:pfam13868 177 EIEEEKEREIARLRAQQEKAQDEKAERDELRAKLyqeEQERKERQKEREEAEKKARQRQELQQAREEQIElkerrlAEEA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2461 AEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQ 2540
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
...
gi 1678729579 2541 QKL 2543
Cdd:pfam13868 337 KKL 339
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3135-3437 |
2.01e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3135 KMLKEKMQAIQESsrLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRrlEEETEEYQKSLEAERRRQLEIVAEAEKLKLQV 3214
Cdd:PRK03918 172 KEIKRRIERLEKF--IKRTENIEELIKEKEKELEEVLREINEISSE--LPELREELEKLEKEVKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3215 SQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEkMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEEL 3294
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE-LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3295 QNKSKEMADAQQKQIEHEKTLLQqtflTEREMllkkeklieeekkklesqfeEEAKKSKALKDEQERQKQQMEEEKKKLH 3374
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKE----LEKRL--------------------EELEERHELYEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 3375 ATMHEalskqkEAEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQLEEAQKEQHTVP 3437
Cdd:PRK03918 383 GLTPE------KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP 439
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2296-2541 |
2.05e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 54.19 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2296 ETTVKQKSTAESELKQLRERAAEAERL---RKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEaakqkqkalddl 2372
Cdd:pfam15709 322 KALLEKREQEKASRDRLRAERAEMRRLeveRKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEI------------ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2373 eNLKKQAEEAERQvKQAEVEKERQIKVAhvAAQKSAAAELQSKHSSfvektskleeslkqehgaVLQLQQeaahlKKQQE 2452
Cdd:pfam15709 390 -RLRKQRLEEERQ-RQEEEERKQRLQLQ--AAQERARQQQEEFRRK------------------LQELQR-----KKQQE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2453 DAINAREEAEKELEKWRQKANEALRLRLQAEEEAhkkslaqedAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQR 2532
Cdd:pfam15709 443 EAERAEAEKQRQKELEMQLAEEQKRLMEMAEEER---------LEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAM 513
|
....*....
gi 1678729579 2533 KVADSTAQQ 2541
Cdd:pfam15709 514 KQAQEQARQ 522
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3061-3432 |
2.10e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3061 QMEELLKLKLRIEDENQRLLKKdkdnSQKFLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDdlIQQRALADKMLKEK 3140
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKE----LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE--LREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3141 MQAIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQR------RLEEETEEYQKSLEAERRRQLE-IVAEAEKLKLQ 3213
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEEleaelaELQEELEELLEQLSLATEEELQdLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3214 VSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEK-----------MTVVEKLEFERLNTSKE--------AGDLR 3274
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKearlllliaaaLLALLGLGGSLLSLILTiagvlflvLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3275 DAIADLEKDKARLKKEAEELQNKSKEMADAQQKQIEhektllqqtFLTEREMLLKKEKLIEEEKKKLESQFEEeaKKSKA 3354
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEE---------LLAALGLPPDLSPEELLELLDRIEELQE--LLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3355 LKDEQERQKQQMEEEKKKL----HATMHEALSKQKEAEKEMLSKQKEMQELE-----KKRLEQEIILADENQKLREKLQQ 3425
Cdd:COG4717 357 EELEEELQLEELEQEIAALlaeaGVEDEEELRAALEQAEEYQELKEELEELEeqleeLLGELEELLEALDEEELEEELEE 436
|
....*..
gi 1678729579 3426 LEEAQKE 3432
Cdd:COG4717 437 LEEELEE 443
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
986-1085 |
2.12e-06 |
|
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: 49.68 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 986 SAKEKLLLWSQRMTgdyQNIRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSN-LENLEQAFNVAERDLGVTRLLD 1064
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQpVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|.
gi 1678729579 1065 PEDVDVQHPDEKSIITYVSSL 1085
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQF 108
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2488-2674 |
2.14e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.01 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2488 KKSLAQEDAEKQKEEAEREAKKRAKaeesalkqkdmaEKELERQRKVAdstaQQKLTAEQELIRLRADFDNAEQQrslLE 2567
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEAEAIKK------------EALLEAKEEIH----KLRNEFEKELRERRNELQKLEKR---LL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2568 DELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKetmsNTEKSKQLLEaEATKMrdVAEEAGK--LRAIAE 2645
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE----LIEEQLQELE-RISGL--TAEEAKEilLEKVEE 165
|
170 180 190
....*....|....*....|....*....|...
gi 1678729579 2646 EAKHQRQV----AEEEAarqRAEAERILKEKLA 2674
Cdd:PRK12704 166 EARHEAAVlikeIEEEA---KEEADKKAKEILA 195
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2439-2669 |
2.36e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.66 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2439 QLQQEAAHLKKQQEdainAREEAEKELEKWRQKANEAlrlRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESAL 2518
Cdd:PRK09510 84 KEQQQAEELQQKQA----AEQERLKQLEKERLAAQEQ---KKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2519 kqKDMAEKELERQRKVADSTAQQKLTAEQelirlradfdnaeqqrslledelyRLKNEVIAAQQQrkqleDELAKVRSEM 2598
Cdd:PRK09510 157 --AAAAKKAAAEAKKKAEAEAAKKAAAEA------------------------KKKAEAEAAAKA-----AAEAKKKAEA 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 2599 DIliqlKSKAEKEtmsntEKSKQLLEAEATKmrdvAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERIL 2669
Cdd:PRK09510 206 EA----KKKAAAE-----AKKKAAAEAKAAA----AKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2667-3124 |
2.39e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2667 RILKEKLAAISEATHLKTEAEIALKEKEAENERL---RRAAEDEAYQRKALEDE-------------ANQHKKEIEEKIV 2730
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDyqaasdhlnlvqtALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2731 QLKKSSDAeMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKlRAEEEAEKLRKLA 2810
Cdd:PRK04863 356 DLEELEER-LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAV-QALERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2811 leeekrrreaEEKVKKITAAEEEAARQRKIAQDELERLKKK---AEEARKQKDEAdveaeVQIVAAQQAALKCSTAEHQV 2887
Cdd:PRK04863 434 ----------DLTADNAEDWLEEFQAKEQEATEELLSLEQKlsvAQAAHSQFEQA-----YQLVRKIAGEVSRSEAWDVA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2888 QSVLAQQKEDSIMHKKLKQeyekakklakeaeaakekaereaalLRQQAEEAERQkaaaeqeaaiqAKAQEDAERLRKEA 2967
Cdd:PRK04863 499 RELLRRLREQRHLAEQLQQ-------------------------LRMRLSELEQR-----------LRQQQRAERLLAEF 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2968 EFEAAKRAQAEGAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSL---LDDELQRLKDEVDDA 3044
Cdd:PRK04863 543 CKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEE 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3045 VKQRGQVEEelfkvkvQMEELLklklriedENQRLLKKDKDnsqkflaEEAENMKRLAEDAARLS-VESQEAARLRQIAE 3123
Cdd:PRK04863 623 FEDSQDVTE-------YMQQLL--------ERERELTVERD-------ELAARKQALDEEIERLSqPGGSEDPRLNALAE 680
|
.
gi 1678729579 3124 D 3124
Cdd:PRK04863 681 R 681
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
982-1085 |
2.45e-06 |
|
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: 49.32 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 982 SEDMSAKEKLLLWSQRMTGDyqnIRCDNFSTSWRDGKLFNAVIHKHHPRLI-DMGKVYRQSNLENLEQAFNVAERDLGVT 1060
Cdd:cd21313 4 AKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGVP 80
|
90 100
....*....|....*....|....*..
gi 1678729579 1061 RLLDPEDVdvQHPD--EKSIITYVSSL 1085
Cdd:cd21313 81 QVITPEEI--IHPDvdEHSVMTYLSQF 105
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2163-2521 |
2.72e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 53.86 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2163 LTSQYIKFITETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQlaaahAKAIAKAEKEAQELKLmmkeevnrrEIAA 2242
Cdd:NF033838 115 LTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKE-----EDRRNYPTNTYKTLEL---------EIAE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2243 VDAEKQKQNIQLELHELKNLSEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAE-SELKQLRERAAEAER 2321
Cdd:NF033838 181 SDVEVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKlKEAVEKNVATSEQDK 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2322 L-----RKVAQEEAEKLHKQVIEETQKKRIAEKELQHKS-EAEKEAAKQKQKALDDLENLKKQAEEAERQ-----VKQAE 2390
Cdd:NF033838 261 PkrrakRGVLGEPATPDKKENDAKSSDSSVGEETLPSPSlKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNyptntYKTLE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2391 VE-KERQIKVahvaaqKSAAAELQSKHSsfveKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEK---ELE 2466
Cdd:NF033838 341 LEiAESDVKV------KEAELELVKEEA----KEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEAKRkaaEED 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2467 KWRQKANEALRLR--LQAEEEAHK--KSLAQEDAEK-QKEEAEREAKKRAKAEESALKQK 2521
Cdd:NF033838 411 KVKEKPAEQPQPApaPQPEKPAPKpeKPAEQPKAEKpADQQAEEDYARRSEEEYNRLTQQ 470
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2617-2875 |
2.83e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 53.80 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2617 EKSK-QLLEAEATKmrdvAEEAgKLRAIAEEAKHQRQVAEEEAARQRAEAER-------------ILKEKLAAISEATHL 2682
Cdd:PRK05035 434 AKAEiRAIEQEKKK----AEEA-KARFEARQARLEREKAAREARHKKAAEARaakdkdavaaalaRVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2683 KTEAEIALKEKEAEnERLRRAAEDEAYQRKALEDEANQHKKEIEEKI--VQLKKSSDAEMERQKAMVDDTLKQRrvVEEE 2760
Cdd:PRK05035 509 KAGARPDNSAVIAA-REARKAQARARQAEKQAAAAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDPKKAA--VAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2761 IRILKLNFEKASSGKLDLELELNklkniAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRKI 2840
Cdd:PRK05035 586 IARAKAKKAAQQAASAEPEEQVA-----EVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKA 660
|
250 260 270
....*....|....*....|....*....|....*
gi 1678729579 2841 AQDELERLKKKAEEARKQKDEADVEAEVQIVAAQQ 2875
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2439-2666 |
2.99e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2439 QLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAE---- 2514
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2515 ---------------ESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIA 2579
Cdd:COG3883 100 gsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2580 AQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAA 2659
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAA 259
|
....*..
gi 1678729579 2660 RQRAEAE 2666
Cdd:COG3883 260 GSAGAAG 266
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
983-1083 |
3.01e-06 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 49.39 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 983 EDMSAKEKLLLWSQRMTGDyqnIRCDNFSTSWRDGKLFNAVIHKHHPRLI-DMGKVYRQSNLENLEQAFNVAERDLGVTR 1061
Cdd:cd21315 13 KGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQ 89
|
90 100
....*....|....*....|..
gi 1678729579 1062 LLDPEDVDVQHPDEKSIITYVS 1083
Cdd:cd21315 90 LIKPEEMVNPKVDELSMMTYLS 111
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2263-2475 |
3.68e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2263 SEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVieetq 2342
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2343 KKRIAE--------------------KELQHKSEAEKEAAKQKQKALDDLENLKKQAEEaerqvKQAEVEKERQIKVAHV 2402
Cdd:COG3883 89 GERARAlyrsggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEA-----KKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 2403 AAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEA 2475
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3091-3326 |
3.74e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3091 LAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDL---IQQRALADkmLKEKMQAIQESSrlkAEAEMLQRQKDLAQEQ 3167
Cdd:COG4913 626 LAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvaSAEREIAE--LEAELERLDASS---DDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3168 AQKLLEDKQLMQRRlEEETEEYQKSLEAERRRQLEIVAEAEKL-KLQVSQLSEAQTKAEEEAKKFKKQADKIAARLH--E 3244
Cdd:COG4913 701 LEELEEELDELKGE-IGRLEKELEQAEEELDELQDRLEAAEDLaRLELRALLEERFAAALGDAVERELRENLEERIDalR 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3245 TEIATKEKMTVVEKLEFERLNTSkEAGDLRDAIADLEKDKARLKK-EAEELQNKSKEMADAQQKQIEHEKTLLQQTFLTE 3323
Cdd:COG4913 780 ARLNRAEEELERAMRAFNREWPA-ETADLDADLESLPEYLALLDRlEEDGLPEYEERFKELLNENSIEFVADLLSKLRRA 858
|
...
gi 1678729579 3324 REM 3326
Cdd:COG4913 859 IRE 861
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
3071-3247 |
3.99e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.42 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3071 RIEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDAARLSVESQEAARLRQiAEDDLIQQRaladkmlkeKMQAIQESSRL 3150
Cdd:pfam15709 354 RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQ-EEEERKQRL---------QLQAAQERARQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3151 KAEA---EMLQRQKDLAQEQAQKLLEDKqlmQRRLEEETEeyqksLEAERRRQLEIvAEAEKLKLQvSQLSEAQTKAEEE 3227
Cdd:pfam15709 424 QQEEfrrKLQELQRKKQQEEAERAEAEK---QRQKELEMQ-----LAEEQKRLMEM-AEEERLEYQ-RQKQEAEEKARLE 493
|
170 180
....*....|....*....|
gi 1678729579 3228 AKKfKKQADKIAARLHETEI 3247
Cdd:pfam15709 494 AEE-RRQKEEEAARLALEEA 512
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2232-2551 |
4.30e-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: 53.22 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2232 KEEVNRREIAAVDAEKQKQNIQLELHELKNLSEQQIKDKGQLVDEA-LQSRTKIEEEIYLIRIQLETTVKQKSTAESELK 2310
Cdd:pfam09731 106 KEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAkDDAIQAVKAHTDSLKEASDTAEISREKATDSAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2311 QLRERAAEAERLRKVAQEEAEKLHKqvieeTQKKRIAEKELQHKSEAEKEAAKQKQKALDD---LENLKKQAEEAERQVK 2387
Cdd:pfam09731 186 QKAEALAEKLKEVINLAKQSEEEAA-----PPLLDAAPETPPKLPEHLDNVEEKVEKAQSLaklVDQYKELVASERIVFQ 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2388 QAEVEKERQIKVAHVAAQKSAAAELqskhSSFVEKTskleeslkqeHGAVLQLQQEAAHLKKQqedainAREEAEKELEK 2467
Cdd:pfam09731 261 QELVSIFPDIIPVLKEDNLLSNDDL----NSLIAHA----------HREIDQLSKKLAELKKR------EEKHIERALEK 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2468 wRQKANEALRLRLQAEEEAHKkslaQEDAEKQKEEAEREAKKRAKAEESALKqkdmaeKELERQRKVADSTAQQKL-TAE 2546
Cdd:pfam09731 321 -QKEELDKLAEELSARLEEVR----AADEAQLRLEFEREREEIRESYEEKLR------TELERQAEAHEEHLKDVLvEQE 389
|
....*
gi 1678729579 2547 QELIR 2551
Cdd:pfam09731 390 IELQR 394
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2422-2555 |
4.62e-06 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 53.08 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2422 KTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEAlrlrlQAEEEAHKKSLAQED---AEK 2498
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEA-----KNLPKPADTSSPKEDkqvAEN 278
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678729579 2499 QKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQK-LTAEQELIRLRAD 2555
Cdd:pfam05262 279 QKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKeLEAQKKREPVAED 336
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3130-3433 |
4.63e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.23 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3130 RALADKMLKEKMQAIQEssrlkaeAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEyqksLEAERRRQLEIVAEAEK 3209
Cdd:pfam13868 9 RELNSKLLAAKCNKERD-------AQIAEKKRIKAEEKEEERRLDEMMEEERERALEEE----EEKEEERKEERKRYRQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3210 LKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKE-KMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLK 3288
Cdd:pfam13868 78 LEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEeKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3289 KEAEELQNKSKEMADAQQKQIEHEKTLLQQTFLTEREMLLKKeklieeekkklesQFEEEAKKSKALKDEQERQ---KQQ 3365
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDE-------------KAERDELRAKLYQEEQERKerqKER 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 3366 MEEEKK-KLHATMHEALSKQKEAEKEMLSKQKEMQELEKKRL-----EQEIILADENQKLREKLQQLEEAQKEQ 3433
Cdd:pfam13868 225 EEAEKKaRQRQELQQAREEQIELKERRLAEEAEREEEEFERMlrkqaEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
3092-3433 |
4.68e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3092 AEEAENMKRLAEDAARLSVESQEAARLRQiaedDLIQQRALADKML-KEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQK 3170
Cdd:pfam07888 16 EEGGTDMLLVVPRAELLQNRLEECLQERA----ELLQAQEAANRQReKEKERYKRDREQWERQRRELESRVAELKEELRQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3171 LLEDKQLMQRRLEEET---EEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEI 3247
Cdd:pfam07888 92 SREKHEELEEKYKELSassEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3248 ATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKskeMADAQQKQIEHEKTLLQQTFLTER--- 3324
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK---LTTAHRKEAENEALLEELRSLQERlna 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3325 ----------EMLLKKEKLIEEEKKKLESQFE------EEAKKSKALKDE-----QERQ--KQQMEEEKKKLHATMHEAL 3381
Cdd:pfam07888 249 serkveglgeELSSMAAQRDRTQAELHQARLQaaqltlQLADASLALREGrarwaQEREtlQQSAEADKDRIEKLSAELQ 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1678729579 3382 SKQKEAEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQLEEAQKEQ 3433
Cdd:pfam07888 329 RLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEK 380
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2832-3310 |
4.94e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2832 EEAARQRKIaqdeLERLKKKAEEARKQKDEADV-EAEVQIVAAQQAALK-------CSTAEHQVQSVLAQQKEDSIMHKK 2903
Cdd:COG4913 245 EDAREQIEL----LEPIRELAERYAAARERLAElEYLRAALRLWFAQRRlelleaeLEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2904 LKQEYEKAKKLAKEAEAAKEKAereaalLRQQAEEAERQKAAAEQEAAiqaKAQEDAERLRKEAEFEAA--KRAQAEGAA 2981
Cdd:COG4913 321 LREELDELEAQIRGNGGDRLEQ------LEREIERLERELEERERRRA---RLEALLAALGLPLPASAEefAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2982 LKQkqQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRgqVEE-----ELF 3056
Cdd:COG4913 392 LLE--ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD--EAElpfvgELI 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3057 KVKVQMEE---------------LL----------------KLKLRI------EDENQRLLKKDKDNSqkfLAEE---AE 3096
Cdd:COG4913 468 EVRPEEERwrgaiervlggfaltLLvppehyaaalrwvnrlHLRGRLvyervrTGLPDPERPRLDPDS---LAGKldfKP 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3097 N------MKRLAEDAARLSVESQEA-----------------ARLRQIAEDDLIQQR---------ALADkmLKEKMQAI 3144
Cdd:COG4913 545 HpfrawlEAELGRRFDYVCVDSPEElrrhpraitragqvkgnGTRHEKDDRRRIRSRyvlgfdnraKLAA--LEAELAEL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3145 QES-SRLKAEAEMLQRQKDLAQEQAQKL--LEDKQLMQRRLEEETEEYQkSLEAERRRQLEIVAEAEKLKLQVSQLSEAQ 3221
Cdd:COG4913 623 EEElAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIA-ELEAELERLDASSDDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3222 TKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEM 3301
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
|
....*....
gi 1678729579 3302 ADAQQKQIE 3310
Cdd:COG4913 782 LNRAEEELE 790
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
3010-3413 |
5.16e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 53.29 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3010 EQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDdaVKQRgqveeelfKVKVqmeellkLKLRIEDENQRLlkKDKDnsqK 3089
Cdd:pfam10174 358 ESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLD--VKER--------KINV-------LQKKIENLQEQL--RDKD---K 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3090 FLAEEAENMKRLAEDA-----ARLSVESQEAARLRQIaeDDLIQQRALADKMLKEKMQAI-QESSRLKAEAEMLQRQKdl 3163
Cdd:pfam10174 416 QLAGLKERVKSLQTDSsntdtALTTLEEALSEKERII--ERLKEQREREDRERLEELESLkKENKDLKEKVSALQPEL-- 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3164 aQEQAQKLLEDKQ----LMQRRLEEETeeYQKSLEAERRRQLEivaeaEKLKLQvSQLSEAQTkAEEEAKKFKKQADKIa 3239
Cdd:pfam10174 492 -TEKESSLIDLKEhassLASSGLKKDS--KLKSLEIAVEQKKE-----ECSKLE-NQLKKAHN-AEEAVRTNPEINDRI- 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3240 aRLHETEIATKEKMTVVEKLEFERL-----NTSKEAGDLRDAIADLEKDKARLKKEaeelqnKSKEMADAQQKQIEHEKT 3314
Cdd:pfam10174 561 -RLLEQEVARYKEESGKAQAEVERLlgilrEVENEKNDKDKKIAELESLTLRQMKE------QNKKVANIKHGQQEMKKK 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3315 LLQqtflterEMLLKKEKLIEEEKKKLESQFEEeakkskaLKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMLSK 3394
Cdd:pfam10174 634 GAQ-------LLEEARRREDNLADNSQQLQLEE-------LMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAER 699
|
410 420
....*....|....*....|
gi 1678729579 3395 QKEMQE-LEKKrleQEIILA 3413
Cdd:pfam10174 700 RKQLEEiLEMK---QEALLA 716
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4548-4582 |
5.56e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 5.56e-06
10 20 30
....*....|....*....|....*....|....*
gi 1678729579 4548 LLETQAATGFIVDPVNNETLTVDEAVRKGVVGPEI 4582
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
868-978 |
6.30e-06 |
|
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: 49.24 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 868 QKKTFTKWVNKHLIKRAESQH------HVTDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHKLQNVQIALDFL 937
Cdd:cd21324 25 EKYAFVNWINKALENDPDCKHvipmnpNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1678729579 938 RHRQVKLVNIRNDDIADGNPKLTLGLIWTVILHFQISDIQI 978
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3224-3433 |
6.54e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3224 AEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMAD 3303
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3304 AQQKQIEHEKTLLQ-------QTFLTEREMLLKKEklieeekkkleSQFEEEAKKSKALKDEQERQKQQMEEEKKKLHAT 3376
Cdd:COG3883 94 ALYRSGGSVSYLDVllgsesfSDFLDRLSALSKIA-----------DADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678729579 3377 MHEALSKQKEAEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQLEEAQKEQ 3433
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2971-3222 |
6.74e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2971 AAKRAQAEGAA---LKQKQQADAEMAKhkklAEQTLkQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQ 3047
Cdd:COG3206 167 ELRREEARKALeflEEQLPELRKELEE----AEAAL-EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3048 RGQVEEELFKVKVQMEELLklklriedENQRLlkkdkdnsQKFLAEEAENMKRLAEDAARLSVESQEAARLRQiaeddli 3127
Cdd:COG3206 242 LAALRAQLGSGPDALPELL--------QSPVI--------QQLRAQLAELEAELAELSARYTPNHPDVIALRA------- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3128 qQRALADKMLKEKMQAIQESSR-----LKAEAEMLQRQKDLAQEQAQKLLEdKQLMQRRLEEETEEYQKSLEA--ERRRQ 3200
Cdd:COG3206 299 -QIAALRAQLQQEAQRILASLEaeleaLQAREASLQAQLAQLEARLAELPE-LEAELRRLEREVEVARELYESllQRLEE 376
|
250 260
....*....|....*....|..
gi 1678729579 3201 LEIVAEAEKLKLQVsqLSEAQT 3222
Cdd:COG3206 377 ARLAEALTVGNVRV--IDPAVV 396
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1446-1538 |
6.77e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.71 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1446 HGFISAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDLQAMGERLVRDGHPGKKTVESFTA 1525
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1678729579 1526 ALQTQWSWILQLC 1538
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2238-2612 |
7.49e-06 |
|
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: 52.65 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2238 REIAAVDAEKQKQNIQLELHELKNLSEQQ--IKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLRER 2315
Cdd:COG5185 162 KDIFGKLTQELNQNLKKLEIFGLTLGLLKgiSELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDP 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2316 AAEAERLRKVAQEeaeklHKQVIEETQKkrIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAErqvKQAEVEKER 2395
Cdd:COG5185 242 ESELEDLAQTSDK-----LEKLVEQNTD--LRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYT---KSIDIKKAT 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2396 QIKVAhVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINARE------EAEKELEKWR 2469
Cdd:COG5185 312 ESLEE-QLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKsseeldSFKDTIESTK 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2470 QKANEALR-LRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQE 2548
Cdd:COG5185 391 ESLDEIPQnQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYD 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678729579 2549 LI--RLRADFDNAEQQRSLLEDELYRLKNEViaaQQQRKQLEDELAKVRSEMDILIQLKSKAEKET 2612
Cdd:COG5185 471 EInrSVRSKKEDLNEELTQIESRVSTLKATL---EKLRAKLERQLEGVRSKLDQVAESLKDFMRAR 533
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2274-2583 |
9.23e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2274 VDEALQSRTKIEEEIYLI--RIQLETTVKQKSTAESELKQLRERAAEAERLRK---VAQEEAEklhkQVI---------E 2339
Cdd:COG3206 73 LSSLSASDSPLETQIEILksRPVLERVVDKLNLDEDPLGEEASREAAIERLRKnltVEPVKGS----NVIeisytspdpE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2340 ETQK--KRIAEKELQHKSEAEKEAAKQKQKALDD-LENLKKQAEEAERQVKQ-------AEVEKERQIKVAHVAAQKSAA 2409
Cdd:COG3206 149 LAAAvaNALAEAYLEQNLELRREEARKALEFLEEqLPELRKELEEAEAALEEfrqknglVDLSEEAKLLLQQLSELESQL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2410 AELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAhlkkqQEDAINAREEAEKELEKWRQKANEA--LRLRLQAEEEAH 2487
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPV-----IQQLRAQLAELEAELAELSARYTPNhpDVIALRAQIAAL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2488 KKSLAQEdAEKQKEEAEREAKkRAKAEESALKQkdmaekELERQRKVADSTAQQkltaEQELIRLRADFDNAEQQ-RSLL 2566
Cdd:COG3206 304 RAQLQQE-AQRILASLEAELE-ALQAREASLQA------QLAQLEARLAELPEL----EAELRRLEREVEVARELyESLL 371
|
330
....*....|....*..
gi 1678729579 2567 EdelyRLKNEVIAAQQQ 2583
Cdd:COG3206 372 Q----RLEEARLAEALT 384
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
868-978 |
9.93e-06 |
|
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: 48.43 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 868 QKKTFTKWVNKHLIKRAESQHHV------TDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHKLQNVQIALDFL 937
Cdd:cd21292 25 EKVAFVNWINKNLGDDPDCKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1678729579 938 RHRQVKLVNIRNDDIADGNPKLTLGLIWTVILHFQISDIQI 978
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIRIGLFADIEL 145
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4747-4783 |
1.03e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 1.03e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1678729579 4747 RYLEGTSCIAGVFLESSKDRLSIYQAMKKNMIRPGTA 4783
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2175-2374 |
1.16e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.35 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2175 QRRLEDEEKaaKKLKAEEQKKMAEMQAELDKQKQlaaahAKAIAKAEKEAQELKLMMKEEVNRREIAAVDAEKQKQniQL 2254
Cdd:PRK09510 100 QERLKQLEK--ERLAAQEQKKQAEEAAKQAALKQ-----KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAK--KK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2255 ELHELKNLSEQQIKDKGqlvdeALQSRTKIEEEiyliriqlettVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKlh 2334
Cdd:PRK09510 171 AEAEAAKKAAAEAKKKA-----EAEAAAKAAAE-----------AKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAA-- 232
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678729579 2335 kqvieetQKKRIAEKELQHKSeAEKEAAKQKQKALDDLEN 2374
Cdd:PRK09510 233 -------EAKAAAEKAAAAKA-AEKAAAAKAAAEVDDLFG 264
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
2225-2521 |
1.26e-05 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 51.92 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2225 QELKLMMKEEVNRREIAAVDAekqkqniqleLHELKNLSEQQIKDKGQLVDEALQSRTKIE---EEIYLIRIQLETTVKQ 2301
Cdd:TIGR00927 606 KQIELWVKEQLSRRPVAKVMA----------LGDLSKGDVAEAEHTGERTGEEGERPTEAEgenGEESGGEAEQEGETET 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2302 KSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKE---LQHKSEAEKEAAKQKQKALDDLENLKKQ 2378
Cdd:TIGR00927 676 KGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEgteDEGEIETGEEGEEVEDEGEGEAEGKHEV 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2379 AEEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSK----HSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDA 2454
Cdd:TIGR00927 756 ETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKgdegAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQ 835
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678729579 2455 -INAREEAE-KELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQK 2521
Cdd:TIGR00927 836 eLNAENQGEaKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQK 904
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1952-2112 |
1.27e-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: 49.75 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1952 VPGDVKEVETYRTKLKKMRGEAEGEQPVFDSLEEElkkatvvSDKMSRVHSERDVELdhyRQHLSGLQDRWKAVFAQMDI 2031
Cdd:cd00176 28 YGDDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHPDAEEI---QERLEELNQRWEELRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2032 RQRELEQLGRQLGYYHESYDwLIHWITDAKERQEKIQAVSitDSKTLKEQLSQEKKLLEEIENNKDNVDECQKYAKAYIN 2111
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLE 174
|
.
gi 1678729579 2112 S 2112
Cdd:cd00176 175 E 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2658-2877 |
1.28e-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: 51.30 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2658 AARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSd 2737
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2738 AEMERQKAMVDDTLkqrRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRR 2817
Cdd:COG4942 97 AELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678729579 2818 REAEEKVKKITAAEEEAARQRKIAQDELERLKKKAEE-----ARKQKDEADVEAEVQIVAAQQAA 2877
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAElaaelAELQQEAEELEALIARLEAEAAA 238
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2525-2671 |
1.29e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2525 EKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRS-------- 2596
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyealq 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678729579 2597 -EMDILIQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKE 2671
Cdd:COG1579 96 kEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3346-3439 |
1.38e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3346 EEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQ--------KEAEKEMLSKQKEMQELEKKRL----EQEIIla 3413
Cdd:PRK00409 533 EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqqaiKEAKKEADEIIKELRQLQKGGYasvkAHELI-- 610
|
90 100
....*....|....*....|....*.
gi 1678729579 3414 DENQKLREKLQQLEEAQKEQHTVPDK 3439
Cdd:PRK00409 611 EARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
868-979 |
1.38e-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: 48.13 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 868 QKKTFTKWVNKHLIKRAESQH------HVTDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHKLQNVQIALDFL 937
Cdd:cd21325 25 EKYAFVNWINKALENDPDCRHvipmnpNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1678729579 938 RHRQVKLVNIRNDDIADGNPKLTLGLIWTVILHFQISDIQIN 979
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4748-4786 |
1.50e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 44.63 E-value: 1.50e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1678729579 4748 YLEGTSCIAGVFLESSKDRLSIYQAMKKNMIRPGTAFEL 4786
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2710-2884 |
1.72e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2710 QRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAmvddtLKQRRVVEEEIRIlklnfEKASSGKLDLELELNKLKNIA 2789
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQ-----LEKERLAAQEQKK-----QAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2790 EETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEE-----EAARQRKIAQDELERLKKKAEEARKQKDEADV 2864
Cdd:PRK09510 140 KAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEakkkaEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
170 180
....*....|....*....|
gi 1678729579 2865 EAEVQIVAAQQAALKCSTAE 2884
Cdd:PRK09510 220 AAEAKAAAAKAAAEAKAAAE 239
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2291-2621 |
1.81e-05 |
|
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: 51.45 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2291 IRIQLETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVieETQKKRIaekelqhkseaEKEAAKQKQKALD 2370
Cdd:pfam15964 319 VRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSEL--ERQKERL-----------EKELASQQEKRAQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2371 DLENLKKqaeeaerqvkqaEVEKERQIKVAHVAAQKSAAAELQSKHSSFV-EKTS---KLEESLKQEHGAVLQLQQEAAH 2446
Cdd:pfam15964 386 EKEALRK------------EMKKEREELGATMLALSQNVAQLEAQVEKVTrEKNSlvsQLEEAQKQLASQEMDVTKVCGE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2447 LKKQQEDAINAREEAEKELEKWRQKANEALRLrlqAEEEAHKKSLAQEDAEKQKEEAEREAkkrAKAEESALKQKDM--- 2523
Cdd:pfam15964 454 MRYQLNQTKMKKDEAEKEHREYRTKTGRQLEI---KDQEIEKLGLELSESKQRLEQAQQDA---ARAREECLKLTELlge 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2524 AEKELERQRKVADSTAQ--------QKLTAEQELIRLRADFDNAEQQRSLLEDELYRL---KNEVIAAQQQR-----KQL 2587
Cdd:pfam15964 528 SEHQLHLTRLEKESIQQsfsneakaQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLltsQNTFIAKLKEEcctlaKKL 607
|
330 340 350
....*....|....*....|....*....|....*...
gi 1678729579 2588 EDELAKVRSEMDILIQ----LKSKAEKETMSNTEKSKQ 2621
Cdd:pfam15964 608 EEITQKSRSEVEQLSQekeyLQDRLEKLQKRNEELEEQ 645
|
|
| DUF1663 |
pfam07909 |
Protein of unknown function (DUF1663); The members of this family are hypothetical proteins ... |
2368-2741 |
1.85e-05 |
|
Protein of unknown function (DUF1663); The members of this family are hypothetical proteins expressed by Trypanosoma cruzi, a eukaryotic parasite that causes Chagas' disease in humans. This region is found as multiple copies per protein.
Pssm-ID: 116521 [Multi-domain] Cd Length: 514 Bit Score: 50.97 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2368 ALDDLENLKkqAEEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQ-----EHGAVLQLQQ 2442
Cdd:pfam07909 96 SFDAAEALA--AEEDAARGQLVGEESSRVFHVVHDRIGREDAAGHHWVPEDALDAEERRETASRKcleleEAAAFDEIGE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2443 EAAHLKKQQEDAINAREEAEKELekwrqkanealrlrLQAEEEAHKKSLAQEDAEKQK-------EEAEREAKKRAKAEE 2515
Cdd:pfam07909 174 MMFQDRLIQAELRSARHEKAEEA--------------LAAEEDAAMCILAEEEREDTYglhrdaiDSEEHADRRRIEAGE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2516 SAlkqkdMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDE-LYRLKNEVIAAQQQ--RKQLEDELA 2592
Cdd:pfam07909 240 AA-----AEDFEEEKGEETADAKDWFFSAFELALEALAAEEDAARGKLVLEEREgNYGKHRDAIDSEEQatMNCLEKGEA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2593 KVRSEMDILIQLKSKAEKETMSNTEKSKQLLEAE---------------ATKMRDVAEEAGKLRAIAEEAKHQRQVAEEE 2657
Cdd:pfam07909 315 AAVDAGSTLAANFSKSEQELGEEYEEATDEIADEaiaaeediiihrnkaAARGELVGEEREDMCGLHKDAIDSETTTGEH 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2658 AARQRAEAERILKEKLaaiSEATHLKTEAEIALKEKEAENERLRRAAEDEayqrkALEDEANQHKKEIEEKIVQLKKSSD 2737
Cdd:pfam07909 395 AVRKLAHPPRLSVQKL---SSQTPLTTTNYNVLIETTTCIERDEAAARDE-----LLDEEILQLIKIIEETRLILTNKTN 466
|
....
gi 1678729579 2738 AEME 2741
Cdd:pfam07909 467 NDGE 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1957-2460 |
2.24e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1957 KEVETYRTKLKKMRGEAEGEQPVFDSLEEELKKA-TVVSDKMSRVHSERDVELDHYRQHLSGLQDRWKAVFAQMDIRQRE 2035
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAeEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2036 LEQLGRQLGYYHEsydwlihwITDAKERQEKIQAVSITDSKTLKEQLSQEKKLLEEIENNKDNVDECQKYAKAYINSIKD 2115
Cdd:COG1196 410 EALLERLERLEEE--------LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2116 YELQLvaynAQADPLASPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKKLKAEEQKK 2195
Cdd:COG1196 482 LLEEL----AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2196 MAEMQAELDKQKQL----AAAHAKAIAKAEKEAQELKLMMKEEVNRREIAAVDAEKQKQNIQLELHELKNLSEQQIKDKG 2271
Cdd:COG1196 558 VAAAAIEYLKAAKAgratFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2272 QLVDEALQSRTKIEEEIYLIRIQLETtvkQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKEL 2351
Cdd:COG1196 638 RAVTLAGRLREVTLEGEGGSAGGSLT---GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2352 QHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKERQIKVAhvaaqksaaaELQskhssfvEKTSKLEESLk 2431
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE----------ELE-------RELERLEREI- 776
|
490 500 510
....*....|....*....|....*....|....*..
gi 1678729579 2432 QEHGAV--------LQLQQEAAHLKKQQEDAINAREE 2460
Cdd:COG1196 777 EALGPVnllaieeyEELEERYDFLSEQREDLEEARET 813
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3146-3405 |
2.33e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3146 ESSRLKAEAEMLQRQ-KDLaqEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQleiVAEAEKLKLQVSQLSEAQTKA 3224
Cdd:COG4913 219 EEPDTFEAADALVEHfDDL--ERAHEALEDAREQIELLEPIRELAERYAAARERLA---ELEYLRAALRLWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3225 EEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNtskeAGDlrDAIADLEKDKARLKKEAEELQNKSKEMADA 3304
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRG----NGG--DRLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3305 QQKqiehektlLQQTFLTEREmllkkeklieeekkklesQFEEEAKKSKALKDeqerqkqQMEEEKKKLHATMHEALSKQ 3384
Cdd:COG4913 368 LAA--------LGLPLPASAE------------------EFAALRAEAAALLE-------ALEEELEALEEALAEAEAAL 414
|
250 260
....*....|....*....|.
gi 1678729579 3385 KEAEKEMLSKQKEMQELEKKR 3405
Cdd:COG4913 415 RDLRRELRELEAEIASLERRK 435
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
3049-3318 |
2.38e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 50.73 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3049 GQVEEELFKVKVQMEELLKLKLRIEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDAARLSVESQEAA-RLRQIAEDDLI 3127
Cdd:COG5185 228 IINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKeKIAEYTKSIDI 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3128 QQRALADKMLKEKMQAIQESSRLKAEAEM----LQRQKDLAQEQAQKLLE--DKQLMQ-------RRLEEETEEYQKSLE 3194
Cdd:COG5185 308 KKATESLEEQLAAAEAEQELEESKRETETgiqnLTAEIEQGQESLTENLEaiKEEIENivgevelSKSSEELDSFKDTIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3195 AERRRQLEIVAEAEK-LKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHE---------TEIATKEKMTVVEKLEFERL 3264
Cdd:COG5185 388 STKESLDEIPQNQRGyAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEvskllneliSELNKVMREADEESQSRLEE 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 3265 NTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQQ 3318
Cdd:COG5185 468 AYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQ 521
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
984-1087 |
2.48e-05 |
|
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: 46.52 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 984 DMSAKEKLLLW-SQRMT-GDYQNIRCDNFSTSWRDGKLFNAVIHKHHPRLID---MGKVYRQSNLE-NLEQAFNVAERdL 1057
Cdd:cd21218 8 YLPPEEILLRWvNYHLKkAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelVLEVLSEEDLEkRAEKVLQAAEK-L 86
|
90 100 110
....*....|....*....|....*....|
gi 1678729579 1058 GVTRLLDPEdvDVQHPDEKSIITYVSSLYD 1087
Cdd:cd21218 87 GCKYFLTPE--DIVSGNPRLNLAFVATLFN 114
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2449-2535 |
2.53e-05 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 47.46 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2449 KQQEDAINAREEAEKELEKWRQKANEALRlrlQAEEEAHKkslAQEDAEKQKEEAEREAKKRAKAEESALKQKdmAEKEL 2528
Cdd:PRK05759 38 KKIADGLAAAERAKKELELAQAKYEAQLA---EARAEAAE---IIEQAKKRAAQIIEEAKAEAEAEAARIKAQ--AQAEI 109
|
....*..
gi 1678729579 2529 ERQRKVA 2535
Cdd:PRK05759 110 EQERKRA 116
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2935-3233 |
2.54e-05 |
|
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: 50.91 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2935 QAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQAEGAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELT 3014
Cdd:pfam09731 157 QAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3015 KVKLKLDDTDKQKSL-------LDDELQRLKDEVDDAVKQRGQVEEELFKVKVqmeelLKLKLRIEDENQRLLKKdKDNS 3087
Cdd:pfam09731 237 KAQSLAKLVDQYKELvaserivFQQELVSIFPDIIPVLKEDNLLSNDDLNSLI-----AHAHREIDQLSKKLAEL-KKRE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3088 QKFLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRaladkmlkeKMQAIQESSRLKAEAEmLQRQKDLAQEQ 3167
Cdd:pfam09731 311 EKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFER---------EREEIRESYEEKLRTE-LERQAEAHEEH 380
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678729579 3168 AQK-LLEDKQLMQRRLEEETEEyqkSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKK 3233
Cdd:pfam09731 381 LKDvLVEQEIELQREFLQDIKE---KVEEERAGRLLKLNELLANLKGLEKATSSHSEVEDENRKAQQ 444
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2459-2800 |
2.70e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2459 EEAEKELEKWRQKANEALRLrlqAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADST 2538
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAA---LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2539 AQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEK 2618
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2619 SKQLLEAEATKMRDVAEEA-GKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAEN 2697
Cdd:COG4372 166 LAALEQELQALSEAEAEQAlDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2698 ERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLD 2777
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340
....*....|....*....|...
gi 1678729579 2778 LELELNKLKNIAEETQQSKLRAE 2800
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLV 348
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4956-4984 |
2.75e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.75e-05
10 20
....*....|....*....|....*....
gi 1678729579 4956 VRKRRVVIVDPETGKEMTVYEAYRKGLID 4984
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2322-2548 |
3.28e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 50.08 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2322 LRKVAQEEAEKlHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKERQIKVah 2401
Cdd:PRK11637 49 LKSIQQDIAAK-EKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERL-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2402 VAAQKSAAAElQSKHSSfVEKTSKLEESLKQEhgavlQLQQEAAHLKKQQEDAINAREEAEKELEKwrQKANealrlrLQ 2481
Cdd:PRK11637 126 LAAQLDAAFR-QGEHTG-LQLILSGEESQRGE-----RILAYFGYLNQARQETIAELKQTREELAA--QKAE------LE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 2482 AEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAE-ESALK--QKDMAE---KELERQRKVADSTAQQKLTAEQE 2548
Cdd:PRK11637 191 EKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGlESSLQkdQQQLSElraNESRLRDSIARAEREAKARAERE 263
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2729-3089 |
3.37e-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: 50.51 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2729 IVQLKKSSDaemERQKAMVDDTLKQRRVVEEEIrilklnfEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEaeklrK 2808
Cdd:pfam17380 277 IVQHQKAVS---ERQQQEKFEKMEQERLRQEKE-------EKAREVERRRKLEEAEKARQAEMDRQAAIYAEQE-----R 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2809 LALEEEKRRREAEEKVKKitaAEEEAARQRKIAQD-----ELERLKKKaeeaRKQKDEAdVEAEVqivaaqQAALKCSTA 2883
Cdd:pfam17380 342 MAMERERELERIRQEERK---RELERIRQEEIAMEisrmrELERLQME----RQQKNER-VRQEL------EAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2884 EHQVQSVLAQQKEDSIMHKKLKQEyekakklAKEAEAAKEKAEREAALLRQQAEEAERQKAAAEQEaaiqakaQEDAERL 2963
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEE-------ARQREVRRLEEERAREMERVRLEEQERQQQVERLR-------QQEEERK 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2964 RKEAEFEAAKRAQAEGAALKQKQQADAEMAKHKKLAEQTLKQKFqVEQELtkvklklddTDKQKSLLDDELQRLKDEvdd 3043
Cdd:pfam17380 474 RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL-LEKEM---------EERQKAIYEEERRREAEE--- 540
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1678729579 3044 avKQRGQVE-EELFKVKVQMEELLKLKLRIE--DENQRLLKKDKDNSQK 3089
Cdd:pfam17380 541 --ERRKQQEmEERRRIQEQMRKATEERSRLEamEREREMMRQIVESEKA 587
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1922-2396 |
3.43e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1922 LKTVEMVIRNTQGAEGVLKQYEDCLREVHTVPGDVKEVETYRTKLKKMRGEAEGEQPVFDSLEEELKKATVVSDKMSRVH 2001
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2002 serdvELDHYRQHLSGLQDRWKAVFAQMDIRQRELEQLGRQLGYYHESYdwlihwITDAKERQEKIQAvsitDSKTLKEQ 2081
Cdd:COG4717 150 -----ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE------LQDLAEELEELQQ----RLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2082 LSQEKKLLEEIENNKDNVdECQKYAKAYINSIKDYELQLVAynaqADPLASPLKKTKLDSASDNIIQEYVTLRTrysELM 2161
Cdd:COG4717 215 LEEAQEELEELEEELEQL-ENELEAAALEERLKEARLLLLI----AAALLALLGLGGSLLSLILTIAGVLFLVL---GLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2162 TLTSQYIKFITETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELklmmkeevnRREIA 2241
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL---------LREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2242 AVDAEKQKQNIQLELHELknLSEQQIKDKGQLVD--EALQSRTKIEEEIYLIRIQLE--TTVKQKSTAESELKQLRERAA 2317
Cdd:COG4717 358 ELEEELQLEELEQEIAAL--LAEAGVEDEEELRAalEQAEEYQELKEELEELEEQLEelLGELEELLEALDEEELEEELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2318 EAERLRKVAQEEAEKLHKQVIE-ETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQaEVEKERQ 2396
Cdd:COG4717 436 ELEEELEELEEELEELREELAElEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEARE-EYREERL 514
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2306-2431 |
3.46e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2306 ESELKQLRERAAEAERLRKvaqeEAEKLHKQVieETQKKRIAEKElqhkseaEKEAAKQKQKALDDLENLKKQAEEAERQ 2385
Cdd:PRK00409 526 EELERELEQKAEEAEALLK----EAEKLKEEL--EEKKEKLQEEE-------DKLLEEAEKEAQQAIKEAKKEADEIIKE 592
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1678729579 2386 VKQAEVEKERQIKvahvaaqksaAAELQSKHSSFVEKTSKLEESLK 2431
Cdd:PRK00409 593 LRQLQKGGYASVK----------AHELIEARKRLNKANEKKEKKKK 628
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2169-2363 |
3.65e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2169 KFITETQrrLEDEEKAAKKLKAEeqkkmAEMQAELDKQkqlaaahakaiakaekeaqELKLMMKEEVNRREIaavDAEKQ 2248
Cdd:PRK12704 26 KKIAEAK--IKEAEEEAKRILEE-----AKKEAEAIKK-------------------EALLEAKEEIHKLRN---EFEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2249 KQNIQLELHELknlsEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLRERA-AEAERLRKVAQ 2327
Cdd:PRK12704 77 LRERRNELQKL----EKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQlQELERISGLTA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678729579 2328 EEA-EKLHKQVIEETQK---KRIAEKELQHKSEAEKEAAK 2363
Cdd:PRK12704 153 EEAkEILLEKVEEEARHeaaVLIKEIEEEAKEEADKKAKE 192
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
3074-3274 |
3.68e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3074 DENQRLLKKDKDNSQKFLAEEAENMK-RLAEDAARL----------SVESQEAARLRQIAE------------DDLIQQR 3130
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRkELEEAEAALeefrqknglvDLSEEAKLLLQQLSElesqlaearaelAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3131 ALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQA---QKLLEDKQLMQRrLEEETEEYQKSLEAERRRQL-EIVAE 3206
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAelsARYTPNHPDVIA-LRAQIAALRAQLQQEAQRILaSLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678729579 3207 AEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLR 3274
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2955-3201 |
3.70e-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: 49.76 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2955 KAQEDAERLRKE---AEFEAAKRAQAEGAALKQKQQADAEMAKhkklAEQTLKqkfQVEQELTKVKLKLDDTDKQKSLLD 3031
Cdd:COG4942 24 EAEAELEQLQQEiaeLEKELAALKKEEKALLKQLAALERRIAA----LARRIR---ALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3032 DELQRLKDEVddavkqrgqveEELFKVKVQMEELLKLKLRIEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDAARLSVE 3111
Cdd:COG4942 97 AELEAQKEEL-----------AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3112 SQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQK 3191
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
250
....*....|
gi 1678729579 3192 SLEAERRRQL 3201
Cdd:COG4942 246 AGFAALKGKL 255
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2248-2744 |
3.74e-05 |
|
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: 50.07 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2248 QKQNIQLELHELKNLSEQqikdkgqlVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLRERAAEAERLRKVAQ 2327
Cdd:pfam05622 29 EKNSLQQENKKLQERLDQ--------LESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2328 EEAEKLHKqVIEETQKKRIAEKELQHKS------EAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKERQIKVA- 2400
Cdd:pfam05622 101 HRNEELTS-LAEEAQALKDEMDILRESSdkvkklEATVETYKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKAn 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2401 ----HVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEdaiNAREeaekelekwrqkANEAL 2476
Cdd:pfam05622 180 alrgQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERD---TLRE------------TNEEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2477 RLrlqAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEesaLKQKDMaekELERQRKVAdsTAQQKLTAEQELIRLRADF 2556
Cdd:pfam05622 245 RC---AQLQQAELSQADALLSPSSDPGDNLAAEIMPAE---IREKLI---RLQHENKML--RLGQEGSYRERLTELQQLL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2557 DNAEQQRSLLEDELyRLKNEVIAA-QQQRKQLEDELAKVRSEMDILIQLKSKAEK------ETMSNTEKSKQLLE----- 2624
Cdd:pfam05622 314 EDANRRKNELETQN-RLANQRILElQQQVEELQKALQEQGSKAEDSSLLKQKLEEhleklhEAQSELQKKKEQIEelepk 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2625 AEATKMRDVAEEAGKLRAIAEEAKhqrqVAEEEAARQRAEAERILK-----EKLAAISEATHLKT-----EAEIALKEKE 2694
Cdd:pfam05622 393 QDSNLAQKIDELQEALRKKDEDMK----AMEERYKKYVEKAKSVIKtldpkQNPASPPEIQALKNqllekDKKIEHLERD 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 2695 AENERLRRAAEDE----AYQRKALedeaNQHKKEIEEKIVQLKKSSDAEMERQK 2744
Cdd:pfam05622 469 FEKSKLQREQEEKlivtAWYNMGM----ALHRKAIEERLAGLSSPGQSFLARQR 518
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2299-2546 |
3.75e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.60 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2299 VKQKSTAESELKQlRERAaEAERlRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDD------- 2371
Cdd:NF012221 1551 AKQDDAAQNALAD-KERA-EADR-QRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEESRAVTKelttlaq 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2372 -LENLKKQAEEAERQVKQ-----AEVEKERqIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQeaa 2445
Cdd:NF012221 1628 gLDALDSQATYAGESGDQwrnpfAGGLLDR-VQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQ--- 1703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2446 HLKKQQEDAINAREEAEKelekwRQKanEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAK-KRAKAEESALKQKDMA 2524
Cdd:NF012221 1704 NQANAEQDIDDAKADAEK-----RKD--DALAKQNEAQQAESDANAAANDAQSRGEQDASAAEnKANQAQADAKGAKQDE 1776
|
250 260
....*....|....*....|..
gi 1678729579 2525 EKELERQRKVADSTAQQKLTAE 2546
Cdd:NF012221 1777 SDKPNRQGAAGSGLSGKAYSVE 1798
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3145-3404 |
3.80e-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: 49.76 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3145 QESSRLKAEAEMLQRQKDLAQeqAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKlqvSQLSEAQTKA 3224
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAE--LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3225 EEEAKKFKKQADKIAARLheteiATKEKMTVVEKLEFerLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMAdA 3304
Cdd:COG4942 93 AELRAELEAQKEELAELL-----RALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA-A 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3305 QQKQIEHEKTLLQQTflteremllkkeklieeekkklESQFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQ 3384
Cdd:COG4942 165 LRAELEAERAELEAL----------------------LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
250 260
....*....|....*....|
gi 1678729579 3385 KEAEKEMLSKQKEMQELEKK 3404
Cdd:COG4942 223 EELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2559-2729 |
3.95e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2559 AEQQRSLLEdeLYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKEtMSNTEKSKQLLEAEatkMRDVAEEAG 2638
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLELE---IEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2639 KLRAIAEEAKHQRQVA-----EEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKA 2713
Cdd:COG1579 77 KYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*.
gi 1678729579 2714 LEDEANQHKKEIEEKI 2729
Cdd:COG1579 157 ELEELEAEREELAAKI 172
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3162-3365 |
4.24e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3162 DLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAAR 3241
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3242 LHETEIATKEKMTVVEKLEFERLNT-----SKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMADAQQKQIEHEKTLL 3316
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSDFLDrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1678729579 3317 QQtfLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQQ 3365
Cdd:COG3883 175 AQ--QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3091-3436 |
4.30e-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: 50.35 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3091 LAEEAENMKRLAEdaARLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQK 3170
Cdd:TIGR00618 181 LALMEFAKKKSLH--GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3171 lleDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATK 3250
Cdd:TIGR00618 259 ---QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3251 EKMTVVEKLEFERLNTSKEagdlrDAIADlEKDKARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQ------------- 3317
Cdd:TIGR00618 336 QQSSIEEQRRLLQTLHSQE-----IHIRD-AHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQslckeldilqreq 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3318 --QTFLTERE-------MLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAE 3388
Cdd:TIGR00618 410 atIDTRTSAFrdlqgqlAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKK 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 3389 KEMLSKQKEMQELEK------KRLEQEIILADENQKLREKLQQLEEAQKEQHTV 3436
Cdd:TIGR00618 490 AVVLARLLELQEEPCplcgscIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETS 543
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2304-2472 |
4.92e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2304 TAESELKQLRE------RAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQhksEAEKEAAKQKQkaldDLENLKK 2377
Cdd:COG1579 1 AMPEDLRALLDlqeldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE---DLEKEIKRLEL----EIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2378 QAEEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINA 2457
Cdd:COG1579 74 RIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170
....*....|....*
gi 1678729579 2458 REEAEKELEKWRQKA 2472
Cdd:COG1579 154 LEAELEELEAEREEL 168
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2740-3433 |
4.99e-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: 49.75 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2740 MERQKAMVDDTLKQRRVVEEEIRILKlnfekassgkldlelelnklkniaEETQQSKLRAEEEAEKLRKLALeeekrrre 2819
Cdd:pfam07111 61 LSQQAELISRQLQELRRLEEEVRLLR------------------------ETSLQQKMRLEAQAMELDALAV-------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2820 aeekVKKITAAEEEAARQrkiAQDELERLKKKAEEARKQKDEadveaEVQIVaaqqaalkcstaeHQVQ-SVLAQQKEDS 2898
Cdd:pfam07111 109 ----AEKAGQAEAEGLRA---ALAGAEMVRKNLEEGSQRELE-----EIQRL-------------HQEQlSSLTQAHEEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2899 IMHKKLKQEyekakklakeaeaakEKAEREAALLRQQAEEAERqkaaaeqeaaiQAKAQEDAERLRKEAEfeaakraqae 2978
Cdd:pfam07111 164 LSSLTSKAE---------------GLEKSLNSLETKRAGEAKQ-----------LAEAQKEAELLRKQLS---------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2979 gaalKQKQQADAEMAKHKKLaeqtlkQKFQVEQELTKVKLKLDDTDKQKSLldDELQRLKDEVDDAvkqrgQVEEELFKV 3058
Cdd:pfam07111 208 ----KTQEELEAQVTLVESL------RKYVGEQVPPEVHSQTWELERQELL--DTMQHLQEDRADL-----QATVELLQV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3059 KVQ-MEELLKLKlriEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDAARLSVesqeaarlrQIAEDDLiqQRALADKML 3137
Cdd:pfam07111 271 RVQsLTHMLALQ---EEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMV---------QLKAQDL--EHRDSVKQL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3138 KEKMQAIQESSRLKAEAEMLQrQKDLAQEQAQklLEDKQLMQRRLEEETEEYQkslEAERRRQLEIVAEAEKLKLQVSQL 3217
Cdd:pfam07111 337 RGQVAELQEQVTSQSQEQAIL-QRALQDKAAE--VEVERMSAKGLQMELSRAQ---EARRRQQQQTASAEEQLKFVVNAM 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3218 SEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTV---------VEKLEFERLNTSKEA----GDLRDAIADLEKDK 3284
Cdd:pfam07111 411 SSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIkglmarkvaLAQLRQESCPPPPPAppvdADLSLELEQLREER 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3285 ARLKKE----AEELQN---KSKEMADAQQKQIEHEKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKD 3357
Cdd:pfam07111 491 NRLDAElqlsAHLIQQevgRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQ 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3358 EQERQKQQMEEEKKKLHATMHEALSKQK----EAEKEMLSKQKEMQELEKKRLEQEiilaDENQKLReKLQqlEEAQKEQ 3433
Cdd:pfam07111 571 QQEIYGQALQEKVAEVETRLREQLSDTKrrlnEARREQAKAVVSLRQIQHRATQEK----ERNQELR-RLQ--DEARKEE 643
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2326-2763 |
4.99e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 49.65 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2326 AQEEAEKLHKQVIEEtQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAevEKERQIKVAHVAAQ 2405
Cdd:COG3064 1 AQEALEEKAAEAAAQ-ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAE--AEQRAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2406 KSAAAElqskhssfvEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAinareeAEKELEKWRQKANEALRLRLQAE-E 2484
Cdd:COG3064 78 KLAEAE---------KAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAA------EKEKAEEAKRKAEEEAKRKAEEErK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2485 EAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRS 2564
Cdd:COG3064 143 AAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2565 LLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIA 2644
Cdd:COG3064 223 ARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2645 EEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKE 2724
Cdd:COG3064 303 LAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLAD 382
|
410 420 430
....*....|....*....|....*....|....*....
gi 1678729579 2725 IEEKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRI 2763
Cdd:COG3064 383 VEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELR 421
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2314-2624 |
5.53e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.48 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2314 ERAAEAERLRKvAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQ-AEEAERQVKQAEVE 2392
Cdd:pfam02029 4 EEEAARERRRR-AREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRtAKREERRQKRLQEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2393 KERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDA---INAREEAEKELEKWR 2469
Cdd:pfam02029 83 LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKwstEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2470 QKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKR--------AKAEESALKQKDMAEKELERQRKVADSTAQQ 2541
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGhpevksqnGEEEVTKLKVTTKRRQGGLSQSQEREEEAEV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2542 KLTAEQELIRLRADFDNAE----------QQRSLLEDELYRLKNE----VIAAQQQRKQLEDELAKVRSEMDILiQLKSK 2607
Cdd:pfam02029 243 FLEAEQKLEELRRRRQEKEseefeklrqkQQEAELELEELKKKREerrkLLEEEEQRRKQEEAERKLREEEEKR-RMKEE 321
|
330
....*....|....*..
gi 1678729579 2608 AEKETMSNTEKSKQLLE 2624
Cdd:pfam02029 322 IERRRAEAAEKRQKLPE 338
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4252-4288 |
5.63e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 5.63e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1678729579 4252 KLLSAEKAVTGYKDPYTGNKISLFEAVQKDLIPKEHA 4288
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2402-2547 |
5.68e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2402 VAAQKSAAAELQSKHssFVEKTSKLEESLKQEhgAVLQLQQEAAHLKKQQEDAINAREEAEKELEKwrqkanealrlRLQ 2481
Cdd:PRK12704 28 IAEAKIKEAEEEAKR--ILEEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELRERRNELQKLEK-----------RLL 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678729579 2482 AEEEAHKKSLaqEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQqkLTAEQ 2547
Cdd:PRK12704 93 QKEENLDRKL--ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG--LTAEE 154
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
3143-3432 |
5.92e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.48 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3143 AIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLE----AERRRQLEIVAEAEKLKLQVSQLS 3218
Cdd:pfam02029 15 AREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDrtakREERRQKRLQEALERQKEFDPTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3219 EAQTKAEEEAKKFKKQADKIAARLHETE----IATKEKMTVVEKLEFERLntsKEAGDLRDAIADLEKDKARLKKEAEEL 3294
Cdd:pfam02029 95 DEKESVAERKENNEEEENSSWEKEEKRDsrlgRYKEEETEIREKEYQENK---WSTEVRQAEEEGEEEEDKSEEAEEVPT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3295 QNKSKEMADAQQKQIEHEKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQER-QKQQMEEEKKKL 3373
Cdd:pfam02029 172 ENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEeAEVFLEAEQKLE 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678729579 3374 HATMHEALSKQKEAEKEMLSKQK---EMQELEKKRLEQEIILADENQKLREklqqlEEAQKE 3432
Cdd:pfam02029 252 ELRRRRQEKESEEFEKLRQKQQEaelELEELKKKREERRKLLEEEEQRRKQ-----EEAERK 308
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
2458-2533 |
6.21e-05 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 48.72 E-value: 6.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678729579 2458 REEAEKELEKWRQKANEALRLRLQAEEeahkkslaQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRK 2533
Cdd:pfam07946 255 RPEALKKAKKTREEEIEKIKKAAEEER--------AEEAQEKKEEAKKKEREEKLAKLSPEEQRKYEEKERKKEQR 322
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2449-2644 |
6.24e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 49.63 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2449 KQQEDAinAREEAEKeLEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKdmAEKEL 2528
Cdd:PTZ00491 662 KSQEAA--ARHQAEL-LEQEARGRLERQKMHDKAKAEEQRTKLLELQAESAAVESSGQSRAEALAEAEARLIE--AEAEV 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2529 ErqrkvadstaQQKLTAEQELIrlradfdnaeqqrslledelyrLKNEVIAAQQQRKQLEDELAKVRSEMDIliqlkska 2608
Cdd:PTZ00491 737 E----------QAELRAKALRI----------------------EAEAELEKLRKRQELELEYEQAQNELEI-------- 776
|
170 180 190
....*....|....*....|....*....|....*...
gi 1678729579 2609 eketmsntEKSKQLLEAEATKMRDVAEEAGK--LRAIA 2644
Cdd:PTZ00491 777 --------AKAKELADIEATKFERIVEALGRetLIAIA 806
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
3142-3304 |
7.51e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 49.25 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3142 QAIQESSRLKAE-----AEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEEteeyqksleAERRRQLEivAEAEKLKLQVSQ 3216
Cdd:PTZ00491 647 DSLQKSVQLAIEittksQEAAARHQAELLEQEARGRLERQKMHDKAKAE---------EQRTKLLE--LQAESAAVESSG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3217 LSEAQTKAEEEAKKFKKQADKIAARLH--------ETEIAtKEKMTVVEKLEFERlntskeagdlrdAIADLEKDKARLK 3288
Cdd:PTZ00491 716 QSRAEALAEAEARLIEAEAEVEQAELRakalrieaEAELE-KLRKRQELELEYEQ------------AQNELEIAKAKEL 782
|
170
....*....|....*.
gi 1678729579 3289 KEAEelQNKSKEMADA 3304
Cdd:PTZ00491 783 ADIE--ATKFERIVEA 796
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2437-2712 |
7.67e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 48.88 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2437 VLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRL-------QAEEEAHKKSLAQEDAEK----QKEEAER 2505
Cdd:pfam15558 13 MLARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLqqsqeqwQAEKEQRKARLGREERRRadrrEKQVIEK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2506 EAKKRAKAE--ESALKQKDMAEKELERQRKvadSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEViaAQQQ 2583
Cdd:pfam15558 93 ESRWREQAEdqENQRQEKLERARQEAEQRK---QCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKER--EEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2584 RKQLEDELAKVRSE-MDILIQLKSKAEKETMSNT---------EKSKQLLEAEATKMRDVA--EEAGKLRA--IAEEAKH 2649
Cdd:pfam15558 168 KVQENNLSELLNHQaRKVLVDCQAKAEELLRRLSleqslqrsqENYEQLVEERHRELREKAqkEEEQFQRAkwRAEEKEE 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 2650 QRQ------VAEEEAARQRAE--AERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRK 2712
Cdd:pfam15558 248 ERQehkealAELADRKIQQARqvAHKTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKK 318
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2459-2875 |
7.89e-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: 49.24 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2459 EEAEKELEKWRQKANEALRLRLQaeeEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALK-QKDMAE---KELERQRKV 2534
Cdd:NF033838 72 SEIQKSLDKRKHTQNVALNKKLS---DIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQfKKDTLEpgkKVAEATKKV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2535 ADstAQQKLTAEQElirlradfdnaEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVrsemdiliQLKSKAEKETMS 2614
Cdd:NF033838 149 EE--AEKKAKDQKE-----------EDRRNYPTNTYKTLELEIAESDVEVKKAELELVKE--------EAKEPRDEEKIK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2615 NTEKSKQLLEAEATKMrdvaeeagklraiaEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKteaeialkeke 2694
Cdd:NF033838 208 QAKAKVESKKAEATRL--------------EKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPK----------- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2695 aenERLRRAAEDEAYQRKALEDEANQHKKEIEEKIV---QLKKSSD-AEMERQKAMVDDTLKQRRvvEEEIRILKLNFEK 2770
Cdd:NF033838 263 ---RRAKRGVLGEPATPDKKENDAKSSDSSVGEETLpspSLKPEKKvAEAEKKVEEAKKKAKDQK--EEDRRNYPTNTYK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2771 ASS---GKLDLELELNKLKNIAEETQQSK-------LRAEEEAEKL-----------RKLALEEEKRRREAEEKVKKITA 2829
Cdd:NF033838 338 TLEleiAESDVKVKEAELELVKEEAKEPRneekikqAKAKVESKKAeatrlekiktdRKKAEEEAKRKAAEEDKVKEKPA 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 2830 AEEEAAR----QRKIAQDELERLKKKAEEARKQKDEAD----VEAEVQIVAAQQ 2875
Cdd:NF033838 418 EQPQPAPapqpEKPAPKPEKPAEQPKAEKPADQQAEEDyarrSEEEYNRLTQQQ 471
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2970-3285 |
8.41e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.53 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2970 EAAKRAQAEGAALKQKQQADAE----MAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAV 3045
Cdd:pfam19220 87 ELVARLAKLEAALREAEAAKEElrieLRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3046 KQRGQVEEELFKVKVQMEELLklklrieDENQRLLKKDKDNSQKFLAEEAenmkRLAEDAARLSVESQEAARLRQIAEDD 3125
Cdd:pfam19220 167 ERLALLEQENRRLQALSEEQA-------AELAELTRRLAELETQLDATRA----RLRALEGQLAAEQAERERAEAQLEEA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3126 LIQQRAlADKMLKEKMQAIQE----SSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEyqksLEAERRRQL 3201
Cdd:pfam19220 236 VEAHRA-ERASLRMKLEALTAraaaTEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAG----LEADLERRT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3202 EIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLhETEIATKEKMTVVEKLEFERLNtskeagdlRDAIADLE 3281
Cdd:pfam19220 311 QQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASL-SDRIAELTKRFEVERAALEQAN--------RRLKEELQ 381
|
....
gi 1678729579 3282 KDKA 3285
Cdd:pfam19220 382 RERA 385
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3061-3242 |
8.59e-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: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3061 QMEELLKLKlRIEDENQRLlKKDKDNSQKFLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKmLKEK 3140
Cdd:COG1579 5 DLRALLDLQ-ELDSELDRL-EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3141 MQAIQeSSRlkaEAEMLQRQKDlAQEQAQKLLEDKQLmqrRLEEETEEYQKSLEAERRRQLEIVAEAEKLKlqvSQLSEA 3220
Cdd:COG1579 82 LGNVR-NNK---EYEALQKEIE-SLKRRISDLEDEIL---ELMERIEELEEELAELEAELAELEAELEEKK---AELDEE 150
|
170 180
....*....|....*....|..
gi 1678729579 3221 QTKAEEEAKKFKKQADKIAARL 3242
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2496-2719 |
8.93e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2496 AEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELyrlkN 2575
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL----G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2576 EVIAAQQQRKQLEDELAKV--------------------RSEMDILIQLKSKAEKetmsnTEKSKQLLEAEATKMRDVAE 2635
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLlgsesfsdfldrlsalskiaDADADLLEELKADKAE-----LEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2636 EAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALE 2715
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
....
gi 1678729579 2716 DEAN 2719
Cdd:COG3883 245 SAAG 248
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2306-2467 |
8.99e-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: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2306 ESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQ-----KKRIAEKELQHKSEAEKEAAKQKQ----KALDDLENLK 2376
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTeledlEKEIKRLELEIEEVEARIKKYEEQlgnvRNNKEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2377 KQAEEAERQVKQAEvEKERQIKVAhVAAQKSAAAELQSKHssfvektSKLEESLKQEHGavlQLQQEAAHLKKQQEDAIN 2456
Cdd:COG1579 96 KEIESLKRRISDLE-DEILELMER-IEELEEELAELEAEL-------AELEAELEEKKA---ELDEELAELEAELEELEA 163
|
170
....*....|.
gi 1678729579 2457 AREEAEKELEK 2467
Cdd:COG1579 164 EREELAAKIPP 174
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2957-3424 |
9.08e-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: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2957 QEDAERLRK-EAEFEAAKRAQAEgaALKQKQQADAEMAKHKKLAEQTLKQKFQV----EQELTKVKLKLDDTDKQKSLLD 3031
Cdd:pfam05557 54 QKRIRLLEKrEAEAEEALREQAE--LNRLKKKYLEALNKKLNEKESQLADAREVisclKNELSELRRQIQRAELELQSTN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3032 DELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLLKKDKDnsqkflAEEAENMK----RLAEDAAR 3107
Cdd:pfam05557 132 SELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQD------SEIVKNSKselaRIPELEKE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3108 LSVESQEAARLRQIAEDDLIQQRALADKMLK----EKMQAiqESSRLKAEAEMLQRQ------------------KDLAQ 3165
Cdd:pfam05557 206 LERLREHNKHLNENIENKLLLKEEVEDLKRKlereEKYRE--EAATLELEKEKLEQElqswvklaqdtglnlrspEDLSR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3166 EQAQKLLEDKQLM----------------QRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAK 3229
Cdd:pfam05557 284 RIEQLQQREIVLKeenssltssarqlekaRRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3230 KFKKQ------ADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKD-KARLKKEAEELQNKSKEMA 3302
Cdd:pfam05557 364 SYDKEltmsnySPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERElQALRQQESLADPSYSKEEV 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3303 DAQQKQIEH----EKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEE----EAKKSKA-----LKDEQERQKQQMEEE 3369
Cdd:pfam05557 444 DSLRRKLETleleRQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMnpaaEAYQQRKnqlekLQAEIERLKRLLKKL 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1678729579 3370 KKKLHATMHEALSKQKEAEKEMLSKQKEMQELEKKrleqeiiladeNQKLREKLQ 3424
Cdd:pfam05557 524 EDDLEQVLRLPETTSTMNFKEVLDLRKELESAELK-----------NQRLKEVFQ 567
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2261-2511 |
9.28e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2261 NLSEQQIKDK-GQLVDEALQSRTKIEEeiylIRIQLETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLhKQVIE 2339
Cdd:COG1340 7 SSSLEELEEKiEELREEIEELKEKRDE----LNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL-KEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2340 ETQKKRiaeKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAER--QVKQAEVEKERQI--------------KVAHVA 2403
Cdd:COG1340 82 ELNEKL---NELREELDELRKELAELNKAGGSIDKLRKEIERLEWrqQTEVLSPEEEKELvekikelekelekaKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2404 AQK-----SAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRL 2478
Cdd:COG1340 159 NEKlkelrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250 260 270
....*....|....*....|....*....|...
gi 1678729579 2479 RLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRA 2511
Cdd:COG1340 239 LRELRKELKKLRKKQRALKREKEKEELEEKAEE 271
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4823-4854 |
9.29e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 9.29e-05
10 20 30
....*....|....*....|....*....|..
gi 1678729579 4823 KLLSAERAVTGYRDPYSGKTISLFQAMKKGLI 4854
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2346-2538 |
9.66e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.85 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2346 IAEKELQHKSEAEKEAAKQKQKALDDLENLKKQ--AEEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKhssfvEKT 2423
Cdd:pfam05262 177 ISDKKVVEALREDNEKGVNFRRDMTDLKERESQedAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRD-----EVR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2424 SKLEESLKQEHGAVLQlqqEAAHLKKQQEDAINAREEAEKELEKwrqKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEA 2503
Cdd:pfam05262 252 QKQQEAKNLPKPADTS---SPKEDKQVAENQKREIEKAQIEIKK---NDEEALKAKDHKAFDLKQESKASEKEAEDKELE 325
|
170 180 190
....*....|....*....|....*....|....*
gi 1678729579 2504 EREAKKRAKAEESALKQKDMAEKELERQRKVADST 2538
Cdd:pfam05262 326 AQKKREPVAEDLQKTKPQVEAQPTSLNEDAIDSSN 360
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2579-2752 |
1.04e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 48.86 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2579 AAQQQRKQLEDElAKVRSEmdiLIQLKSKAEKEtmsntEKSKQLLEAEATKMrdVAEEAGKLRAIAE---EAKHQRQVAE 2655
Cdd:PTZ00491 667 AARHQAELLEQE-ARGRLE---RQKMHDKAKAE-----EQRTKLLELQAESA--AVESSGQSRAEALaeaEARLIEAEAE 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2656 EEAARQRAEAERIlkeklaaiseathlkteaeialkEKEAENERLRraaedeayQRKALEDEANQHKKEIEekIVQLKKS 2735
Cdd:PTZ00491 736 VEQAELRAKALRI-----------------------EAEAELEKLR--------KRQELELEYEQAQNELE--IAKAKEL 782
|
170 180
....*....|....*....|.
gi 1678729579 2736 SDAEMERQKAMVD----DTLK 2752
Cdd:PTZ00491 783 ADIEATKFERIVEalgrETLI 803
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2619-2805 |
1.05e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2619 SKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQrqvAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENE 2698
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLE---AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2699 RLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKssdaEMERQKAMVDDTLKQR--RVVEEEIRIlklnfEKASsgkl 2776
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEARH-----EAAV---- 173
|
170 180
....*....|....*....|....*....
gi 1678729579 2777 dlelelnKLKNIAEEtqqsklrAEEEAEK 2805
Cdd:PRK12704 174 -------LIKEIEEE-------AKEEADK 188
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2575-2696 |
1.09e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2575 NEVIAA-QQQRKQLEDELAKVRSemdiliqLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQ--R 2651
Cdd:PRK00409 519 NELIASlEELERELEQKAEEAEA-------LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiiK 591
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1678729579 2652 QVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAE 2696
Cdd:PRK00409 592 ELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3352-3432 |
1.13e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3352 SKALKDEQERQKQQMEEEKKKLHATMHEALSKQK--------EAEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKL 3423
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKeeihklrnEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
....*....
gi 1678729579 3424 QQLEEAQKE 3432
Cdd:PRK12704 110 EELEKKEKE 118
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2171-2395 |
1.13e-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: 48.22 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2171 ITETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELKLMMKE-EVNRREIAAVDAEKQK 2249
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2250 QNIQLELHeLKNLSEQQIKDKGQLV---DEALQSRTKIEEEIYLIRIQLETTVKQKSTAEsELKQLRERAAEAERLRKVA 2326
Cdd:COG4942 102 QKEELAEL-LRALYRLGRQPPLALLlspEDFLDAVRRLQYLKYLAPARREQAEELRADLA-ELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 2327 QEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLEN----LKKQAEEAERQVKQAEVEKER 2395
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAliarLEAEAAAAAERTPAAGFAALK 252
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2427-2626 |
1.13e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.41 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2427 EESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKslaQEDAEKQKEEAERE 2506
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR---QEEEERKQRLQLQA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2507 AKKRAKAEESALKQKdMAEKELERQRKVADSTAQQKLTAEQELIRLradfdnAEQQRSLLEdelyrLKNEVIAAQQQRKQ 2586
Cdd:pfam15709 417 AQERARQQQEEFRRK-LQELQRKKQQEEAERAEAEKQRQKELEMQL------AEEQKRLME-----MAEEERLEYQRQKQ 484
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678729579 2587 LEDElaKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEAE 2626
Cdd:pfam15709 485 EAEE--KARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2975-3375 |
1.19e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2975 AQAEGAALKQKQQADAEMAKHKKLAEQtLKQKFQVEQELTkvklklddTDKQKSllDDELQRlkdeVDDAVKQRGQVEEe 3054
Cdd:COG3096 288 LELRRELFGARRQLAEEQYRLVEMARE-LEELSARESDLE--------QDYQAA--SDHLNL----VQTALRQQEKIER- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3055 lfkvkvQMEELLKLKLRIEDenqrllkkdkdnsQKFLAEEAEnmKRLAEDAARLSVESQEAARLR-QIAED----DLIQQ 3129
Cdd:COG3096 352 ------YQEDLEELTERLEE-------------QEEVVEEAA--EQLAEAEARLEAAEEEVDSLKsQLADYqqalDVQQT 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3130 RALADKmlkekmQAIQEssrlKAEAEMLQRQKDLAQEQAQKLLED-----KQLMQRRLEEETeeyQKSLEAERRRQLEIV 3204
Cdd:COG3096 411 RAIQYQ------QAVQA----LEKARALCGLPDLTPENAEDYLAAfrakeQQATEEVLELEQ---KLSVADAARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3205 AEA-EKLKLQVSQlSEAQTKAEE---EAKKFKKQADK---IAARLHETEIATKEKMTVVEKLEfeRLNtsKEAGDLRDAI 3277
Cdd:COG3096 478 YELvCKIAGEVER-SQAWQTAREllrRYRSQQALAQRlqqLRAQLAELEQRLRQQQNAERLLE--EFC--QRIGQQLDAA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3278 ADLEKDKARLKKEAEELQNkskEMADAQQKQIEHEKTLLQ------------------QTFLTE-REMLLKKEKLIEEEK 3338
Cdd:COG3096 553 EELEELLAELEAQLEELEE---QAAEAVEQRSELRQQLEQlrarikelaarapawlaaQDALERlREQSGEALADSQEVT 629
|
410 420 430
....*....|....*....|....*....|....*..
gi 1678729579 3339 KKLESQFEEEaKKSKALKDEQERQKQQMEEEKKKLHA 3375
Cdd:COG3096 630 AAMQQLLERE-REATVERDELAARKQALESQIERLSQ 665
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
3002-3433 |
1.20e-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: 48.66 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3002 TLKQKFQ-VEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDdAVKQRGQVEEElfkvkvqmeELLKLKLRIEDENQRLL 3080
Cdd:pfam10174 293 QLKQELSkKESELLALQTKLETLTNQNSDCKQHIEVLKESLT-AKEQRAAILQT---------EVDALRLRLEEKESFLN 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3081 KK-----DKDNSQKFLAEEAENMKRLaedaarLSVESQEAARLRQIAEDdLIQQRALADKML---KEKMQAIQESSRlka 3152
Cdd:pfam10174 363 KKtkqlqDLTEEKSTLAGEIRDLKDM------LDVKERKINVLQKKIEN-LQEQLRDKDKQLaglKERVKSLQTDSS--- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3153 eaemlqrQKDLAQEQAQKLLEDKQLMQRRLEE--ETEEYQKSLEAERRRQLEIVAEaEKLKLQVSQLSEAQTKA---EEE 3227
Cdd:pfam10174 433 -------NTDTALTTLEEALSEKERIIERLKEqrEREDRERLEELESLKKENKDLK-EKVSALQPELTEKESSLidlKEH 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3228 AKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLR------DAIADLEKDKARLKKEAEELQNKSKEM 3301
Cdd:pfam10174 505 ASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpeinDRIRLLEQEVARYKEESGKAQAEVERL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3302 ADAQqKQIEHEKTLLQQTFLTEREMLLKkeklieeekkklesQFEEEAKKSKALKDEQerqkqqmEEEKKKLHATMHEAL 3381
Cdd:pfam10174 585 LGIL-REVENEKNDKDKKIAELESLTLR--------------QMKEQNKKVANIKHGQ-------QEMKKKGAQLLEEAR 642
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678729579 3382 SKQKEAEKEMLSKQKE--MQELEKKRLEQEII---LADENQKLREKLQQLEEAQKEQ 3433
Cdd:pfam10174 643 RREDNLADNSQQLQLEelMGALEKTRQELDATkarLSSTQQSLAEKDGHLTNLRAER 699
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2584-2907 |
1.23e-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: 48.11 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2584 RKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAK----HQRQVAEEEA- 2658
Cdd:pfam15558 16 RHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRradrREKQVIEKESr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2659 -ARQRAEAERILKEKLA-AISEATHLKTEAEIALKEKEAENERLRrAAEDEAYQRKALEDEANQHKKEIEE--KIVQLKK 2734
Cdd:pfam15558 96 wREQAEDQENQRQEKLErARQEAEQRKQCQEQRLKEKEEELQALR-EQNSLQLQERLEEACHKRQLKEREEqkKVQENNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2735 SSDAEMERQKAMVDDTLKQrrvvEEEIRilklnfekassgKLDLELELNKLKNIAEetQQSKLRAEEEAEKLRKlaleee 2814
Cdd:pfam15558 175 SELLNHQARKVLVDCQAKA----EELLR------------RLSLEQSLQRSQENYE--QLVEERHRELREKAQK------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2815 krrreaeekvkkitaaEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEAEVQiVAAQQAALKcstAEHQVQSVLAQQ 2894
Cdd:pfam15558 231 ----------------EEEQFQRAKWRAEEKEEERQEHKEALAELADRKIQQARQ-VAHKTVQDK---AQRARELNLERE 290
|
330
....*....|...
gi 1678729579 2895 KEDSIMHKKLKQE 2907
Cdd:pfam15558 291 KNHHILKLKVEKE 303
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2632-2866 |
1.24e-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: 48.22 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2632 DVAEEAGKLRAIAEEAKHQRQvAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRaaedeayQR 2711
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEK-ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2712 KALEDEANQHKKEIEEKIVQLKKSSD-------------AEMERQKAMVDDTLKQRRvveEEIRILKLNFEKASSGKLDL 2778
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRqpplalllspedfLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2779 ELELNKLKNIAEETQQSKLRAEEEAEKLRKLAleeekrrREAEEKVKKITAAEEEAARQRKIAQDELERLKKKAEEARKQ 2858
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLL-------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....*...
gi 1678729579 2859 KDEADVEA 2866
Cdd:COG4942 243 TPAAGFAA 250
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2440-2531 |
1.24e-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: 45.12 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2440 LQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEAlrlRLQAEE---EAHKKslAQEDAEKQKEEAEREAKK-RAKAEE 2515
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEA---RAEAQEiieEARKE--AEKIKEEILAEAKEEAERiLEQAKA 102
|
90
....*....|....*.
gi 1678729579 2516 SALKQKDMAEKELERQ 2531
Cdd:cd06503 103 EIEQEKEKALAELRKE 118
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2439-2511 |
1.24e-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: 45.12 E-value: 1.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678729579 2439 QLQQEAAHLKKQQEDAI-NAREEAEKELEKWRQKANEAL-RLRLQAEEEAHK-KSLAQEDAEKQKEEAEREAKKRA 2511
Cdd:cd06503 44 KAKEEAEELLAEYEEKLaEARAEAQEIIEEARKEAEKIKeEILAEAKEEAERiLEQAKAEIEQEKEKALAELRKEV 119
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2305-2521 |
1.24e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.74 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2305 AESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKkriAEKELQHKSEAE-KEAAKQKQKALDDLENLKKQAEEAE 2383
Cdd:COG1842 35 MEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEK---ARLALEKGREDLaREALERKAELEAQAEALEAQLAQLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2384 RQVKQAevekerqikvahvaaqKSAAAELQskhssfvektSKLEEsLKQEHgAVLQLQQEAAHLKKQQEDAINA--REEA 2461
Cdd:COG1842 112 EQVEKL----------------KEALRQLE----------SKLEE-LKAKK-DTLKARAKAAKAQEKVNEALSGidSDDA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2462 EKELEKWRQKANEalrlrLQAEEEAHKKSLAQEDAEKQKEEAEREAkkRAKAEESALKQK 2521
Cdd:COG1842 164 TSALERMEEKIEE-----MEARAEAAAELAAGDSLDDELAELEADS--EVEDELAALKAK 216
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4215-4248 |
1.25e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.25e-04
10 20 30
....*....|....*....|....*....|....
gi 1678729579 4215 LLEAQASTGFLVDPVRNQCLTVDEAVKSGLVGPE 4248
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2783-3007 |
1.26e-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: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2783 NKLKNIAEETQQSKLRAEEEAEKLRK--LALEEEKRRREAEEKVKKITAAEEEAARQRKIAQDELERLKKKAEEARKQKD 2860
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKqrAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2861 EADVEAEVQIVAAQQAAlkcstAEHQVQSVLAQQKEDSIMHKKLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAE 2940
Cdd:TIGR02794 137 EAEAERKAKEEAAKQAE-----EEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAA 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678729579 2941 rqkaaaeqeaaiqaKAQEDAERL------RKEAEFEAAKRAQAEGAALKQKQ------QADAEMAKHKKLAEQTLKQKF 3007
Cdd:TIGR02794 212 --------------KAEAEAAAAaaaeaeRKADEAELGDIFGLASGSNAEKQggargaAAGSEVDKYAAIIQQAIQQNL 276
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2242-2447 |
1.27e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2242 AVDAEKQKQNIQlelhelknlsEQQIKDKGQLVDEALQSRTKIEEEiyliRIQLEttvKQKSTAESELKQLRERAAEAER 2321
Cdd:PRK09510 74 AKRAEEQRKKKE----------QQQAEELQQKQAAEQERLKQLEKE----RLAAQ---EQKKQAEEAAKQAALKQKQAEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2322 LRKVAQEEAEKLhkqviEETQKKRIAEKELQHKSEAEK-EAAKQKQKALDDLenlKKQAEEAERQVKQAEVEK----ERQ 2396
Cdd:PRK09510 137 AAAKAAAAAKAK-----AEAEAKRAAAAAKKAAAEAKKkAEAEAAKKAAAEA---KKKAEAEAAAKAAAEAKKkaeaEAK 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 2397 IKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHL 2447
Cdd:PRK09510 209 KKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2347-2584 |
1.32e-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: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2347 AEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKERQikvahVAAQKSAAAELQSKHSSFVEKTSKL 2426
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-----QAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2427 EE---SLKQEHGAVLQLQQ--EAAHLkkqqEDAINareeaekelekwRQKANEALRLRLQAEEEAHKKslAQEDAEKQKE 2501
Cdd:COG3883 89 GErarALYRSGGSVSYLDVllGSESF----SDFLD------------RLSALSKIADADADLLEELKA--DKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2502 EAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQ 2581
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
...
gi 1678729579 2582 QQR 2584
Cdd:COG3883 231 AAA 233
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2410-2618 |
1.34e-04 |
|
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: 47.64 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2410 AELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEK---ELEKWRQKANEALRLRLQAEEEA 2486
Cdd:pfam09728 21 AALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKlcrELQKQNKKLKEESKKLAKEEEEK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2487 HK--------------KSLAQEDAEKQK---EEAEREAKKRAKAEESALKQKD----MAEKELERQ----RKVADSTAQQ 2541
Cdd:pfam09728 101 RKelsekfqstlkdiqDKMEEKSEKNNKlreENEELREKLKSLIEQYELRELHfeklLKTKELEVQlaeaKLQQATEEEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2542 KLTAEQELIRLRAdfdnAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAK-------VRSEMDILIQLKSKAEKETMS 2614
Cdd:pfam09728 181 KKAQEKEVAKARE----LKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKsnevfttFKKEMEKMSKKIKKLEKENLT 256
|
....
gi 1678729579 2615 NTEK 2618
Cdd:pfam09728 257 WKRK 260
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2173-2489 |
1.35e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.61 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2173 ETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELKLMMKEEVNRREIAAVDAEKQKQNI 2252
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2253 QLELHELKNLSEQQIKDKgqlvdealqSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLR-ERAAEAERLRKVAQEEAE 2331
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWK---------ELEKEEEREEDERILEYLKEKAEREEEREAEREEiEEEKEREIARLRAQQEKA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2332 KLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKERQIKVAHVAAQKSAAAE 2411
Cdd:pfam13868 197 QDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEI 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678729579 2412 LQskhssfvektskleeslKQEHGAVLQLQQEAAHLKKQQEDAINARE-EAEKELEKWRQKANEALRLRLQAEEEAHKK 2489
Cdd:pfam13868 277 EQ-----------------EEAEKRRMKRLEHRRELEKQIEEREEQRAaEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
2306-2529 |
1.37e-04 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 46.58 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2306 ESELKQLREraAEAERLRKVAQEEAEKlhkqvIEETQKKRIAEKELQHK----SEAEKEAAKQKQKALDDLENLKKQAEE 2381
Cdd:pfam15665 13 EAEIQALKE--AHEEEIQQILAETREK-----ILQYKSKIGEELDLKRRiqtlEESLEQHERMKRQALTEFEQYKRRVEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2382 aerqvKQAEVEKERQIKVAhvaaqkSAAAELQSKHSSFVEKTSKLEEslkqehgavLQLQQEAAHLKKQQEDAINAREEA 2461
Cdd:pfam15665 86 -----RELKAEAEHRQRVV------ELSREVEEAKRAFEEKLESFEQ---------LQAQFEQEKRKALEELRAKHRQEI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 2462 EKELEKWRQKANEAL--RLRLQAEEEAHKKSLAQE----DAEKQKEEAEREAKKrakaeesaLKQKDMAEKELE 2529
Cdd:pfam15665 146 QELLTTQRAQSASSLaeQEKLEELHKAELESLRKEvedlRKEKKKLAEEYEQKL--------SKAQAFYERELE 211
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3077-3230 |
1.38e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3077 QRLLKKDKDNSQKFLAE---EAENMKRLAEDAARlsvesQEAARLRQIAEDDLIQQRALADKMLKekmQAIQESSRLKAE 3153
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEakkEAEAIKKEALLEAK-----EEIHKLRNEFEKELRERRNELQKLEK---RLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3154 AEMLQRQKDLAQEQAQKLLEdkqlMQRRLEEETEEYQKsLEAERRRQLEIVA-----EA---------EKLKLQVSQL-S 3218
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQ----KQQELEKKEEELEE-LIEEQLQELERISgltaeEAkeillekveEEARHEAAVLiK 176
|
170
....*....|..
gi 1678729579 3219 EAQTKAEEEAKK 3230
Cdd:PRK12704 177 EIEEEAKEEADK 188
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2178-2464 |
1.42e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.95 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2178 LEDEEKAakkLKAEEQKKMAEMQAELDKQK-QLAAAHAKAIAKAEKEAQELKLMMKEEVNRREIAAVDAEKQKQNIQLel 2256
Cdd:COG2268 179 LEDENNY---LDALGRRKIAEIIRDARIAEaEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEE-- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2257 hELKNLSEQQIKDKGQLVDEALQSRtKIEEEIYLIRIQLETTVKQKSTAESELKQLRER--AAEAERLRKVAQEEAEklh 2334
Cdd:COG2268 254 -RREAETARAEAEAAYEIAEANAER-EVQRQLEIAEREREIELQEKEAEREEAELEADVrkPAEAEKQAAEAEAEAE--- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2335 KQVIEEtqkkrIAEKELQHKsEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKErqIKVAHVAAQKSAAAelqs 2414
Cdd:COG2268 329 AEAIRA-----KGLAEAEGK-RALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDK--ITIIDGGNGGNGAG---- 396
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2415 khSSFVEKTSKLEESLKQEHGAVLqlqqeAAHLKKQQEDAINAREEAEKE 2464
Cdd:COG2268 397 --SAVAEALAPLLESLLEETGLDL-----PGLLKGLTGAGAAAPAGEPAE 439
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3268-3442 |
1.44e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3268 KEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEE 3347
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3348 EAKKSKALKdEQERQKQQMEEEKKKLHATMHEAL-SKQKEAEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQL 3426
Cdd:COG4717 151 LEERLEELR-ELEEELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|....*.
gi 1678729579 3427 EEAQKEQHTVPDKELI 3442
Cdd:COG4717 230 EQLENELEAAALEERL 245
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
863-974 |
1.47e-04 |
|
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: 44.59 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 863 ERDRVQKKTFTKWVNKHLIkraesQHHVTDLYEDLRDGHNLISLLEV---------LSGDTLPREKGRMRfhKLQNVQIA 933
Cdd:cd21329 2 EGESSEERTFRNWMNSLGV-----NPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1678729579 934 LDFLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTVILHFQIS 974
Cdd:cd21329 75 VELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
3080-3429 |
1.62e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3080 LKKDKDNSQKFLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDL-IQQRALAdkmLKEKMQAIQE-----SSRLKAE 3153
Cdd:COG3096 290 LRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLnLVQTALR---QQEKIERYQEdleelTERLEEQ 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3154 AEMLqrqkdlaqEQAQKLLEDKQLMQRRLEEETEE-------YQKSLEAERRRQ------LEIVAEAEKLkLQVSQLSEA 3220
Cdd:COG3096 367 EEVV--------EEAAEQLAEAEARLEAAEEEVDSlksqladYQQALDVQQTRAiqyqqaVQALEKARAL-CGLPDLTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3221 QtkAEEEAKKFKKQADKIAARLHETEiatkEKMTV--------------VEKL--EFERLNTSKEAgdlRDAIADLEKDK 3284
Cdd:COG3096 438 N--AEDYLAAFRAKEQQATEEVLELE----QKLSVadaarrqfekayelVCKIagEVERSQAWQTA---RELLRRYRSQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3285 AR------LKKEAEELQNKSKEMADAQQKQIEHEKTLLQQtfLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDE 3358
Cdd:COG3096 509 ALaqrlqqLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQ--LDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 3359 QERQKQQMEEEKKKLHA--TMHEALSKQKEAEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQLEEA 3429
Cdd:COG3096 587 LEQLRARIKELAARAPAwlAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQ 659
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2438-2636 |
1.63e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 47.94 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2438 LQLQQEAAHLK--KQQEDAINAREEAEKELEKWRQKAnealrlrlQAEEEAHKKSL---AQEDAEKQKEEAEREakkrAK 2512
Cdd:PRK00106 26 MKSAKEAAELTllNAEQEAVNLRGKAERDAEHIKKTA--------KRESKALKKELlleAKEEARKYREEIEQE----FK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2513 AEESALKQKD--MAEKELERQRKVADSTAQQKL--TAEQELIRLRADFDNAEQQRSLLEDElYRLKNEVIAAQQQRKQLE 2588
Cdd:PRK00106 94 SERQELKQIEsrLTERATSLDRKDENLSSKEKTleSKEQSLTDKSKHIDEREEQVEKLEEQ-KKAELERVAALSQAEARE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2589 DELAKVRSEM--DILIQLKsKAEKETMSNTEKSKQLLEAEAtkMRDVAEE 2636
Cdd:PRK00106 173 IILAETENKLthEIATRIR-EAEREVKDRSDKMAKDLLAQA--MQRLAGE 219
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
856-967 |
1.69e-04 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 44.57 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 856 WPHFIEDERDrvqKKTFTKWVNKHLikrAESQHH--VTDLYEDLRDGHNLISLLEVLSGDTLPREKG--RMRFHKLQNVQ 931
Cdd:cd21285 2 KSWEAENGFD---KQIYTDWANHYL---AKSGHKrlIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENID 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 1678729579 932 IALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTV 967
Cdd:cd21285 76 ACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
2104-2396 |
1.70e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.54 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2104 KYAKAYINSIKDYELQLVAYNaqadpLASPLKKTKLDSASDNIIQEYV---TLRTRYSELmtltsQYIKFITETQRRLED 2180
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREK-----KLRETEEVEFSLKAEVLIQKFGrslKAKKRFSLL-----KKETIYLQSAQRVEL 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2181 EEKAAKKLK--AEEQKKMAEMQAELDKQkqlaaahakaiAKAEKEAQELKLMMKEEVNRREIAAVdaEKQKQNIQLELHE 2258
Cdd:COG5022 880 AERQLQELKidVKSISSLKLVNLELESE-----------IIELKKSLSSDLIENLEFKTELIARL--KKLLNNIDLEEGP 946
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2259 LKNLSEQQIKDKGQLVDEALQSRTKIEEEIYlirIQLETTVKQKSTAESELKQLRERAAEAERLRKVAQEEaEKLHKQVI 2338
Cdd:COG5022 947 SIEYVKLPELNKLHEVESKLKETSEEYEDLL---KKSTILVREGNKANSELKNFKKELAELSKQYGALQES-TKQLKELP 1022
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1678729579 2339 EETQKKRIAEKELQHKSeaekeAAKQKQKALDDLENLK-KQAEEAERQVKQAEVEKERQ 2396
Cdd:COG5022 1023 VEVAELQSASKIISSES-----TELSILKPLQKLKGLLlLENNQLQARYKALKLRRENS 1076
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2117-2595 |
1.70e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 48.04 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2117 ELQLVAYNAQADPLASPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKKLKAEEQKKM 2196
Cdd:COG4995 1 LLALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2197 AEMQAELDKQKQLAAAHAKAIAKAEKEAQELKLMMKEEVNRREIAAVDAEKQKQNIQLELHELKNLSEQQIKDKGQLVDE 2276
Cdd:COG4995 81 ALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2277 ALQSRTkiEEEIYLIRIQLETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSE 2356
Cdd:COG4995 161 AAAALL--ALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2357 AEKEAAKQKQKALDDLENLKKQAEEAERQvkQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGA 2436
Cdd:COG4995 239 ALLALAAAAAALAAAAAALLALAAALLLL--AALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2437 VLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEkqkeeAEREAKKRAKAEES 2516
Cdd:COG4995 317 LLLLAALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLAL-----LLEALLLLLLALLA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2517 ALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELY---RLKNEVIAaqqqrkQLEDELAK 2593
Cdd:COG4995 392 ALLLLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLYafvQLYQLLIA------PIEAELPG 465
|
..
gi 1678729579 2594 VR 2595
Cdd:COG4995 466 IK 467
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2300-2414 |
1.78e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 44.55 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2300 KQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKkriAEKELQHKSEAEKEAAKQK---QKALDDLENLK 2376
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQN---YERELVLHAEDIKALQALReelNELKAEIAELK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1678729579 2377 KQAEEAERQVKQAEV--EKERQIKVAHVAAQKSAAAELQS 2414
Cdd:pfam07926 78 AEAESAKAELEESEEswEEQKKELEKELSELEKRIEDLNE 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3276-3436 |
1.81e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3276 AIADLEKDKARLKKEAEELQNKSKEmADAQQKQIEHEKTLLQQTFLteremllkkeklieeekkklesqfEEEAKKSKAL 3355
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEE-LEAELAELEAELEELRLELE------------------------ELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3356 KDEQERQKQQMEEEKKKLHATmhealSKQKEAEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQLEEAQKEQHT 3435
Cdd:COG1196 288 AEEYELLAELARLEQDIARLE-----ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
.
gi 1678729579 3436 V 3436
Cdd:COG1196 363 A 363
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2069-2587 |
1.82e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.21 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2069 AVSITDSKTLKEQLSqekKLLEEIENNKDNVDECQKYAKAYINSikdyELQLVAYNAQADPLASPLKKTKLDSASDNIIQ 2148
Cdd:pfam07111 193 AEAQKEAELLRKQLS---KTQEELEAQVTLVESLRKYVGEQVPP----EVHSQTWELERQELLDTMQHLQEDRADLQATV 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2149 EYVTLRTR-YSELMTLTSQYIKFITETQRRLEDE-EKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQE 2226
Cdd:pfam07111 266 ELLQVRVQsLTHMLALQEEELTRKIQPSDSLEPEfPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2227 lklmmKEEVNRREIAAVDAEKQKQNIQLELHELKNLSEQQIKDKGQLVDEALQSRT-KIEEEIYLI-------RIQLETT 2298
Cdd:pfam07111 346 -----QVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTaSAEEQLKFVvnamsstQIWLETT 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2299 VKQKSTAESELKQLRERAAEAER-LRKVAQEEAEKLH-KQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLK 2376
Cdd:pfam07111 421 MTRVEQAVARIPSLSNRLSYAVRkVHTIKGLMARKVAlAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLS 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2377 KQ--AEEAERQVKQAEVEKERQIKVAHVAAQksaaaELQSKHSSFVektskleeSLKQEHGAVLQLQQEAAhlkkqqEDA 2454
Cdd:pfam07111 501 AHliQQEVGRAREQGEAERQQLSEVAQQLEQ-----ELQRAQESLA--------SVGQQLEVARQGQQEST------EEA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2455 INAREEAEKELEKWRQkaneALRLRLQAEEEAHKKSLAqeDAEKQKEEAEREakkRAKAEESALKQKDMAEKELERQrkv 2534
Cdd:pfam07111 562 ASLRQELTQQQEIYGQ----ALQEKVAEVETRLREQLS--DTKRRLNEARRE---QAKAVVSLRQIQHRATQEKERN--- 629
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 2535 adstaqqkltaeQELIRLRADFDNAEQQR-SLLEDELYRLKNEVIAAQQQRKQL 2587
Cdd:pfam07111 630 ------------QELRRLQDEARKEEGQRlARRVQELERDKNLMLATLQQEGLL 671
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
3070-3428 |
1.87e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3070 LRIEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDAARLS-------VESQEAARLRQIAEDDLIQQ----RALADkmLK 3138
Cdd:PRK04863 281 RRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNeaesdleQDYQAASDHLNLVQTALRQQekieRYQAD--LE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3139 EKMQAIQESSRLKAEA----EMLQRQKDLAQEQAQKLleDKQL--MQRRLEE-ETE--EYQKSLEA-ERRRQLEIVAEae 3208
Cdd:PRK04863 359 ELEERLEEQNEVVEEAdeqqEENEARAEAAEEEVDEL--KSQLadYQQALDVqQTRaiQYQQAVQAlERAKQLCGLPD-- 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3209 klkLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEiATKEKMTVVEKL------EFERLNTSKEAgdlRDAIADLEK 3282
Cdd:PRK04863 435 ---LTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ-AAHSQFEQAYQLvrkiagEVSRSEAWDVA---RELLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3283 DKAR------LKKEAEELQNKSKEMADAQQKQIEHEKTLLQQtfLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALK 3356
Cdd:PRK04863 508 QRHLaeqlqqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKN--LDDEDELEQLQEELEARLESLSESVSEARERRMALR 585
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 3357 DEQERQKQQMEEEKKKLHA--TMHEALSKQKEAEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQLEE 3428
Cdd:PRK04863 586 QQLEQLQARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDE 659
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2276-2374 |
1.89e-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: 44.35 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2276 EALQSRT-KIEEEIYLIRIQLETTVKQKSTAESELKQLREraaEAERLRKVAQEEAEKLHKQVIEETQKKriAEKELQhk 2354
Cdd:cd06503 26 KALDEREeKIAESLEEAEKAKEEAEELLAEYEEKLAEARA---EAQEIIEEARKEAEKIKEEILAEAKEE--AERILE-- 98
|
90 100
....*....|....*....|
gi 1678729579 2355 sEAEKEAAKQKQKALDDLEN 2374
Cdd:cd06503 99 -QAKAEIEQEKEKALAELRK 117
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2300-2532 |
2.14e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.38 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2300 KQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKkrIAEKELQHKSEaEKEAAKQ-----KQKALDDLEn 2374
Cdd:PRK11637 68 QQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNAS--IAKLEQQQAAQ-ERLLAAQldaafRQGEHTGLQ- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2375 LKKQAEEAER------------QVKQAEVEKERQIKVAhVAAQKsaaAELQSKHSsfvektskleeslkqEHGAVLQLQQ 2442
Cdd:PRK11637 144 LILSGEESQRgerilayfgylnQARQETIAELKQTREE-LAAQK---AELEEKQS---------------QQKTLLYEQQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2443 EAahlKKQQEDAINAREEAEKELEKWRQKANEALrLRLQAEEEAHKKSLAQEDAEKqKEEAEREAKK--RAKAEESALKQ 2520
Cdd:PRK11637 205 AQ---QQKLEQARNERKKTLTGLESSLQKDQQQL-SELRANESRLRDSIARAEREA-KARAEREAREaaRVRDKQKQAKR 279
|
250
....*....|..
gi 1678729579 2521 KDMAEKELERQR 2532
Cdd:PRK11637 280 KGSTYKPTESER 291
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2259-2467 |
2.21e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2259 LKNLSEQQIKDKGQLVDEALQSrTKIEEEIYLIRIQLEttvkqkstAESELKQLREraaEAERLRKVAQEEAEKLHKQVI 2338
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEE-AKKEAEAIKKEALLE--------AKEEIHKLRN---EFEKELRERRNELQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2339 eetQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKERqikvahvaaqksaAAELQSKhss 2418
Cdd:PRK12704 93 ---QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER-------------ISGLTAE--- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1678729579 2419 fvEKTSKLEESLKQEhgavlqLQQEAAHLKKQQEDaiNAREEAEKELEK 2467
Cdd:PRK12704 154 --EAKEILLEKVEEE------ARHEAAVLIKEIEE--EAKEEADKKAKE 192
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2281-2804 |
2.26e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2281 RTKIEEEIYLIRIQLETTVKQKSTaeseLKQLRERAAEAERLR---KVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEA 2357
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDV----IDMLRAEISNIDYLEeklKSSNLELENIKKQIADDEKSHSITLKEIERLSIE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2358 EKEAAKQKQKALDDLENLKKQAEEAER-QVKQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGA 2436
Cdd:PRK01156 227 YNNAMDDYNNLKSALNELSSLEDMKNRyESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKND 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2437 VLQLQQEAAHLKKQqedaINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEES 2516
Cdd:PRK01156 307 IENKKQILSNIDAE----INKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEY 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2517 ALKQKDMAEkELERQRKVADSTAQQkLTAEQELIRlradfdnaeqqRSLLEdelyrLKNEVIAAQQQRKQLEDELAKVRS 2596
Cdd:PRK01156 383 SKNIERMSA-FISEILKIQEIDPDA-IKKELNEIN-----------VKLQD-----ISSKVSSLNQRIRALRENLDELSR 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2597 EMDILIQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKL----RAIAEEAKHQRQVAEEEAARQ----------- 2661
Cdd:PRK01156 445 NMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIeievKDIDEKIVDLKKRKEYLESEEinksineynki 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2662 ---RAEAERIlKEKLAAISEAtHLKTEAEIA-LKEKEAENERLRRAAEDEAY-QRKALEDEANQHKKeiEEKIVQLKKSS 2736
Cdd:PRK01156 525 esaRADLEDI-KIKINELKDK-HDKYEEIKNrYKSLKLEDLDSKRTSWLNALaVISLIDIETNRSRS--NEIKKQLNDLE 600
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 2737 DAEMERQKAMVDD---TLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAE 2804
Cdd:PRK01156 601 SRLQEIEIGFPDDksyIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE 671
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2442-2709 |
2.27e-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: 47.15 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2442 QEAAHLKKQQEDAINAREEAEKELEKWRQKANEAlrlrlQAEEEAHKKSLAQedaekqkeeaereakkRAKAEESAlKQK 2521
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQ-----RAAEQARQKELEQ----------------RAAAEKAA-KQA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2522 DMAEKELERQRKVADSTAQQkltaeqelirlradfDNAEQQRslledelyrlkneviAAQQQRKQLEDELAKVRSEMDIL 2601
Cdd:TIGR02794 108 EQAAKQAEEKQKQAEEAKAK---------------QAAEAKA---------------KAEAEAERKAKEEAAKQAEEEAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2602 IQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQvAEEEAARQRAEAERILKEKLAAISEATH 2681
Cdd:TIGR02794 158 AKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAE-AAAKAEAEAAAAAAAEAERKADEAELGD 236
|
250 260
....*....|....*....|....*...
gi 1678729579 2682 LKTEAEIALKEKEAENERLRRAAEDEAY 2709
Cdd:TIGR02794 237 IFGLASGSNAEKQGGARGAAAGSEVDKY 264
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2375-2613 |
2.30e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2375 LKKQAEEAERQVKQAEVEK---ERQIKV--AHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEhgaVLQLQQEAAHLKK 2449
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIdhiQQQIKTynKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAE---IEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2450 QQEDAINAreeaekeLEKWRQKanealRLRLQAEEEAHKK--SLAQEDAE----KQ--KEEAEREAKKRAKAEESALKQK 2521
Cdd:PHA02562 249 DIEDPSAA-------LNKLNTA-----AAKIKSKIEQFQKviKMYEKGGVcptcTQqiSEGPDRITKIKDKLKELQHSLE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2522 DMAEKELERQRKVADSTAQQKltaeqELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDIL 2601
Cdd:PHA02562 317 KLDTAIDELEEIMDEFNEQSK-----KLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
250
....*....|..
gi 1678729579 2602 IQLKSKAEKETM 2613
Cdd:PHA02562 392 VKTKSELVKEKY 403
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
874-966 |
2.47e-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: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 874 KWVNKHLIKRAESQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRM---RFHKLQNVQIALDFLrhRQVKLVN-IRN 949
Cdd:cd21218 17 RWVNYHLKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAA--EKLGCKYfLTP 94
|
90
....*....|....*..
gi 1678729579 950 DDIADGNPKLTLGLIWT 966
Cdd:cd21218 95 EDIVSGNPRLNLAFVAT 111
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2986-3263 |
2.79e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 47.02 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2986 QQADAEMAKHKKlaeQTLKQKFQVEQELTKVKLKLDDTDKQKsllDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEEL 3065
Cdd:pfam03528 7 QQRVAELEKENA---EFYRLKQQLEAEFNQKRAKFKELYLAK---EEDLKRQNAVLQEAQVELDALQNQLALARAEMENI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3066 LKLKLRIEDENQRLLKKDKDNSQkflaEEAENMKRLAEDAARlSVESQEAARLRQiAEDDLIQQRALADKMLKEKMQAIQ 3145
Cdd:pfam03528 81 KAVATVSENTKQEAIDEVKSQWQ----EEVASLQAIMKETVR-EYEVQFHRRLEQ-ERAQWNQYRESAEREIADLRRRLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3146 ESSrlkaEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEE------ETEEYQKSLEAERRRQLEIVAEAEK-----LKLQV 3214
Cdd:pfam03528 155 EGQ----EEENLEDEMKKAQEDAEKLRSVVMPMEKEIAAlkakltEAEDKIKELEASKMKELNHYLEAEKscrtdLEMYV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1678729579 3215 SQLSEAQTKAEEEAKKFKKQadkiaarLHEteiatkekmtVVEKLEFER 3263
Cdd:pfam03528 231 AVLNTQKSVLQEDAEKLRKE-------LHE----------VCHLLEQER 262
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
2381-2631 |
2.83e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2381 EAERQvkqaEVEKERQIKVAHvaaQKSaaaELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREE 2460
Cdd:pfam17045 5 EAELQ----ELMKQIDIMVAH---KKS---EWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2461 AEKELEKWRQKANEALRLRLQAEEEAHKKSL--AQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADST 2538
Cdd:pfam17045 75 LVAKYEQQLQKLQEELSKLKRSYEKLQRKQLkeAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2539 AQQKLTAEQ-ELIRLRADFDNAEQQRSLLED---ELYRLKNEVIAAQQQRKQLEDELAKVRSEMDIL------IQLKSKA 2608
Cdd:pfam17045 155 AQRKALAEQsSLIQSAAYQVQLEGRKQCLEAsqsEIQRLRSKLERAQDSLCAQELELERLRMRVSELgdsnrkLLEEQQR 234
|
250 260
....*....|....*....|...
gi 1678729579 2609 EKETMSNTEKSKQLLEAEATKMR 2631
Cdd:pfam17045 235 LLEELRMSQRQLQVLQNELMELK 257
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1795-2348 |
3.04e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1795 LLRSMEKGMVVRLKGQQDETLCKNYISEIKDLRVRIEDCEAGTVARIRKPMEKEPLKECVQKATDQKKVQVKLEGLKKDL 1874
Cdd:pfam02463 481 KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEV 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1875 NKVSVKTQEVLASPQKSASAPVLRSELDLTVQKMDHAYMLSSVYLEKLKTVEMVIRNTQGAEGVLKQYEDCLREVHTVPG 1954
Cdd:pfam02463 561 EERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKES 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1955 DVKEVETYRTKLKKMRGEAE-------GEQPVFDSLEEELKKATVVSDKMSRVHSERDVELDHYRQHLSGLQDRWKAVFA 2027
Cdd:pfam02463 641 AKAKESGLRKGVSLEEGLAEksevkasLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2028 QMDIRQRELEQLGRQlgyyhESYDWLIHWITDAKERQEKIQAVSITDSKTLKEQLSQEKKLLEEIENNKDNVDECQKYAK 2107
Cdd:pfam02463 721 ELLADRVQEAQDKIN-----EELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEK 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2108 ayinsIKDYELQLVAYNAQADPLASPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYiKFITETQRRLEDEEKAAKK 2187
Cdd:pfam02463 796 -----LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEK-LAEEELERLEEEITKEELL 869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2188 LKAEEQKKMAEMQAELDKQKQLaaahakaiakAEKEAQELKLMMKEEvnRREIAAVDAEKQKQN-IQLELHELKNLSEQQ 2266
Cdd:pfam02463 870 QELLLKEEELEEQKLKDELESK----------EEKEKEEKKELEEES--QKLNLLEEKENEIEErIKEEAEILLKYEEEP 937
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2267 IKDKGQLVDEALQSRTKIEEEIYLI-----RIQLETTVKQKSTAESELKQLRERAAEAERLRKvaQEEAEKLHKQVIEET 2341
Cdd:pfam02463 938 EELLLEEADEKEKEENNKEEEEERNkrlllAKEELGKVNLMAIEEFEEKEERYNKDELEKERL--EEEKKKLIRAIIEET 1015
|
....*..
gi 1678729579 2342 QKKRIAE 2348
Cdd:pfam02463 1016 CQRLKEF 1022
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2603-2748 |
3.10e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.79 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2603 QLKSKAEKETmSNTEKSKQLLEAEATKMRDVAEEAgklraiAEEAKHQRQVAEEEA--------ARQRAEAERILKEKLA 2674
Cdd:COG2268 196 EIIRDARIAE-AEAERETEIAIAQANREAEEAELE------QEREIETARIAEAEAelakkkaeERREAETARAEAEAAY 268
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 2675 AISEAthlKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMVD 2748
Cdd:COG2268 269 EIAEA---NAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAE 339
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2480-2724 |
3.16e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2480 LQAEEEAHKKSLAQEDAEKQKeeaeREAKKRAKAEESALKQ-KDMAEKELERQRKVADSTAQQKLTAeqelirlradfdN 2558
Cdd:NF012221 1540 SSQQADAVSKHAKQDDAAQNA----LADKERAEADRQRLEQeKQQQLAAISGSQSQLESTDQNALET------------N 1603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2559 AEQQRSLLEDELYRLKNEVIAAQQQRKQLEDE-------------------LAKVRSEMDiliQLKSKAEKETmsntEKS 2619
Cdd:NF012221 1604 GQAQRDAILEESRAVTKELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLD---DAKKISGKQL----ADA 1676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2620 KQLLEAEATKMRDvaeEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENER 2699
Cdd:NF012221 1677 KQRHVDNQQKVKD---AVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQ 1753
|
250 260
....*....|....*....|....*
gi 1678729579 2700 LRRAAEDEAYQRKALEDEANQHKKE 2724
Cdd:NF012221 1754 DASAAENKANQAQADAKGAKQDESD 1778
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
2490-2743 |
3.23e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.45 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2490 SLAQEDAEKQKEEAEREAKKRAkaEESALKQkdMAEKELERQRKVADSTAQQKLTAEQELIRLRADfdnAEQQRSLLEDE 2569
Cdd:pfam00038 22 FLEQQNKLLETKISELRQKKGA--EPSRLYS--LYEKEIEDLRRQLDTLTVERARLQLELDNLRLA---AEDFRQKYEDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2570 LyRLKNEVIAA-QQQRKQLEDE-LAKVRSEMDI------LIQLKSKAE---KETMSNTEKSKQLLEAEATKMRDVAeeag 2638
Cdd:pfam00038 95 L-NLRTSAENDlVGLRKDLDEAtLARVDLEAKIeslkeeLAFLKKNHEeevRELQAQVSDTQVNVEMDAARKLDLT---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2639 klRAIAEeakhQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERL--RRAAEDEAY--QRKAL 2714
Cdd:pfam00038 170 --SALAE----IRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTiqSLEIELQSLkkQKASL 243
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1678729579 2715 ED-----------EANQHKKEIEEKIVQLKKSSDaEMERQ 2743
Cdd:pfam00038 244 ERqlaeteeryelQLADYQELISELEAELQETRQ-EMARQ 282
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3921-3957 |
3.30e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.30e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1678729579 3921 KLLSAERAVTGYKDPYTGKTVSLFQAMKKDLIPKEQG 3957
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2336-2732 |
3.65e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2336 QVIEETQKKRIAEKELQHKS-EAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKERqikvahvaaqksaaaelqs 2414
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTgILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQ------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2415 khssfvektskLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQE 2494
Cdd:COG4372 64 -----------LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2495 DAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLK 2574
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2575 NEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVA 2654
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678729579 2655 EEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQL 2732
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2615-2966 |
4.03e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.45 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2615 NTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEA-EIALKEK 2693
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEyEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2694 EAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKamvddtlkqrrvvEEEIRILKLNFEKAss 2773
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEER-------------EEDERILEYLKEKA-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2774 GKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKlaleeekrrreaeekvkkitaAEEEAARQRKI--AQDELERLKKK 2851
Cdd:pfam13868 166 EREEEREAEREEIEEEKEREIARLRAQQEKAQDEK---------------------AERDELRAKLYqeEQERKERQKER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2852 AEEARKQKDEADV----EAEVQIVAAQQAALKcSTAEHQVQSVLAQQKEDSIMHKKLKQEyekakklakeaeaAKEKAER 2927
Cdd:pfam13868 225 EEAEKKARQRQELqqarEEQIELKERRLAEEA-EREEEEFERMLRKQAEDEEIEQEEAEK-------------RRMKRLE 290
|
330 340 350
....*....|....*....|....*....|....*....
gi 1678729579 2928 EAALLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKE 2966
Cdd:pfam13868 291 HRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRE 329
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
3109-3325 |
4.03e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.14 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3109 SVESQEAARLRQIAEDDLIQQRALADkmlKEKMQAiqESSRLKAEaemlqRQKDLAQ-EQAQKLLEDKQlmQRRLEEETE 3187
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALAD---KERAEA--DRQRLEQE-----KQQQLAAiSGSQSQLESTD--QNALETNGQ 1605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3188 EYQKSLEAERRrqlEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQ-ADKIAARLHETEIATKEkmTVVEKLEFERLNT 3266
Cdd:NF012221 1606 AQRDAILEESR---AVTKELTTLAQGLDALDSQATYAGESGDQWRNPfAGGLLDRVQEQLDDAKK--ISGKQLADAKQRH 1680
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678729579 3267 SKEAGDLRDAIADLEKDKAR---LKKEAEelQNKSKEMADAQQKQIEhekTLLQQTFLTERE 3325
Cdd:NF012221 1681 VDNQQKVKDAVAKSEAGVAQgeqNQANAE--QDIDDAKADAEKRKDD---ALAKQNEAQQAE 1737
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2997-3319 |
4.09e-04 |
|
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: 46.10 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2997 KLAEQTLKQKFQVEQELTKVKL---KLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKlrie 3073
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAAlckKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLC---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3074 DENQRLLKKDKDNSQKFLAEEAENmkrlaedaaRLSVESQEAARLRQIA---EDDLIQQRALAD--KMLKEKMQAIQESS 3148
Cdd:pfam09728 77 RELQKQNKKLKEESKKLAKEEEEK---------RKELSEKFQSTLKDIQdkmEEKSEKNNKLREenEELREKLKSLIEQY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3149 RLkaeaemlqRQKDLAQEQAQKLLEdKQLMQRRLEEETEEYQKSL-EAErrrqleiVAEAEKLKLQVSQLSEAQTKAEEE 3227
Cdd:pfam09728 148 EL--------RELHFEKLLKTKELE-VQLAEAKLQQATEEEEKKAqEKE-------VAKARELKAQVQTLSETEKELREQ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3228 AKKFKKQADKIAARLHETEiatkEKMTVVeKLEFERLNtskeagdlrDAIADLEKDKARLKKEAEELQNKSKEMADAQQK 3307
Cdd:pfam09728 212 LNLYVEKFEEFQDTLNKSN----EVFTTF-KKEMEKMS---------KKIKKLEKENLTWKRKWEKSNKALLEMAEERQK 277
|
330
....*....|..
gi 1678729579 3308 QIEHEKTLLQQT 3319
Cdd:pfam09728 278 LKEELEKLQKKL 289
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
2984-3404 |
4.24e-04 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 46.78 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2984 QKQQADAEMAKHKKLAEQTLKQKF------QVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFK 3057
Cdd:pfam09730 8 KKVAADGESREESLLQESASKEAYyaqrilELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDEIKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3058 VKVQMEELLKLKLRIEDENQRLLKKD---KDNSQKFLAEEAEnMKRLAEDAARLSVESQEAARLRQIAEddliqqralad 3134
Cdd:pfam09730 88 YKVREARLLQDYSELEEENISLQKQVsvlKQNQVEFEGLKHE-ITRKEEETELLNSQLEEAIRLREIAE----------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3135 KMLKEKMQAIQESSRLKAeaemlqrqkDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEA------- 3207
Cdd:pfam09730 156 RQLDEALETLKTEREQKN---------SLRKELSHYMTLNDFDYVSHLSISLDGLKFSEDEGAGTEPNNDGEAmdggeng 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3208 -EKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEI---------ATKEKMTVVEKLEferlNTSKEAGDLRDAI 3277
Cdd:pfam09730 227 gGGLKNSGLDNRTSTPRKSEVFPPAPSLVSDLLSELNISEIqklkqqliqVEREKVSLLSTLQ----ESQKQLEQAKGAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3278 ADLEKDKARLKKEAEELQN--KSKEmadaQQKQIEHEKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKAL 3355
Cdd:pfam09730 303 SEQQEKVNRLTENLEAMRGlqASKE----RQDALDSEKDRDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREELKAL 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1678729579 3356 KDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMLSKQKEMQELEKK 3404
Cdd:pfam09730 379 KARYNTLEERYKEEKTRWEAEAQDLAEKIRQLEKASHQDQERIAHLEKE 427
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
3110-3433 |
4.70e-04 |
|
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: 46.86 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3110 VESQEAARLRQIAEDDLIQQRAladkmlkekmQAIQESSRLKAEAEMLQRQKDLAQEQAQKLLE--DKQLMQRR--LEEE 3185
Cdd:pfam15818 10 LEALEELRMRREAETQYEEQIG----------KIIVETQELKWQKETLQNQKETLAKQHKEAMAvfKKQLQMKMcaLEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3186 TEEYQKSLEAERRrqlEIVAEAEKLK-LQVSQLSeAQTKAEEEAKKFkkQADKIAARLHETEIATKEK--MTVVEKLEFE 3262
Cdd:pfam15818 80 KGKYQLATEIKEK---EIEGLKETLKaLQVSKYS-LQKKVSEMEQKL--QLHLLAKEDHHKQLNEIEKyyATITGQFGLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3263 RLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMADAQQKQIEHEKTllqqtflteremllkkeklieeekkkLE 3342
Cdd:pfam15818 154 KENHGKLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKVT--------------------------CQ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3343 SQFEEE----AKKSKALKDEQERQKQQMEEEKKklhatMHEALSKQKEAEKEMLSKQKEMQELEKKRLEQEIILADENQK 3418
Cdd:pfam15818 208 YKMGEEninlTIKEQKFQELQERLNMELELNKK-----INEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKA 282
|
330
....*....|....*...
gi 1678729579 3419 LREKLQQLE---EAQKEQ 3433
Cdd:pfam15818 283 LKENNQTLErdnELQREK 300
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2962-3362 |
5.04e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.44 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2962 RLRKEAEFEAAKRAQAEGAALKQKQQADAEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEV 3041
Cdd:COG5278 128 ALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3042 DDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDAARLSVESQEAARLRQI 3121
Cdd:COG5278 208 LLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3122 AEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQL 3201
Cdd:COG5278 288 ALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3202 EIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLE 3281
Cdd:COG5278 368 AAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASS 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3282 KDKARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQER 3361
Cdd:COG5278 448 ELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALAS 527
|
.
gi 1678729579 3362 Q 3362
Cdd:COG5278 528 A 528
|
|
| PRK09173 |
PRK09173 |
F0F1 ATP synthase subunit B; Validated |
2310-2415 |
5.20e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 169691 [Multi-domain] Cd Length: 159 Bit Score: 43.96 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2310 KQLRERAAEAERLRKVAQeeaeklhkQVIEETQKKRI-AEKELQH-----KSEAEKEAAKQKQKALDDLENLKKQAEEae 2383
Cdd:PRK09173 36 DRIKNELAEARRLREEAQ--------QLLAEYQRKRKeAEKEAADivaaaEREAEALTAEAKRKTEEYVARRNKLAEQ-- 105
|
90 100 110
....*....|....*....|....*....|....*..
gi 1678729579 2384 rQVKQAEVEKERQIKVAHV-----AAQKSAAAELQSK 2415
Cdd:PRK09173 106 -KIAQAETDAINAVRSSAVdlaiaAAEKLLAEKVDAK 141
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2309-2450 |
5.26e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.24 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2309 LKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEK------------ELQHKSEAEKEAAKQKQKALDDLENLK 2376
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERnqqrqearrereELQREEERLVQKEEQLDARAEKLDNLE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678729579 2377 KQAEEAERQVKQAEVE-KERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQ 2450
Cdd:PRK12705 105 NQLEEREKALSARELElEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQ 179
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2316-2611 |
5.30e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2316 AAEAERLRKvAQEEAEKLhkqvieetqkkriaEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEker 2395
Cdd:COG4372 27 AALSEQLRK-ALFELDKL--------------QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2396 qikvahVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEA 2475
Cdd:COG4372 89 ------LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2476 LR--LRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLR 2553
Cdd:COG4372 163 QEelAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678729579 2554 ADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKE 2611
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2836-3186 |
5.40e-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: 46.18 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2836 RQRKIAQDELERLKKkAEEARKQKDEADVEAEVQIVAAQQAALkcsTAEHQVQSVLAQQKEDSIMHKKLKQEYEKAKKLA 2915
Cdd:pfam15558 5 RDRKIAALMLARHKE-EQRMRELQQQAALAWEELRRRDQKRQE---TLERERRLLLQQSQEQWQAEKEQRKARLGREERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2916 KEAEAAKEKAEREAALLRQ-QAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQAEgaalkQKQQADAEMAK 2994
Cdd:pfam15558 81 RADRREKQVIEKESRWREQaEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNS-----LQLQERLEEAC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2995 HKK-LAEQTLKQKFQVE--QELTKVKLKLDDTDKQkSLLDDELQRLkdevddAVKQRGQVEEELFKvKVQMEELLKLKLR 3071
Cdd:pfam15558 156 HKRqLKEREEQKKVQENnlSELLNHQARKVLVDCQ-AKAEELLRRL------SLEQSLQRSQENYE-QLVEERHRELREK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3072 IEDENQRLLK---------KDKDNSQKFLAEEAENMKRLAEDAARLSVEsQEAARLRQIAEDDLIQQRALADKMLKE--- 3139
Cdd:pfam15558 228 AQKEEEQFQRakwraeekeEERQEHKEALAELADRKIQQARQVAHKTVQ-DKAQRARELNLEREKNHHILKLKVEKEekc 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1678729579 3140 KMQAIQESSRLKAE-AEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEET 3186
Cdd:pfam15558 307 HREGIKEAIKKKEQrSEQISREKEATLEEARKTARASFHMREKVREET 354
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2442-2531 |
5.41e-04 |
|
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: 43.62 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2442 QEAAHLKkqqEDAINAREEAEKELEKWRQKANEalrLRLQAEEEahkkslAQEDAEKQKEEAEREAKKR-AKAEESALKQ 2520
Cdd:COG0711 41 AEAERAK---EEAEAALAEYEEKLAEARAEAAE---IIAEARKE------AEAIAEEAKAEAEAEAERIiAQAEAEIEQE 108
|
90
....*....|.
gi 1678729579 2521 KDMAEKELERQ 2531
Cdd:COG0711 109 RAKALAELRAE 119
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3557-3590 |
5.45e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 5.45e-04
10 20 30
....*....|....*....|....*....|....
gi 1678729579 3557 LLEAQAATGYMLDPMKNQKLSVNEAVKEGLIGPE 3590
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2355-2586 |
5.55e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2355 SEAEKEAAKQKQKALDDLENLKKQAEEAERQVKqaEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEH 2434
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELK--ELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2435 GAVLQLQQEAAHLKKQQEDAINARE-----------------------EAEKEL-EKWRQKANEALRLRLQAEEEAHKKS 2490
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGsidklrkeierlewrqqtevlspEEEKELvEKIKELEKELEKAKKALEKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2491 LAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAE--KELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLED 2568
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAEEAQELHEEMIElyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRK 244
|
250
....*....|....*...
gi 1678729579 2569 ELYRLKNEVIAAQQQRKQ 2586
Cdd:COG1340 245 ELKKLRKKQRALKREKEK 262
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
861-968 |
5.63e-04 |
|
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: 42.82 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 861 EDERdrvqkKTFTKWVNKHLIKRAESQHHV---TD---LYEDLRDGHNLISLLEVLSGDTL-------PREKGRM--RFH 925
Cdd:cd21294 5 EDER-----REFTKHINAVLAGDPDVGSRLpfpTDtfqLFDECKDGLVLSKLINDSVPDTIdervlnkPPRKNKPlnNFQ 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1678729579 926 KLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTVI 968
Cdd:cd21294 80 MIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2503-2867 |
5.73e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2503 AEREAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQ 2582
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2583 QRKQLEDELakvrsemdiliqlkskaeketmsntEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQR 2662
Cdd:COG4372 81 ELEELNEQL-------------------------QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2663 AEAERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQR-KALEDEANQHKKEIEEKIVQLKKSSDAEME 2741
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAlDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2742 RQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAE 2821
Cdd:COG4372 216 LAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALEL 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1678729579 2822 EKVKKITAAEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEAE 2867
Cdd:COG4372 296 KLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
1636-1680 |
5.81e-04 |
|
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212702 [Multi-domain] Cd Length: 54 Bit Score: 40.72 E-value: 5.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1678729579 1636 VQAVCDFK---QQEITVHKGDECALLNNSQPFNWKVLNRFGNEAVVPS 1680
Cdd:cd11768 2 VVALYDFQpiePGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2623-2753 |
5.83e-04 |
|
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: 43.62 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2623 LEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAarqRAEAERILKEklaAISEAthlKTEAEIALKEKEAENERLRR 2702
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEA---RAEAAEIIAE---ARKEA---EAIAEEAKAEAEAEAERIIA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1678729579 2703 AAEDEAYQ-----RKALEDEANQHKKEIEEKIvqLKKSSDAemERQKAMVDDTLKQ 2753
Cdd:COG0711 100 QAEAEIEQerakaLAELRAEVADLAVAIAEKI--LGKELDA--AAQAALVDRFIAE 151
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3140-3307 |
5.84e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.95 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3140 KMQAIQESSRLKAEaemlQRQKDlAQEQAQKLLEDKQLMQRRLEEEteEYQKSLEAERRRQLEivAEAEKLKLQVSQLSE 3219
Cdd:PRK09510 66 RQQQQQKSAKRAEE----QRKKK-EQQQAEELQQKQAAEQERLKQL--EKERLAAQEQKKQAE--EAAKQAALKQKQAEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3220 AQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSK 3299
Cdd:PRK09510 137 AAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216
|
....*...
gi 1678729579 3300 EMADAQQK 3307
Cdd:PRK09510 217 KKAAAEAK 224
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2611-2980 |
6.07e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.83 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2611 ETMSNTEKSK-QLLEAEaTKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILkeklAAISEATHLKTEAEIA 2689
Cdd:pfam19220 38 AILRELPQAKsRLLELE-ALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLE----AALREAEAAKEELRIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2690 LKEKEAENERLRRAAEDEAYQRKALEDEaNQHKKEieEKIVQLKKSSDAEMERqkamvdDTLKQRR-VVEEEIRILKLNF 2768
Cdd:pfam19220 113 LRDKTAQAEALERQLAAETEQNRALEEE-NKALRE--EAQAAEKALQRAEGEL------ATARERLaLLEQENRRLQALS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2769 EKASsgkldleLELNKLKNIAEETQQsklRAEEEAEKLRKLALEEekrrreaeekvkkitaAEEEAARQRKIAQDELERL 2848
Cdd:pfam19220 184 EEQA-------AELAELTRRLAELET---QLDATRARLRALEGQL----------------AAEQAERERAEAQLEEAVE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2849 KKKAE-----------------------EARKQ---KDEADVEAEVqivAAQQAALKCSTAEHQVQSVLAQQKEDSIMHK 2902
Cdd:pfam19220 238 AHRAEraslrmklealtaraaateqllaEARNQlrdRDEAIRAAER---RLKEASIERDTLERRLAGLEADLERRTQQFQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2903 KLKQEYEKAKKLAKEAEAAKEKAEREAallrQQAEE-----AERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQA 2977
Cdd:pfam19220 315 EMQRARAELEERAEMLTKALAAKDAAL----ERAEEriaslSDRIAELTKRFEVERAALEQANRRLKEELQRERAERALA 390
|
...
gi 1678729579 2978 EGA 2980
Cdd:pfam19220 391 QGA 393
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2177-2393 |
6.29e-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: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2177 RLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQlaaahakaiakaekeAQELKLMMKEEVNRREIAAVDAEKQKQNIQLEL 2256
Cdd:TIGR02794 54 RIQQQKKPAAKKEQERQKKLEQQAEEAEKQRA---------------AEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2257 HELKNLSEQQIKDKgQLVDEALQSRTKIEEeiyliriqlettVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKlhkq 2336
Cdd:TIGR02794 119 KQAEEAKAKQAAEA-KAKAEAEAERKAKEE------------AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA---- 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678729579 2337 vIEETQKKRIAEkELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEK 2393
Cdd:TIGR02794 182 -KAEAEAKAKAE-EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGD 236
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2347-2569 |
6.54e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.09 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2347 AEKELQHKSEAEKEAAKQKQKALDdlenlKKQAEEAERQVKQAEVEKE-----RQIKVAHVAAQKSAAAELQSKHSSFVE 2421
Cdd:PRK05035 440 AIEQEKKKAEEAKARFEARQARLE-----REKAAREARHKKAAEARAAkdkdaVAAALARVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2422 KTSKL----EESLKQEHGAVLQLQQ-EAAHLKKQQEDAINAREEAEK-ELEKWRQKANEALRLRLQAEEEA-----HKKS 2490
Cdd:PRK05035 515 DNSAViaarEARKAQARARQAEKQAaAAADPKKAAVAAAIARAKAKKaAQQAANAEAEEEVDPKKAAVAAAiarakAKKA 594
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678729579 2491 LAQEDAEKQKEEAEREAKKRAKAEESALKQKdmaEKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDE 2569
Cdd:PRK05035 595 AQQAASAEPEEQVAEVDPKKAAVAAAIARAK---AKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPE 670
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2270-2597 |
6.81e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2270 KGQLvdEALQSRTKIEEEIYLIRIQLETT---VKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQK--K 2344
Cdd:PRK11281 42 QAQL--DALNKQKLLEAEDKLVQQDLEQTlalLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETREtlS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2345 RIAEKELQHKSEAEKEAAKQKQKALDD----LENLKKQAEEAERQV--KQAEVEKERQIKVAHVAAQKSAAAELQSK--- 2415
Cdd:PRK11281 120 TLSLRQLESRLAQTLDQLQNAQNDLAEynsqLVSLQTQPERAQAALyaNSQRLQQIRNLLKGGKVGGKALRPSQRVLlqa 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2416 HSSFVEKTSKLEeslKQEHGAVLQLQQeaahLKKQQEDAINAR-EEAEKELEKWRQKANEalrlrlqaeeeahkKSLAQe 2494
Cdd:PRK11281 200 EQALLNAQNDLQ---RKSLEGNTQLQD----LLQKQRDYLTARiQRLEHQLQLLQEAINS--------------KRLTL- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2495 dAEKQKEEAErEAKKRAKAEESALKQkdmaeKELERQRKVADS--TAQQKLTA-EQELIRLRADFDNAEQQRSLLEDELY 2571
Cdd:PRK11281 258 -SEKTVQEAQ-SQDEAARIQANPLVA-----QELEINLQLSQRllKATEKLNTlTQQNLRVKNWLDRLTQSERNIKEQIS 330
|
330 340 350
....*....|....*....|....*....|....*...
gi 1678729579 2572 RLKNEV----IAAQQQR--------KQLEDELAKVRSE 2597
Cdd:PRK11281 331 VLKGSLllsrILYQQQQalpsadliEGLADRIADLRLE 368
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2180-2385 |
6.98e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.10 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2180 DEEKAAKKLKAEEQKKMAEMQAELDKQKQlaaahaKAIAKAEKEAQELKLMMKEEVNRREiaavdaEKQKQNIQLELHEL 2259
Cdd:pfam15709 329 EQEKASRDRLRAERAEMRRLEVERKRREQ------EEQRRLQQEQLERAEKMREELELEQ------QRRFEEIRLRKQRL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2260 KNLSEQQIKD--KGQLVDEALQSRTKIEEEIY---LIRIQLETTVKQKSTAESE---LKQLRER-AAEAERLRKVAQEEA 2330
Cdd:pfam15709 397 EEERQRQEEEerKQRLQLQAAQERARQQQEEFrrkLQELQRKKQQEEAERAEAEkqrQKELEMQlAEEQKRLMEMAEEER 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1678729579 2331 EKLHKQVIEETQKKRIaekelqhksEAEKEAAKQKQKALDDLENLKKQAEEAERQ 2385
Cdd:pfam15709 477 LEYQRQKQEAEEKARL---------EAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2982-3387 |
7.04e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2982 LKQKQQADAEMAKHKKL-AEQTLKQKFQVEQELTKVKLKLDDTDKQK-----SLLDDELQRLKDEVDDAVKQRGQVEEEL 3055
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKeLEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKII 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3056 FKVKVQMEELLKLKLRIEDENQRLLKKDKDNSQKFLAEEAENMKRLAEdaaRLSVESQEAARLRQIAEDDliQQRALADK 3135
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQE---IKNLESQINDLESKIQNQE--KLNQQKDE 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3136 MLK----EKMQAIQESSRLKAEAEMLQRQ-KDLAQEQAQKLLEDKQLMQRR--LEEETEEYQKSLEAERR------RQLE 3202
Cdd:TIGR04523 413 QIKklqqEKELLEKEIERLKETIIKNNSEiKDLTNQDSVKELIIKNLDNTResLETQLKVLSRSINKIKQnleqkqKELK 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3203 I-VAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFE--RLNTSKEAGDLRDAIAD 3279
Cdd:TIGR04523 493 SkEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3280 LEKDKARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQQTFLTEREMLLKKEKLIeeekkklesQFEEEAKKSKALKDEQ 3359
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE---------KLSSIIKNIKSKKNKL 643
|
410 420
....*....|....*....|....*...
gi 1678729579 3360 ERQKQQMEEEKKKLHATMHEALSKQKEA 3387
Cdd:TIGR04523 644 KQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2324-2536 |
7.19e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2324 KVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQ--AEEAERQVKQAEVEKERQIKVAH 2401
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTikAEIEELTDELLNLVMDIEDPSAA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2402 VAAQKSAAAELQSKHSSFVEKTSKLEE---------SLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKELEKWRQKA 2472
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQS 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678729579 2473 NEAlrLRLQAEEEAHKKSLAQEDAEKQKEEAERE---AKKRAKAEESALKQKDMAEKELERQRKVAD 2536
Cdd:PHA02562 337 KKL--LELKNKISTNKQSLITLVDKAKKVKAAIEelqAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5210-5247 |
7.24e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 7.24e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1678729579 5210 QRFLEVQYLTGGLIEPDVESRVSLDESIKKGSIDARTA 5247
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2448-2543 |
7.33e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 43.23 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2448 KKQQEDAINAREEAEKELEKWRQKANEalrLRLQAEEEAHK-----KSLAQEDAEKQKEEAEREAKKRAKAEESALKQK- 2521
Cdd:PRK05759 48 ERAKKELELAQAKYEAQLAEARAEAAE---IIEQAKKRAAQiieeaKAEAEAEAARIKAQAQAEIEQERKRAREELRKQv 124
|
90 100
....*....|....*....|....*..
gi 1678729579 2522 -----DMAEKELERQrkvADSTAQQKL 2543
Cdd:PRK05759 125 adlavAGAEKILGRE---LDAAAQSDL 148
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2273-2457 |
7.52e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.23 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2273 LVDEAlQSRtkieeeiylIRIQLETTVKQKSTAESELKQLRERAAEAERLRKVA-QEEAEKLHKQviEETQKKRIAEKEL 2351
Cdd:COG0542 394 LIDEA-AAR---------VRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAsFERLAELRDE--LAELEEELEALKA 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2352 QHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKERQIKVAHVAAQksAAAELQSKhssfveKT----SKLE 2427
Cdd:COG0542 462 RWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEE--DIAEVVSR------WTgipvGKLL 533
|
170 180 190
....*....|....*....|....*....|...
gi 1678729579 2428 ESLKQehgAVLQLQQEaahLKKQ---QEDAINA 2457
Cdd:COG0542 534 EGERE---KLLNLEEE---LHERvigQDEAVEA 560
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2443-2699 |
7.64e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2443 EAAHLKKQQEDAINAREEAEKELEK----WRQKANEALRLRLQAE--EEAHK--KSLAQEDAEKQKEEAEREAKKRAKAE 2514
Cdd:COG3206 101 DKLNLDEDPLGEEASREAAIERLRKnltvEPVKGSNVIEISYTSPdpELAAAvaNALAEAYLEQNLELRREEARKALEFL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2515 ESALKQkdmAEKELERQRKvadstAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKV 2594
Cdd:COG3206 181 EEQLPE---LRKELEEAEA-----ALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2595 RSEMDI-------------LIQLKSKAEKETMSNTEKSKQLLEAEAtKMRDVAEE-AGKLRAIAEEAKHQRQVAEEEAAR 2660
Cdd:COG3206 253 PDALPEllqspviqqlraqLAELEAELAELSARYTPNHPDVIALRA-QIAALRAQlQQEAQRILASLEAELEALQAREAS 331
|
250 260 270
....*....|....*....|....*....|....*....
gi 1678729579 2661 QRAEAERiLKEKLAAISEathlkTEAEIALKEKEAENER 2699
Cdd:COG3206 332 LQAQLAQ-LEARLAELPE-----LEAELRRLEREVEVAR 364
|
|
| SH3_and_anchor |
TIGR04211 |
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
3008-3107 |
7.72e-04 |
|
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.
Pssm-ID: 275056 [Multi-domain] Cd Length: 198 Bit Score: 44.23 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3008 QVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKvqmeELLKLKLRIEDENQRLLKKDKDNS 3087
Cdd:TIGR04211 70 ELQQELAELQEELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIK----QISANAIELDEENRELREELAELK 145
|
90 100
....*....|....*....|
gi 1678729579 3088 QKFLAEEAENmKRLAEDAAR 3107
Cdd:TIGR04211 146 QENEALEAEN-ERLQENEQR 164
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5100-5133 |
7.84e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 7.84e-04
10 20 30
....*....|....*....|....*....|....
gi 1678729579 5100 EETGPIAGILDIDTLEKVSITEAIHRNLVDNITG 5133
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
2460-2723 |
7.95e-04 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 45.82 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2460 EAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEK-ELERQRKVADst 2538
Cdd:pfam04747 62 EQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEARRAEAEAKKRAAQEEEHKQWKAEQERiQKEQEKKEAD-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2539 aQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEK 2618
Cdd:pfam04747 140 -LKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTPTNTPAEPAEQVQEITGKKNKK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2619 SKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQrQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKEAENE 2698
Cdd:pfam04747 219 NKKKSESEATAAPASVEQVVEQPKVVTEEPHQ-QAAPQEKKNKKNKRKSESENVPAASETPVEPVVETTPPASENQKKNK 297
|
250 260
....*....|....*....|....*
gi 1678729579 2699 RLRRAAEDEAYQRKALEDEANQHKK 2723
Cdd:pfam04747 298 KDKKKSESEKVVEEPVQAEAPKSKK 322
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
3181-3432 |
7.97e-04 |
|
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: 45.94 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3181 RLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAK---KFKKQADKIAARL-----------HETE 3246
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQaetELCAEAEEMRARLaarkqeleeilHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3247 IATKEKMTVVEKLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMAD------AQQKQIEHEKTLLQQ-- 3318
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEdillleDQNSKLSKERKLLEEri 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3319 ----TFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMLSK 3394
Cdd:pfam01576 162 seftSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 1678729579 3395 QKEMQELEkKRLEQEIILADENQK-LREKLQQLEEAQKE 3432
Cdd:pfam01576 242 EEELQAAL-ARLEEETAQKNNALKkIRELEAQISELQED 279
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2240-2424 |
8.05e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2240 IAAVDAEKQKQNIQLELHELKNLSEQ---QIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLRERA 2316
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAaqaELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2317 AE------------------------------AERLRKVAQEEAEKLH-----KQVIEETQKKRIAEKELQHKSEAEKEA 2361
Cdd:COG3883 89 GEraralyrsggsvsyldvllgsesfsdfldrLSALSKIADADADLLEelkadKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 2362 AK--------QKQKALDDLENLKKQAEEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTS 2424
Cdd:COG3883 169 AKaeleaqqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2420-2533 |
8.46e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2420 VEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKEL-EKWRQKANEALRlrlQAEEEAHK--KSLAQEDA 2496
Cdd:PRK00409 522 IASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLlEEAEKEAQQAIK---EAKKEADEiiKELRQLQK 598
|
90 100 110
....*....|....*....|....*....|....*..
gi 1678729579 2497 EKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRK 2533
Cdd:PRK00409 599 GGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
3176-3432 |
8.78e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3176 QLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEaQTKAE-EEAKKFKKQADKIAARLHEteiatkekmt 3254
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNA-QVKELrEEAQELREKRDELNEKVKE---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3255 vvekLEFERLNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMADAQQKQ------IEHEKTLLQQTFLTEREMLL 3328
Cdd:COG1340 76 ----LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQqtevlsPEEEKELVEKIKELEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3329 KKEKLIEEekkkleSQFEEEAKKSKALKDEQERQKQQMEE---EKKKLHATMHEALSKQKEAEKEMLSKQKEMQELEKKr 3405
Cdd:COG1340 152 AKKALEKN------EKLKELRAELKELRKEAEEIHKKIKElaeEAQELHEEMIELYKEADELRKEADELHKEIVEAQEK- 224
|
250 260
....*....|....*....|....*..
gi 1678729579 3406 leqeiiLADENQKLREKLQQLEEAQKE 3432
Cdd:COG1340 225 ------ADELHEEIIELQKELRELRKE 245
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4786-4820 |
8.91e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 8.91e-04
10 20 30
....*....|....*....|....*....|....*
gi 1678729579 4786 LLEAQASTGYVIDPIKNLKLTVNEAVRMGIVGPEF 4820
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1914-2520 |
9.32e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1914 LSSVYLEKLKTVEMVIRNTQGAEGVLKQYEDCLREVHTVPGDVKEVETYRTKLKKMRGEAEGEQPVFDSLEEELKKATVV 1993
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 1994 SDKMSRVHSERDVELDhyrqhlsglqdrwkavfaqmdiRQRELEQLgrqLGYYHESYDWLIHWITDAKERQEKIQAVSIT 2073
Cdd:PRK03918 292 AEEYIKLSEFYEEYLD----------------------ELREIEKR---LSRLEEEINGIEERIKELEEKEERLEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2074 DSKTLK--EQLSQEKKLLEEIENNKDNVDECQKYAKAYINSIKDYELQLVAYnaqadplasplKKTKLDSASDNIIQEYV 2151
Cdd:PRK03918 347 LKELEKrlEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK-----------AKEEIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2152 TLRTRYSELMTLTSQYIKFITE---TQRRLEDEEKaaKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELK 2228
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKcpvCGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2229 LMMKEEVNRREIAAVDAEKQKQNIQ---LELHELKNLSEQQIKDKGQLvdEALQSRTKIEEEIYLIRIQLETTVKQKSTA 2305
Cdd:PRK03918 494 ELIKLKELAEQLKELEEKLKKYNLEeleKKAEEYEKLKEKLIKLKGEI--KSLKKELEKLEELKKKLAELEKKLDELEEE 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2306 ESEL-KQLRERAAEAERLRKVAQEEAEKLHKQVIEetqkKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAER 2384
Cdd:PRK03918 572 LAELlKELEELGFESVEELEERLKELEPFYNEYLE----LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2385 QVKqaevekerqikvahvaaqksaaaELQSKHSsfvektsklEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAEKE 2464
Cdd:PRK03918 648 ELE-----------------------ELEKKYS---------EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2465 LEKwrqkaneaLRLRLQAEEEAHKKSlaqEDAEKQKEEAEREAKK----RAKAEESALKQ 2520
Cdd:PRK03918 696 LEK--------LKEELEEREKAKKEL---EKLEKALERVEELREKvkkyKALLKERALSK 744
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
2492-2679 |
9.34e-04 |
|
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: 44.59 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2492 AQEDAEKQKEEAEREAKKRAKA-EESALKQKDMAEKELERQR---KVADSTAQQKLTAEQELIRLRADFDNA------EQ 2561
Cdd:pfam12037 1 GGPGSDKDPKKSNDKPRTAYSGfDPEALERAAKAARELESSPhakKALELMKKQEQTRQAELQAKIKEYEAAqeqlkiER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2562 QRsLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAE-----------KETMSNTEKSKQLLEAEA--- 2627
Cdd:pfam12037 81 QR-VEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEEllrkqeesvakQEAMRIQAQRRQTEEHEAelr 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 2628 --TKMRDVAEEAgklRAIAEEAKHQRQVAEEEaARQRAEAERilKEKLAAISEA 2679
Cdd:pfam12037 160 reTERAKAEAEA---EARAKEERENEDLNLEQ-LREKANEER--ETVLESINTA 207
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4176-4212 |
9.35e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 9.35e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1678729579 4176 KYLQGSDSIAGIYLEPTKEKISIYQAMKKKLLRQNTG 4212
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3075-3252 |
9.39e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3075 ENQRLLKKDKDNSQKFLAE--EAENMKRLAEDAARLSVESQEAARLRQIAE--DDLIQQRALADKMLKEKMQAIQESSRL 3150
Cdd:PRK09510 68 QQQQKSAKRAEEQRKKKEQqqAEELQQKQAAEQERLKQLEKERLAAQEQKKqaEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3151 KAEAEMLQrqkdlAQEQAQKLLEDKQlmqrrlEEETEEYQKSLEAERRRQLEIVAEAEKLKlqvsqlsEAQTKAEEEAKK 3230
Cdd:PRK09510 148 KAEAEAKR-----AAAAAKKAAAEAK------KKAEAEAAKKAAAEAKKKAEAEAAAKAAA-------EAKKKAEAEAKK 209
|
170 180
....*....|....*....|....*..
gi 1678729579 3231 -----FKKQADKIAARLHETEIATKEK 3252
Cdd:PRK09510 210 kaaaeAKKKAAAEAKAAAAKAAAEAKA 236
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2505-3404 |
1.04e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2505 REAKKRAKAEESALKqkdmAEKELERQRKvadstaqqKLTAEQE-LIRLRADFDNAEQQRSLLEDELYRLK---NEVIAA 2580
Cdd:PRK04863 276 RHANERRVHLEEALE----LRRELYTSRR--------QLAAEQYrLVEMARELAELNEAESDLEQDYQAASdhlNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2581 QQQRKQLEdelakvRSEMDILiQLKSKAEKETMSNTEKSKQLLEAEAtKMRDVAEEAGKLRA------IAEEAKHQRQVA 2654
Cdd:PRK04863 344 LRQQEKIE------RYQADLE-ELEERLEEQNEVVEEADEQQEENEA-RAEAAEEEVDELKSqladyqQALDVQQTRAIQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2655 EEEAARQRAEAERILKekLAAISEATHLKTEAEIALKEKEAENERLrraaedEAYQRKALEDEAnqhkKEIEEKIVQLKK 2734
Cdd:PRK04863 416 YQQAVQALERAKQLCG--LPDLTADNAEDWLEEFQAKEQEATEELL------SLEQKLSVAQAA----HSQFEQAYQLVR 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2735 SSDAEMERQKAMvddtlKQRRVVEEEIRILKLNFEKASSgkldLELELNKLKNIAEEtQQSKLRAEEEAEKLRKLALEee 2814
Cdd:PRK04863 484 KIAGEVSRSEAW-----DVARELLRRLREQRHLAEQLQQ----LRMRLSELEQRLRQ-QQRAERLLAEFCKRLGKNLD-- 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2815 krrreaeekvkkitaAEEEAARQRKIAQDELERLKKKAEEARKQKdeADVEAEVQIVAAQQAAL-KCSTAEHQVQSVLAQ 2893
Cdd:PRK04863 552 ---------------DEDELEQLQEELEARLESLSESVSEARERR--MALRQQLEQLQARIQRLaARAPAWLAAQDALAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2894 QKE------------DSIMHKKLKQEYEkakklakeaeaakekaereaalLRQQAEE-AERQKAAAEQEAAIQAKAQEDA 2960
Cdd:PRK04863 615 LREqsgeefedsqdvTEYMQQLLERERE----------------------LTVERDElAARKQALDEEIERLSQPGGSED 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2961 ERLRKEAE---------------------FEaakraqaegAALKQKQQA----DAEMAKHKKLA-EQTLKQKFQVEQELT 3014
Cdd:PRK04863 673 PRLNALAErfggvllseiyddvsledapyFS---------ALYGPARHAivvpDLSDAAEQLAGlEDCPEDLYLIEGDPD 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3015 kvklKLDDtdkqkSLLD-DELQR--LKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLLKkdkdnsqkfL 3091
Cdd:PRK04863 744 ----SFDD-----SVFSvEELEKavVVKIADRQWRYSRFPEVPLFGRAAREKRIEQLRAEREELAERYAT---------L 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3092 AEEAENMKRLAEDAAR-------LSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQeSSRLKAEAEMLQRQKDLA 3164
Cdd:PRK04863 806 SFDVQKLQRLHQAFSRfigshlaVAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQ-LEQAKEGLSALNRLLPRL 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3165 qeqaqKLLEDKQLMQrRLEEETEEYQKSLEAER--RRQLEIVAEAEKL--KLQVSQLSEAQTKAE-EEAKKFKKQADKIA 3239
Cdd:PRK04863 885 -----NLLADETLAD-RVEEIREQLDEAEEAKRfvQQHGNALAQLEPIvsVLQSDPEQFEQLKQDyQQAQQTQRDAKQQA 958
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3240 arlheteIATKEKMTVVEKLEFErlntskEAGDLRDAIADL-EKDKARLkKEAEELQNKSKEMA-DAQQKQIEHEKTL-- 3315
Cdd:PRK04863 959 -------FALTEVVQRRAHFSYE------DAAEMLAKNSDLnEKLRQRL-EQAEQERTRAREQLrQAQAQLAQYNQVLas 1024
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3316 LQQTFLTEREMLLkkeklieeekkklesQFEEEAKK--SKALKDEQERQKQQMEEekkkLHATMHEALSKQKEAEKEMLS 3393
Cdd:PRK04863 1025 LKSSYDAKRQMLQ---------------ELKQELQDlgVPADSGAEERARARRDE----LHARLSANRSRRNQLEKQLTF 1085
|
970
....*....|.
gi 1678729579 3394 KQKEMQELEKK 3404
Cdd:PRK04863 1086 CEAEMDNLTKK 1096
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2829-3220 |
1.19e-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: 45.71 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2829 AAEEEAARQRKIAQDELERLKKKAEEARKQKD-EADVEAEVQivaaqqaalkcSTAEH--QVQSVLAQQkedsimhKKLk 2905
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSArESDLEQDYQ-----------AASDHlnLVQTALRQQ-------EKI- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2906 QEYEKAKKLAKEAeaakekaereaalLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKE-AEFEAAKRAQAEGAAlkQ 2984
Cdd:COG3096 350 ERYQEDLEELTER-------------LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQlADYQQALDVQQTRAI--Q 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2985 KQQADAEMAKHKKL----------AEQTLKQKFQVEQELTKVKL----KLDDTDKQKSLLDDELQRLK---DEVD--DAV 3045
Cdd:COG3096 415 YQQAVQALEKARALcglpdltpenAEDYLAAFRAKEQQATEEVLeleqKLSVADAARRQFEKAYELVCkiaGEVErsQAW 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3046 KQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLlkkdkdnsqkflaEEAENMKRLAED-AARLSVESQEAARLrqiaED 3124
Cdd:COG3096 495 QTARELLRRYRSQQALAQRLQQLRAQLAELEQRL-------------RQQQNAERLLEEfCQRIGQQLDAAEEL----EE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3125 DLIQQRALADKMLKEKMQAIQESSRLKAEAEML-QRQKDL---------AQEQAQKL-------LEDKQ----LMQRRLE 3183
Cdd:COG3096 558 LLAELEAQLEELEEQAAEAVEQRSELRQQLEQLrARIKELaarapawlaAQDALERLreqsgeaLADSQevtaAMQQLLE 637
|
410 420 430
....*....|....*....|....*....|....*..
gi 1678729579 3184 EETEeyqksLEAERRrqlEIVAEAEKLKLQVSQLSEA 3220
Cdd:COG3096 638 RERE-----ATVERD---ELAARKQALESQIERLSQP 666
|
|
| NtpH |
COG2811 |
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ... |
2456-2530 |
1.21e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 442060 [Multi-domain] Cd Length: 108 Bit Score: 41.44 E-value: 1.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678729579 2456 NAREEAEKELEKWRQKANEalrLRLQAEEEAHKksLAQEDAEKQKEEAEREAKK-RAKAEESALKQKDMAEKELER 2530
Cdd:COG2811 23 EAKEEREERIAEAREEAEE---IIEQAEEEAEE--EAQERLEEAREEAEAEAEEiIEEGEKEAEALKKKAEDKLDK 93
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2453-2671 |
1.23e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.66 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2453 DAINAREEAEKELEKWRQKANEALRlrlQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQ--KDMAEKELER 2530
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDMEEDLV---EARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgrEDLAREALER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2531 qrkvadstaqqKLTAEQELIRLRADFDNAEQQrslledelyrlkneVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAE- 2609
Cdd:COG1842 93 -----------KAELEAQAEALEAQLAQLEEQ--------------VEKLKEALRQLESKLEELKAKKDTLKARAKAAKa 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678729579 2610 KETMSNTEKSKQLLEAEAT--KMRD-VAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKE 2671
Cdd:COG1842 148 QEKVNEALSGIDSDDATSAleRMEEkIEEMEARAEAAAELAAGDSLDDELAELEADSEVEDELAA 212
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
3022-3433 |
1.24e-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: 45.07 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3022 DTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIE---DENQRLlkkdkdnsqkflaeeaENm 3098
Cdd:pfam05622 18 ELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEqlqEENFRL----------------ET- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3099 krlAEDAARLSVESQEaarlRQIAEddlIQQRaladkmLKEKMQAIQESSRLKAEAEMLQRQKD-LAQEQAQ-----KLL 3172
Cdd:pfam05622 81 ---ARDDYRIKCEELE----KEVLE---LQHR------NEELTSLAEEAQALKDEMDILRESSDkVKKLEATvetykKKL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3173 ED-----KQLmqRRLEEETEEYQK---SLEAERRRQLEIVAEAEKLKLQVSQLseaQTKAEEEAKKfkkqADKIA---AR 3241
Cdd:pfam05622 145 EDlgdlrRQV--KLLEERNAEYMQrtlQLEEELKKANALRGQLETYKRQVQEL---HGKLSEESKK----ADKLEfeyKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3242 LHET-EIATKEKmtvvEKLEFERlNTSKEAGD-LRDA---IADLEKDKARLKKEAEELQNKSKEMADAQQK----QIEHE 3312
Cdd:pfam05622 216 LEEKlEALQKEK----ERLIIER-DTLRETNEeLRCAqlqQAELSQADALLSPSSDPGDNLAAEIMPAEIRekliRLQHE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3313 -KTLLQQTFLTEREmllkkeklieeEKKKLESQFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEM 3391
Cdd:pfam05622 291 nKMLRLGQEGSYRE-----------RLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSS 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 3392 LSKQKEMQ----------ELEKKRLEQEIILADENQKLREKLQQLEEA--QKEQ 3433
Cdd:pfam05622 360 LLKQKLEEhleklheaqsELQKKKEQIEELEPKQDSNLAQKIDELQEAlrKKDE 413
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2479-2636 |
1.24e-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: 44.15 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2479 RLQAEEEAHKKSLAqeDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELE--RQRKVADSTAQQKLTAEQELIRLRADF 2556
Cdd:COG1579 21 RLEHRLKELPAELA--ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEevEARIKKYEEQLGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2557 DNAEQQRSLLEDELYRLKNEVIAAQQQRKQLEDELAKVRSEmdiLIQLKSKAEKEtMSNTEKSKQLLEAEATKMRDVAEE 2636
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEE-LAELEAELEELEAEREELAAKIPP 174
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3596-3626 |
1.29e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.29e-03
10 20 30
....*....|....*....|....*....|.
gi 1678729579 3596 LSAERAVIGYKDPYTGRKISVFEAMKKGLME 3626
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2450-2728 |
1.32e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.97 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2450 QQEDAINAREEAEKELEKwRQKANEAlrlrlQAEEEAHKKSLAQEdaeKQKEEAEREAKKRAKAEESA-----LKQK--- 2521
Cdd:PRK07735 11 KKEAARRAKEEARKRLVA-KHGAEIS-----KLEEENREKEKALP---KNDDMTIEEAKRRAAAAAKAkaaalAKQKreg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2522 --DMAEKELERQRKVADSTAQQKLTAeqelirlradfdnaeqqrslledelyrLKNEVIAAQQQRKQLEDELAKVRSEMD 2599
Cdd:PRK07735 82 teEVTEEEKAKAKAKAAAAAKAKAAA---------------------------LAKQKREGTEEVTEEEKAAAKAKAAAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2600 ILIQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIA---EEAKHQRQ----VAEEEAARQRAEAERILKEK 2672
Cdd:PRK07735 135 AKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAAlakQKAAEAGEgteeVTEEEKAKAKAKAAAAAKAK 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1678729579 2673 LAAISEAthlKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEK 2728
Cdd:PRK07735 215 AAALAKQ---KASQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTKGAEGKKEEEPK 267
|
|
| 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 ... |
2655-2754 |
1.38e-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: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2655 EEEAARQRAEAERILKEKLAAISEAthlkteaEIALKEKEAENERLRRAAEDEAYQrkaledEANQHKKEIEEKIVQLKK 2734
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAALAEA-------EQQLKEARAEAQEIIENAKKRAEK------LKEEIVAAAEAEAERIIE 98
|
90 100
....*....|....*....|
gi 1678729579 2735 SSDAEMERQKAMVDDTLKQR 2754
Cdd:pfam00430 99 QAAAEIEQEKDRALAELRQQ 118
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2710-3258 |
1.40e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2710 QRKALEDEANQHKKEIEEKIVQLKKSSDaEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIA 2789
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLT-EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2790 EETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRKI---AQDELERLKKKAEEARKQKDEADVEA 2866
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEisnTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2867 EvqivaaqQAALKCSTAEHQVQ------SVLAQQKEDSImHKKLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAE 2940
Cdd:TIGR04523 277 E-------QNNKKIKELEKQLNqlkseiSDLNNQKEQDW-NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2941 RQKAAA----EQEAAIQAKAQEDAERLRKEAE--FEAAKRAQAEGAALKQKQQADAEMAKHKKLAEQTLKQ-KFQVEQEL 3013
Cdd:TIGR04523 349 KELTNSesenSEKQRELEEKQNEIEKLKKENQsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQeKELLEKEI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3014 TKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQME----ELLKLKLRIEDENQRL--LKKDKDNS 3087
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINkikqNLEQKQKELKSKEKELkkLNEEKKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3088 QKFLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKML--KEKMQAIQESSRLKAEAEMLQRqkdlAQ 3165
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKK----KQ 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3166 EQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHET 3245
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
|
570
....*....|...
gi 1678729579 3246 EIATKEKMTVVEK 3258
Cdd:TIGR04523 665 IKKIKESKTKIDD 677
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
3133-3244 |
1.44e-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: 44.11 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3133 ADKMLKEKMQAIQESsrlKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEivaeaEKLKL 3212
Cdd:cd16269 189 ADQALTEKEKEIEAE---RAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLK-----EQERA 260
|
90 100 110
....*....|....*....|....*....|..
gi 1678729579 3213 QVSQLSEaqtKAEEEAKKFKKQADKIAARLHE 3244
Cdd:cd16269 261 LESKLKE---QEALLEEGFKEQAELLQEEIRS 289
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
2300-2386 |
1.49e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 42.30 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2300 KQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKElqhksEAEKEAAKQKQKALDDLEnlkKQA 2379
Cdd:PRK07353 54 EAEKLEAQYEQQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQASKE-----KARREIEQQKQAALAQLE---QQV 125
|
....*..
gi 1678729579 2380 EEAERQV 2386
Cdd:PRK07353 126 DALSRQI 132
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2932-3264 |
1.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2932 LRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQAEgaalKQKQQADAEMAKHKKLAEQTLKQKFQVEQ 3011
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE----EELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3012 ELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLLKKDKDNSQKFL 3091
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3092 AEEAENM------KRLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQ 3165
Cdd:COG4372 189 LKEANRNaekeeeLAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3166 EQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHET 3245
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330
....*....|....*....
gi 1678729579 3246 EIATKEKMTVVEKLEFERL 3264
Cdd:COG4372 349 GLLDNDVLELLSKGAEAGV 367
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
2506-2861 |
1.74e-03 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 44.65 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2506 EAKKRAKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIRlradfDNAEQQRSLLEDELYRLKNEVIAAQ---- 2581
Cdd:pfam14817 64 QDKGKAESRQSAAARRLELQKEIERLRAEISRLDKQLEARELELSR-----EEAERERALDEISDSRHRQLLLEAYdqqc 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2582 -QQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKS--KQLLEAEATKMRDVaEEAGKLRAiaeeakHQRQvaeeea 2658
Cdd:pfam14817 139 eEARKILAEDHQRLQGQLQQLRDAARKAEKEVVFGDSKGskSSVIALEPQVLRDV-REACELRA------QFLQ------ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2659 arqraeaERILKEKLAAISEATHLKTEaeialkEKEAENERLRRAAEDEAYQR------KALEDEANQHKKEIEEKIVQL 2732
Cdd:pfam14817 206 -------ELLESSLKAYEGSGIHMNRD------QRRAVIQHWLSAVETLLTSHppshllQALEHLAAREKTAIQEETESL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2733 KKSSDAEMERQKAMVDDTLKqrrVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQ--SKLRAEEEAEKLRKLA 2810
Cdd:pfam14817 273 DVRADAEALRFRYESNHLLD---VSSDESSDLPSVRQLLERQWAHVQQFLNELAETRSRCQQlqARLQGLKDEAELESLG 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678729579 2811 LEEEKRRREAEEKV--KKITAAEEEA---------------ARQRKIAQDELERLKKKAEEARKQKDE 2861
Cdd:pfam14817 350 IGDTSQNDSLLRQVleLELQAAGLAAsrdtlrsecqqlnklARERQEALRSLQKKWQRILDFRQLVSE 417
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2231-2373 |
1.87e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2231 MKEEVNRREIAAVDAEKQKQNIQLELHELknlsEQQIKDKGQLV--DEALQSRTKIEEEIYLIRIQLETTVKQKSTAESE 2308
Cdd:COG1579 36 LEDELAALEARLEAAKTELEDLEKEIKRL----ELEIEEVEARIkkYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678729579 2309 LKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQhksEAEKEAAKQKQKALDDLE 2373
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE---AELEELEAEREELAAKIP 173
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
3126-3433 |
1.92e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3126 LIQQRAlADKMLKEKMQAIQESSRLKAEAEMLQRQkDLAQEQAQKLLEDKQLMQRRLEEET--EEYQKSLEAERRRQ--- 3200
Cdd:COG3206 60 LVEPQS-SDVLLSGLSSLSASDSPLETQIEILKSR-PVLERVVDKLNLDEDPLGEEASREAaiERLRKNLTVEPVKGsnv 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3201 LEIVAEAE-----KLKLQ------VSQLSEAQTKAEEEAKKF-KKQADKIAARLHETEiatkekmtvvEKLE-FER---- 3263
Cdd:COG3206 138 IEISYTSPdpelaAAVANalaeayLEQNLELRREEARKALEFlEEQLPELRKELEEAE----------AALEeFRQkngl 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3264 LNTSKEAGDLRDAIADLEKDKARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQQTFLTEremLLKKEKLIEEEKKKLES 3343
Cdd:COG3206 208 VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3344 QFEEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMlskQKEMQELEKK------------RLEQEII 3411
Cdd:COG3206 285 RYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASL---QAQLAQLEARlaelpeleaelrRLEREVE 361
|
330 340
....*....|....*....|...
gi 1678729579 3412 LADEN-QKLREKLQQLEEAQKEQ 3433
Cdd:COG3206 362 VARELyESLLQRLEEARLAEALT 384
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
3346-3425 |
1.96e-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: 43.72 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3346 EEEAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMLSKQKEmQELEKKRLEQEIILADENQKLREKLQQ 3425
Cdd:cd16269 207 AEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQE-RALESKLKEQEALLEEGFKEQAELLQE 285
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2857-3043 |
1.97e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2857 KQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKEDSIMHKKLKQEYEKAKKLAKEAEAAKEKAEREAALLRQQA 2936
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2937 EEAERQKAAAEQEAAIQAKAQEDAE-------RLRKEAEFEAAKRAQAEG---AALKQKQQADAEmAKHKKLAEqtlkQK 3006
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEaakkaaaEAKKKAEAEAAAKAAAEAkkkAEAEAKKKAAAE-AKKKAAAE----AK 224
|
170 180 190
....*....|....*....|....*....|....*..
gi 1678729579 3007 FQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDD 3043
Cdd:PRK09510 225 AAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2166-2337 |
2.11e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2166 QYIKFITETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELKLMMKEEVNR-------- 2237
Cdd:COG4942 62 RRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavrrlqyl 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2238 REIAAVDAE--KQKQNIQLELHELKNLSEQQIKDKGQLVDEALQSRTKIEEEIYLIRIQLETTVKQKSTAESELKQLRER 2315
Cdd:COG4942 142 KYLAPARREqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
170 180
....*....|....*....|..
gi 1678729579 2316 AAEAERLRKVAQEEAEKLHKQV 2337
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERT 243
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2292-2667 |
2.17e-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: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2292 RIQLETTVKQkstAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALD- 2370
Cdd:pfam05701 221 KLNWEKELKQ---AEEELQRLNQQLLSAKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAALAs 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2371 ---DLENLKKQAEEAERQVK---------QAEVEKErqikvahvaaqKSAAAELQSKHSSFVEKTSKLEESLKqehgavl 2438
Cdd:pfam05701 298 akkELEEVKANIEKAKDEVNclrvaaaslRSELEKE-----------KAELASLRQREGMASIAVSSLEAELN------- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2439 QLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLrlqaeeeAHKkslAQEDAEKQKEEAErEAKKRAKAEESAL 2518
Cdd:pfam05701 360 RTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSL-------AQA---AREELRKAKEEAE-QAKAAASTVESRL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2519 KQkdmAEKELErQRKVADSTAQQKLTA--EQELIRLRADFDNAEQQRSLLEDELYRLkneviaaqQQRKQLEDELAKVRS 2596
Cdd:pfam05701 429 EA---VLKEIE-AAKASEKLALAAIKAlqESESSAESTNQEDSPRGVTLSLEEYYEL--------SKRAHEAEELANKRV 496
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 2597 eMDILIQLKSKAEKETMSnTEKSKQLleAEATKMRDVAEEAGKLRaiAEEAKHQRQVAEEEAARQRAEAER 2667
Cdd:pfam05701 497 -AEAVSQIEEAKESELRS-LEKLEEV--NREMEERKEALKIALEK--AEKAKEGKLAAEQELRKWRAEHEQ 561
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
3092-3237 |
2.29e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.09 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3092 AEEAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAqkl 3171
Cdd:COG2268 223 AEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEA--- 299
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678729579 3172 ledkqlmQRRLEEETEEYQKSLEAERRRQlEIVAEAEKlklqvsQLSEAQTKAEEEAKKFKKQADK 3237
Cdd:COG2268 300 -------EREEAELEADVRKPAEAEKQAA-EAEAEAEA------EAIRAKGLAEAEGKRALAEAWN 351
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3631-3667 |
2.29e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.29e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1678729579 3631 IRVLEAQLATGGIIDPINSHRVPNETAYKQGQYDVEM 3667
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2173-2393 |
2.42e-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: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2173 ETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQELKLMMKEEVNRREIAAVDAEKQKQNi 2252
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKE- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2253 qlelhELKNLSEQQIKDKgqlvdEALQSRTKIEEeiyliriqlettVKQKSTAESELKQLRERAAEAERlrkvAQEEAEK 2332
Cdd:TIGR02794 147 -----EAAKQAEEEAKAK-----AAAEAKKKAEE------------AKKKAEAEAKAKAEAEAKAKAEE----AKAKAEA 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 2333 LHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDL--ENLKKQAEEAERQVKQAEVEK 2393
Cdd:TIGR02794 201 AKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLasGSNAEKQGGARGAAAGSEVDK 263
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2173-2519 |
2.47e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 43.87 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2173 ETQRRLEDEEKAAkkLKAEEQKKMAE---MQAELDKQKQLAAAhakaiakaekeaQELKLMMKEEVNRReiaaVDAEKQK 2249
Cdd:pfam15558 19 EEQRMRELQQQAA--LAWEELRRRDQkrqETLERERRLLLQQS------------QEQWQAEKEQRKAR----LGREERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2250 QNIQLElhelKNLSEQQIKDKGQLVDEALQSRTKIEEEIYLiriqlettvkqkstAESELKQLRERAAEAERLRKVAQEE 2329
Cdd:pfam15558 81 RADRRE----KQVIEKESRWREQAEDQENQRQEKLERARQE--------------AEQRKQCQEQRLKEKEEELQALREQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2330 AE-KLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKKQAEEAERQV------KQAEVEKERQIKVAHV 2402
Cdd:pfam15558 143 NSlQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRLsleqslQRSQENYEQLVEERHR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2403 AAQKSAAAELQskHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINAREEAE--KELEKWRQKANEALRLRL 2480
Cdd:pfam15558 223 ELREKAQKEEE--QFQRAKWRAEEKEEERQEHKEALAELADRKIQQARQVAHKTVQDKAQraRELNLEREKNHHILKLKV 300
|
330 340 350
....*....|....*....|....*....|....*....
gi 1678729579 2481 QAEEEAHKKSLaQEDAEKQKEEAEREAKKRAKAEESALK 2519
Cdd:pfam15558 301 EKEEKCHREGI-KEAIKKKEQRSEQISREKEATLEEARK 338
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
869-937 |
2.57e-03 |
|
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: 40.72 E-value: 2.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 869 KKTFTKWVNKHLIKraesQH-HVTDLYEDLRDGHNLISLLEVLSGDTLPREK----GRMRFHKLQNVQIALDFL 937
Cdd:cd21221 3 VRVLTEWINEELAD----DRiVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2826-3019 |
2.69e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2826 KITAAEEEA-----------ARQRKIAQDELER---LKKKAeEARKQKDEADVEAEVQIVAAQQAALKCSTAE-HQVQSV 2890
Cdd:PRK05035 437 EIRAIEQEKkkaeeakarfeARQARLEREKAARearHKKAA-EARAAKDKDAVAAALARVKAKKAAATQPIVIkAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2891 LAQQKEDSIMHKKLKQEyeKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKAAAeqeaaiqakAQEDAERLRKEAEFE 2970
Cdd:PRK05035 516 NSAVIAAREARKAQARA--RQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANA---------EAEEEVDPKKAAVAA 584
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1678729579 2971 AAKRAQAEGAALKQKQQADAEMakhkklAEQTLKQKFQVEQELTKVKLK 3019
Cdd:PRK05035 585 AIARAKAKKAAQQAASAEPEEQ------VAEVDPKKAAVAAAIARAKAK 627
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
2391-2708 |
2.70e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.07 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2391 VEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEES---------------LKQEhgaVLQLQQEAAHLKKQQEDAI 2455
Cdd:PLN03229 413 VDPERKVNMKKREAVKTPVRELEGEVEKLKEQILKAKESsskpselalnemiekLKKE---IDLEYTEAVIAMGLQERLE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2456 NAREEAEKELEKwRQKANEALRLRLQAEEEAHKKSLAQEDAE---KQKEEAEREAkKRAKaeeSALKQKDMAEK-ELERQ 2531
Cdd:PLN03229 490 NLREEFSKANSQ-DQLMHPVLMEKIEKLKDEFNKRLSRAPNYlslKYKLDMLNEF-SRAK---ALSEKKSKAEKlKAEIN 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2532 RKVADSTAQQKLTAEQELIRlradfDNAEQQRSLLEDELYR-LKNEVIAAqqqRKQLEDELAKVRSEMDILIQLKSKAEK 2610
Cdd:PLN03229 565 KKFKEVMDRPEIKEKMEALK-----AEVASSGASSGDELDDdLKEKVEKM---KKEIELELAGVLKSMGLEVIGVTKKNK 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2611 ETMSNT------EKSKQLLEAEATKMRDVAEEAGkLRAIAEEAKhqRQVAEEEAARQRAEAERI------LKEKLAAISE 2678
Cdd:PLN03229 637 DTAEQTpppnlqEKIESLNEEINKKIERVIRSSD-LKSKIELLK--LEVAKASKTPDVTEKEKIealeqqIKQKIAEALN 713
|
330 340 350
....*....|....*....|....*....|....*..
gi 1678729579 2679 ATHLKT-----EAEIALKEK--EAENERLRRAAEDEA 2708
Cdd:PLN03229 714 SSELKEkfeelEAELAAAREtaAESNGSLKNDDDKEE 750
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2440-2776 |
2.76e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.94 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2440 LQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEalrLRLQAEEEAHKKSLAQEDAEKQ---------KEEAEREAKKR 2510
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKE---LYLAKEEDLKRQNAVLQEAQVEldalqnqlaLARAEMENIKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2511 AKAEESALKQKDMAEKELERQRKVADSTAQQKLTAEQELIR--LRADFDNAE--QQRSLLEDELYRLKNEVIAAQQQrKQ 2586
Cdd:pfam03528 83 VATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVREYEVQfhRRLEQERAQwnQYRESAEREIADLRRRLSEGQEE-EN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2587 LEDELAKVRSEMDILIQLKSKAEKETMS----NTEKSKQLLEAEATKMRDVAE--EAGK-----LRAIAEEAKHQRQVAE 2655
Cdd:pfam03528 162 LEDEMKKAQEDAEKLRSVVMPMEKEIAAlkakLTEAEDKIKELEASKMKELNHylEAEKscrtdLEMYVAVLNTQKSVLQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2656 EEAARQRAEAERILKEKLAAISEATHLKTEAEIAlKEKEAENERLrrAAEDEAYQRKALEDEANQHKKEIEekivqlKKS 2735
Cdd:pfam03528 242 EDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKA-NDQFLESQRL--LMRDMQRMESVLTSEQLRQVEEIK------KKD 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1678729579 2736 SDAEMERQKAMVDDTLKQRRVVEEEIRILKLNFEKASSGKL 2776
Cdd:pfam03528 313 QEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPL 353
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
3112-3455 |
2.96e-03 |
|
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: 44.27 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3112 SQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAemLQRQKDlAQEQAQKLLEDKQLMQRRLEEETEEYQK 3191
Cdd:TIGR00606 236 SREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK--KQMEKD-NSELELKMEKVFQGTDEQLNDLYHNHQR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3192 SLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFErlntskeag 3271
Cdd:TIGR00606 313 TVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFE--------- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3272 dlRDAIADLEKDKA-RLKKEAEELQNK--SKEMADAQqkqiehEKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEEE 3348
Cdd:TIGR00606 384 --RGPFSERQIKNFhTLVIERQEDEAKtaAQLCADLQ------SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3349 AKKSKalkdeqeRQKQQMEEEKKKLhATMHEALSKqKEAEKEMLSKQKEMQELEKKRLEQEIILADENQKLREKLQQLEE 3428
Cdd:TIGR00606 456 LKFVI-------KELQQLEGSSDRI-LELDQELRK-AERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQ 526
|
330 340
....*....|....*....|....*..
gi 1678729579 3429 AQKEQHTVPDKELICVTTVDTTKKVYN 3455
Cdd:TIGR00606 527 LNHHTTTRTQMEMLTKDKMDKDEQIRK 553
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2305-2625 |
3.15e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2305 AESELKQLRERAAEAERLRKVAQEEAE-KLHKQVIEETQkkriaekelqhkseaEKEAAKQKQKAldDLENLKKQAEEAE 2383
Cdd:PRK11281 31 SNGDLPTEADVQAQLDALNKQKLLEAEdKLVQQDLEQTL---------------ALLDKIDRQKE--ETEQLKQQLAQAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2384 RQVKQAEVEKERQIKVAHVAAQKSAA----AELQskhssfvektSKLEESLKQehgavLQLQQEAahLKKQQEDAINAR- 2458
Cdd:PRK11281 94 AKLRQAQAELEALKDDNDEETRETLStlslRQLE----------SRLAQTLDQ-----LQNAQND--LAEYNSQLVSLQt 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2459 --EEAEKELEkwrqkANEAlrlRLQAEEeahkKSLAQEDAEKQKEEAEReaKKRAKAEESALkqkdMAEKELERQRKVAD 2536
Cdd:PRK11281 157 qpERAQAALY-----ANSQ---RLQQIR----NLLKGGKVGGKALRPSQ--RVLLQAEQALL----NAQNDLQRKSLEGN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2537 STAQQKLTAEQELIRLRAdfDNAEQQRSLLEDELYRlKNeVIAAQQQRKQLEDELAKVRSEMDILIQlkskaeKETMSNT 2616
Cdd:PRK11281 219 TQLQDLLQKQRDYLTARI--QRLEHQLQLLQEAINS-KR-LTLSEKTVQEAQSQDEAARIQANPLVA------QELEINL 288
|
....*....
gi 1678729579 2617 EKSKQLLEA 2625
Cdd:PRK11281 289 QLSQRLLKA 297
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
2308-2396 |
3.26e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 43.05 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2308 ELKQLRERAAEAERLRkvAQEEAEKLhKQVIEETQKKRIAEKELQHK-SEAEKEAAKQKQKALDDLE--NLKKQAEEAER 2384
Cdd:cd03406 183 QHQKVVEKEAETERKR--AVIEAEKD-AEVAKIQMQQKIMEKEAEKKiSEIEDEMHLAREKARADAEyyRALREAEANKL 259
|
90
....*....|..
gi 1678729579 2385 QVKQAEVEKERQ 2396
Cdd:cd03406 260 KLTPEYLELKKY 271
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
2440-2598 |
3.28e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2440 LQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEAL--RLRLQA------EEEAHKKSLAQE----------------- 2494
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATlaRVDLEAkieslkEELAFLKKNHEEevrelqaqvsdtqvnve 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2495 -DAEKQKEEAEREAKKRAKAEESALKQKDMAEK----ELERQRKVADSTAQQKLTAEQELI-------RLRADFDNAEQQ 2562
Cdd:pfam00038 160 mDAARKLDLTSALAEIRAQYEEIAAKNREEAEEwyqsKLEELQQAAARNGDALRSAKEEITelrrtiqSLEIELQSLKKQ 239
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1678729579 2563 RSLLEDELY----RLKNEVIAAQQQRKQLEDELAKVRSEM 2598
Cdd:pfam00038 240 KASLERQLAeteeRYELQLADYQELISELEAELQETRQEM 279
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
2435-2524 |
3.42e-03 |
|
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex
Pssm-ID: 339878 [Multi-domain] Cd Length: 104 Bit Score: 40.11 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2435 GAVLQLQQEAAHLKKQQEdaiNAREEAEKELEKWRQKANealrlRLQAEEEAHKKSLAQEDAEKQKEEAER---EAKKRA 2511
Cdd:pfam16999 5 RLLSELAEREAALDQQIE---AARKEAEREVEAAEAEAA-----RILREAEAKAKALQAEYRQELAAETARireEARARA 76
|
90
....*....|...
gi 1678729579 2512 KAEESALKQKDMA 2524
Cdd:pfam16999 77 EAEAQAVRTRAEG 89
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2574-2974 |
3.50e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 43.86 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2574 KNEVIAAQQQRKQLEDELAKVRSEMdiliqlkskaeketmsnTEKSKQLLEAEATKMRdVAEEAGKLRAIAEEAKH--QR 2651
Cdd:pfam05701 27 KAHRIQTVERRKLVELELEKVQEEI-----------------PEYKKQSEAAEAAKAQ-VLEELESTKRLIEELKLnlER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2652 QVAEEEAARQRAE-AERILKE--KLAAISEATHLKTEAEIA----------LKEKEAENERLRR-----AAEDEAYQRKA 2713
Cdd:pfam05701 89 AQTEEAQAKQDSElAKLRVEEmeQGIADEASVAAKAQLEVAkarhaaavaeLKSVKEELESLRKeyaslVSERDIAIKRA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2714 leDEANQHKKEIEE-------KIVQLKKSSDA------EMERQK---AMV--DDTLKQRR---VVEEEIRilKLNFEKAS 2772
Cdd:pfam05701 169 --EEAVSASKEIEKtveeltiELIATKESLESahaahlEAEEHRigaALAreQDKLNWEKelkQAEEELQ--RLNQQLLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2773 SGKLDLELELNKLKniaeetqQSKLRAEEEAEKLRKLaleeeKRRREAEEKVKKITAAEEEAARQrkiAQDELERLKKKA 2852
Cdd:pfam05701 245 AKDLKSKLETASAL-------LLDLKAELAAYMESKL-----KEEADGEGNEKKTSTSIQAALAS---AKKELEEVKANI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2853 EEARkqkdeadveAEVQIVAAQQAALKCSTAEHQVQSVLAQQKED--SIMHKKLKQEYEKAKKLAKEAEAAKEKAEREA- 2929
Cdd:pfam05701 310 EKAK---------DEVNCLRVAAASLRSELEKEKAELASLRQREGmaSIAVSSLEAELNRTKSEIALVQAKEKEAREKMv 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 2930 ---ALLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRK-----EAEFEAAKR 2974
Cdd:pfam05701 381 elpKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAaastvESRLEAVLK 433
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
2621-3185 |
3.58e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 44.08 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2621 QLLEAeatkmRDVAEEAGKLRAIA---EEAKHQRQVAE--EEAARQ------RAEAERILKEKLAAISEATHLKTEAEIA 2689
Cdd:COG3899 674 RALEA-----RGPEPLEERLFELAhhlNRAGERDRAARllLRAARRalargaYAEALRYLERALELLPPDPEEEYRLALL 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2690 LKEKEAENERLRRAAEDEAYQRkALEDEANQHkkEIEEKIVQLKKSSDAEMERQKAMVDDTLKQRRVVEEEIRIL-KLNF 2768
Cdd:COG3899 749 LELAEALYLAGRFEEAEALLER-ALAARALAA--LAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAeRLGD 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2769 EKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKL--RKLALEEEKRRREAEEKVKKITAAEEEAARQRKIAQDELE 2846
Cdd:COG3899 826 RRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALA 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2847 RLKKKAEEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKEDSIMHKKLKQEYEKAKKLAKEAEAAKEKAE 2926
Cdd:COG3899 906 AAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAA 985
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2927 REAALLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQAEGAALKQKQQADAEMAKHKKLAEQTLKQk 3006
Cdd:COG3899 986 AAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAA- 1064
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3007 FQVEQELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLLKKDKDN 3086
Cdd:COG3899 1065 AAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALAL 1144
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3087 SQKFLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQE 3166
Cdd:COG3899 1145 ALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLL 1224
|
570
....*....|....*....
gi 1678729579 3167 QAQKLLEDKQLMQRRLEEE 3185
Cdd:COG3899 1225 LLLLAALALAAALLALRLL 1243
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
867-971 |
3.60e-03 |
|
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: 40.48 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 867 VQKKTFTKWVNKHLIKraeSQHHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRF----HKLQNVQIALDFLRHRQV 942
Cdd:cd21306 16 VVKKSLITFVNKHLNK---LNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGL 92
|
90 100
....*....|....*....|....*....
gi 1678729579 943 KLVNIRNDDIADGNPKLTLGLIWTVILHF 971
Cdd:cd21306 93 PKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3066-3238 |
3.84e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3066 LKLKLRIEDENQRLLKKDKDNSQKFLAEEAENMKRLAEDAARLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQ 3145
Cdd:PRK00409 497 LGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3146 ES-SRLKAEAEMLQRQKDLAQEQAQKLLEDKQL--MQRRLEEETEEYQKSLEAERRRQ--------------------LE 3202
Cdd:PRK00409 577 QAiKEAKKEADEIIKELRQLQKGGYASVKAHELieARKRLNKANEKKEKKKKKQKEKQeelkvgdevkylslgqkgevLS 656
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1678729579 3203 IVAEAE--------KLKLQVSQLSEAQTKAEEEAKKFKKQADKI 3238
Cdd:PRK00409 657 IPDDKEaivqagimKMKVPLSDLEKIQKPKKKKKKKPKTVKPKP 700
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2326-2554 |
3.91e-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: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2326 AQEEAEKLHKQVIEEtqkkriAEKELQhksEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAevekerqiKVAHVAAQ 2405
Cdd:pfam04012 19 KAEDPEKMLEQAIRD------MQSELV---KARQALAQTIARQKQLERRLEQQTEQAKKLEEKA--------QAALTKGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2406 KSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAinareEAEKELEKWRQKANEAlrlrlQAEEE 2485
Cdd:pfam04012 82 EELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQL-----KAKKNLLKARLKAAKA-----QEAVQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 2486 AHKKSLAQEDAEKQKEE-----AEREAKKRAKAEesalkqkdmAEKELERQRKVADSTAQQKLTaEQELIRLRA 2554
Cdd:pfam04012 152 TSLGSLSTSSATDSFERieekiEEREARADAAAE---------LASAVDLDAKLEQAGIQMEVS-EDVLARLKA 215
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5105-5136 |
4.02e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.08 E-value: 4.02e-03
10 20 30
....*....|....*....|....*....|..
gi 1678729579 5105 IAGILDIDTLEKVSITEAIHRNLVDNITGQRL 5136
Cdd:pfam00681 8 TGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3136-3302 |
4.07e-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: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3136 MLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVS 3215
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3216 QLSEAQTkaEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKE----AGDLRDAIADLEKDKARLKKEA 3291
Cdd:COG1579 81 QLGNVRN--NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAElaelEAELEEKKAELDEELAELEAEL 158
|
170
....*....|.
gi 1678729579 3292 EELQNKSKEMA 3302
Cdd:COG1579 159 EELEAEREELA 169
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2824-3000 |
4.10e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2824 VKKITaaeeEAARQRKIAQDELERLKKKA-EEARKQKDEADVEAEVQIVAAQQAAlkcSTAEhqvqsvLAQQKEDsimhK 2902
Cdd:COG2268 191 RRKIA----EIIRDARIAEAEAERETEIAiAQANREAEEAELEQEREIETARIAE---AEAE------LAKKKAE----E 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2903 KLKQEyekakklakeaeAAKEKAEREAALLRQQAEEAERQKAAAEQEAAIQAKAQEDAERLRKEAEFEAAKRAQAEGAAL 2982
Cdd:COG2268 254 RREAE------------TARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAA 321
|
170
....*....|....*...
gi 1678729579 2983 KQKQQADAEMAKHKKLAE 3000
Cdd:COG2268 322 EAEAEAEAEAIRAKGLAE 339
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
2453-2553 |
4.12e-03 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 42.90 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2453 DAINAREEAEkelekwRQKanEALRLRLQAEEEAhKKSLAQEDAEKQKEEAEreakkrAKAEESALKqkdmAEKELERQR 2532
Cdd:COG0330 171 DAMEDRMKAE------RER--EAAILEAEGYREA-AIIRAEGEAQRAIIEAE------AYREAQILR----AEGEAEAFR 231
|
90 100
....*....|....*....|.
gi 1678729579 2533 KVADStaqqkLTAEQELIRLR 2553
Cdd:COG0330 232 IVAEA-----YSAAPFVLFYR 247
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4177-4215 |
4.18e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 37.69 E-value: 4.18e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1678729579 4177 YLQGSDSIAGIYLEPTKEKISIYQAMKKKLLRQNTGISL 4215
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3081-3265 |
4.26e-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: 42.91 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3081 KKDKDNSQKFLAEEAENMKrlaedaARLSVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQ 3160
Cdd:TIGR02794 63 AKKEQERQKKLEQQAEEAE------KQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3161 KDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKlklqvsqlsEAQTKAEEEAKK---FKKQADK 3237
Cdd:TIGR02794 137 EAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEA---------EAKAKAEEAKAKaeaAKAKAAA 207
|
170 180
....*....|....*....|....*...
gi 1678729579 3238 IAARLHETEIATKEKMTVVEKLEFERLN 3265
Cdd:TIGR02794 208 EAAAKAEAEAAAAAAAEAERKADEAELG 235
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2439-2527 |
4.26e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2439 QLQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEE-----EAHKKSLAQEDAEKQKEEAEreakKRAKA 2513
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEkqqelEAQLEQLQEKAAETSQERKQ----KRKEI 221
|
90
....*....|....
gi 1678729579 2514 EESALKQKDMAEKE 2527
Cdd:PRK11448 222 TDQAAKRLELSEEE 235
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4293-4326 |
4.38e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 4.38e-03
10 20 30
....*....|....*....|....*....|....
gi 1678729579 4293 EAQMVSGGIIDPVNSHRVPIDVAYQKNIFSKEIA 4326
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
2294-2569 |
4.45e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.83 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2294 QLETTVKqkstaeselKQLRERAAEA----ERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKE-------AA 2362
Cdd:TIGR00927 607 QIELWVK---------EQLSRRPVAKvmalGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEqegetetKG 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2363 KQKQKALDDLENLKKQAEEAERQVKQAEVEKERQikvahvaaqksaAAELQSKHSSFVEKTSKLEESLKQEHGAVlqlqq 2442
Cdd:TIGR00927 678 ENESEGEIPAERKGEQEGEGEIEAKEADHKGETE------------AEEVEHEGETEAEGTEDEGEIETGEEGEE----- 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2443 eaahlkKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSL-AQEDAEKQKEEAEREAKKRAKAEESALKQK 2521
Cdd:TIGR00927 741 ------VEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIqAGEDGEMKGDEGAEGKVEHEGETEAGEKDE 814
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1678729579 2522 DMAEKElerqrKVADSTAQQKLTAEQELirlradfdNAEQQRSLLEDE 2569
Cdd:TIGR00927 815 HEGQSE-----TQADDTEVKDETGEQEL--------NAENQGEAKQDE 849
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
983-1085 |
4.48e-03 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 40.17 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 983 EDMSAKEKLLlwSQRMTGDYQN----IRCDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSN-LENLEQAFNVAERDL 1057
Cdd:cd21312 4 EDEEAKKQTP--KQRLLGWIQNklpqLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKpVTNAREAMQQADDWL 81
|
90 100
....*....|....*....|....*...
gi 1678729579 1058 GVTRLLDPEDVDVQHPDEKSIITYVSSL 1085
Cdd:cd21312 82 GIPQVITPEEIVDPNVDEHSVMTYLSQF 109
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
3089-3440 |
4.48e-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: 43.79 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3089 KFLAEEAENMkrLAEDAARlsvesqEAARLRQIAEDDLIQQRALAD--KMLKEKMQAIQESSRlkaEAEMLQ-RQKDLAQ 3165
Cdd:COG3096 259 KHLITEATNY--VAADYMR------HANERRELSERALELRRELFGarRQLAEEQYRLVEMAR---ELEELSaRESDLEQ 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3166 EQaQKLLEDKQLMQR--RLEEETEEYQKSLEA--ER-RRQLEIVAEAEKlklQVSQLSEAQTKAEEEAKKFKKQ-ADKIA 3239
Cdd:COG3096 328 DY-QAASDHLNLVQTalRQQEKIERYQEDLEEltERlEEQEEVVEEAAE---QLAEAEARLEAAEEEVDSLKSQlADYQQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3240 A--RLHETEIATKEKMTVVEKleferlntSKEAGDLRD-AIADLEKDKARLKKEAEE-----LQNKSK-EMADAQQKQIE 3310
Cdd:COG3096 404 AldVQQTRAIQYQQAVQALEK--------ARALCGLPDlTPENAEDYLAAFRAKEQQateevLELEQKlSVADAARRQFE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3311 HEKTLLQQ-TFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQKQQmeEEKKKLHATMHEALSKQKEAEk 3389
Cdd:COG3096 476 KAYELVCKiAGEVERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQ--QNAERLLEEFCQRIGQQLDAA- 552
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 3390 EMLSKQKEMQELEKKRLEQEiiLADENQKLREKLQQLEEAQKEQHTVPDKE 3440
Cdd:COG3096 553 EELEELLAELEAQLEELEEQ--AAEAVEQRSELRQQLEQLRARIKELAARA 601
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3022-3209 |
4.49e-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: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3022 DTDKQKSLLDdeLQRLKDEVDDAVKQRGQVEEELfkvKVQMEELLKLKLRIEDENQRLLKKDKDNSQKfLAEEAENMKRL 3101
Cdd:COG1579 2 MPEDLRALLD--LQELDSELDRLEHRLKELPAEL---AELEDELAALEARLEAAKTELEDLEKEIKRL-ELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3102 AEDAARL-SVESQEAARLRQIAEDDLIQQRALADKMLKEKMQAIQEssrlkAEAEMLQRQKDLAQEQAQklLEDKqlmQR 3180
Cdd:COG1579 76 KKYEEQLgNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEE-----LEEELAELEAELAELEAE--LEEK---KA 145
|
170 180
....*....|....*....|....*....
gi 1678729579 3181 RLEEETEEYQKSLEAERRRQLEIVAEAEK 3209
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
3122-3439 |
4.55e-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: 43.14 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3122 AEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQKLledkqlmqRRLEEETEEYQKSLE--AERRR 3199
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKV--------KKLEATVETYKKKLEdlGDLRR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3200 QLEIVAEAEKLKLQVSQLSEaqtkaeEEAKKF---KKQADKIAARLHETEIATKEKMTVVEKLEFERLNtskeagdLRDA 3276
Cdd:pfam05622 153 QVKLLEERNAEYMQRTLQLE------EELKKAnalRGQLETYKRQVQELHGKLSEESKKADKLEFEYKK-------LEEK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3277 IADLEKDKARLKKEAEELQNKSKEMADAQQKQieheKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALK 3356
Cdd:pfam05622 220 LEALQKEKERLIIERDTLRETNEELRCAQLQQ----AELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3357 DEQERQKQQMEEEkkklhatmhealskqkeaekemLSKQKEMQELEKKRLEQEIILAdeNQKLREKLQQLEEAQKEQHTV 3436
Cdd:pfam05622 296 LGQEGSYRERLTE----------------------LQQLLEDANRRKNELETQNRLA--NQRILELQQQVEELQKALQEQ 351
|
...
gi 1678729579 3437 PDK 3439
Cdd:pfam05622 352 GSK 354
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2296-2689 |
4.56e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2296 ETTVKQKSTAESELKQLRERAAEAERLRKVAQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENL 2375
Cdd:COG3064 30 EAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2376 KKQAEEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAI 2455
Cdd:COG3064 110 AEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2456 NAREEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMAEKELERQRKVA 2535
Cdd:COG3064 190 VEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2536 DSTAQQKLTAEQELIRLRADFDNAEQQRsllEDELYRLKNEVIAAQQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSN 2615
Cdd:COG3064 270 GAAALSSGLVVVAAALAGLAAAAAGLVL---DDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAA 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 2616 TEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIA 2689
Cdd:COG3064 347 GAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVEL 420
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
992-1085 |
4.60e-03 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 39.59 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 992 LLWSQRMTGDyQNIrcDNFSTSWRDGKLFNAVIHKHHPRLIDMGKVYRQSNLENLEQAFNVAERdLGVTRLLDPEDVDVQ 1071
Cdd:cd21185 7 LRWVRQLLPD-VDV--NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADP 82
|
90
....*....|....
gi 1678729579 1072 HPDEKSIITYVSSL 1085
Cdd:cd21185 83 EVEHLGIMAYAAQL 96
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2695-2807 |
4.63e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2695 AENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAMVDDTLKQ-RRVVEEEIRILK-LNFEKAS 2772
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEaKKEADEIIKELRqLQKGGYA 602
|
90 100 110
....*....|....*....|....*....|....*.
gi 1678729579 2773 SGKL-DLELELNKLKNIAEETQQSKLRAEEEAEKLR 2807
Cdd:PRK00409 603 SVKAhELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
2560-2712 |
5.09e-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: 40.80 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2560 EQQRSLLEDELYRLKNEVIaaqqqRKQLEDELAKVRSEMDILIQLKSKAEKETMsntekskqlleaeatkMRDVAEEAGK 2639
Cdd:pfam15346 2 EAESKLLEEETARRVEEAV-----AKRVEEELEKRKDEIEAEVERRVEEARKIM----------------EKQVLEELER 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678729579 2640 LRAIAEEAKHQRqvaEEEAARQRAEAERILKEKLAAISEATHLKTEAEIALKEKE--AENERLRRAAEDEAYQRK 2712
Cdd:pfam15346 61 EREAELEEERRK---EEEERKKREELERILEENNRKIEEAQRKEAEERLAMLEEQrrMKEERQRREKEEEEREKR 132
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
3149-3432 |
5.24e-03 |
|
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: 43.17 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3149 RLKAEAEMlqRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEA 3228
Cdd:pfam05483 94 KVSIEAEL--KQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3229 KKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAG-DLRDaiaDLEKDKARLKKEAEELQNKSKEMADAQQK 3307
Cdd:pfam05483 172 KKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKE---DHEKIQHLEEEYKKEINDKEKQVSLLLIQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3308 QIEHEKTLLQQTFLTEREmllkkeklieeekKKLESQFEEEAK-KSKALKDEQERQkQQMEEEKKKLHATMHEALSKQKE 3386
Cdd:pfam05483 249 ITEKENKMKDLTFLLEES-------------RDKANQLEEKTKlQDENLKELIEKK-DHLTKELEDIKMSLQRSMSTQKA 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 3387 AEKEM---------LSKQKE--MQELEKKRLEQEIILAD-------ENQKLREKLQQLEEAQKE 3432
Cdd:pfam05483 315 LEEDLqiatkticqLTEEKEaqMEELNKAKAAHSFVVTEfeattcsLEELLRTEQQRLEKNEDQ 378
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
3346-3427 |
5.37e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.66 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3346 EEEAKKSKALKDEQERQKQQMEEEKKKLHATmHEALSKQK-EAEKEMLSKQKEMQeLEKKRLEQEIIL----ADENQKLR 3420
Cdd:pfam02841 213 AEAAEAEQELLREKQKEEEQMMEAQERSYQE-HVKQLIEKmEAEREQLLAEQERM-LEHKLQEQEELLkegfKTEAESLQ 290
|
....*..
gi 1678729579 3421 EKLQQLE 3427
Cdd:pfam02841 291 KEIQDLK 297
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3885-3917 |
5.55e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 5.55e-03
10 20 30
....*....|....*....|....*....|...
gi 1678729579 3885 LEAQAGTGYVVDPIHDQKYTVDEAVKAGVVGPE 3917
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
3158-3442 |
5.66e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3158 QRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQ-LEIVAEAeklklqVSQLSEAQTKAEEeakkfkKQAD 3236
Cdd:PRK05035 441 IEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAKdKDAVAAA------LARVKAKKAAATQ------PIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3237 KIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDAI--ADLEKDKARlKKEAEELQNKSKEMADAQQKQIEHEKT 3314
Cdd:PRK05035 509 KAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAvaAAIARAKAK-KAAQQAANAEAEEEVDPKKAAVAAAIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3315 LLQqtflteremllkkeklieeekkklesqfeeeAKKSKALKDEQERQKQQMEEEKKKLHATMHEALSKQKEAEKEMLSK 3394
Cdd:PRK05035 588 RAK-------------------------------AKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAE 636
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1678729579 3395 QKEMQELEKKRLEQEIILAdenqKLREKLQQLEEAQKEQHTVPDKELI 3442
Cdd:PRK05035 637 PEEPVDPRKAAVAAAIARA----KARKAAQQQANAEPEEAEDPKKAAV 680
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
3062-3436 |
5.85e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3062 MEELLKlKLRIEDENQRLLKKDKDNSqKFLAEEAENMkrLAEDAARlsvesqEAARLRQIAEDDLIQQRALADKmlKEKM 3141
Cdd:PRK04863 235 MEAALR-ENRMTLEAIRVTQSDRDLF-KHLITESTNY--VAADYMR------HANERRVHLEEALELRRELYTS--RRQL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3142 QAIQES-SRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQ--RRLEEETEEYQKSLEAERRR---QLEIVAEAEKlklQVS 3215
Cdd:PRK04863 303 AAEQYRlVEMARELAELNEAESDLEQDYQAASDHLNLVQtaLRQQEKIERYQADLEELEERleeQNEVVEEADE---QQE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3216 QLSEAQTKAEEEAKKFKKQ-ADkiaarlheteiatkekmtVVEKLEFERlntsKEAGDLRDAIADLEKDKARLKKEAEEL 3294
Cdd:PRK04863 380 ENEARAEAAEEEVDELKSQlAD------------------YQQALDVQQ----TRAIQYQQAVQALERAKQLCGLPDLTA 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3295 QNKSKEMADAQQKqiehEKTLLQQTFLTEREMLLKKEKLieeekkkleSQFEEEAKKSKALKDEQERQ--KQQMEE---- 3368
Cdd:PRK04863 438 DNAEDWLEEFQAK----EQEATEELLSLEQKLSVAQAAH---------SQFEQAYQLVRKIAGEVSRSeaWDVAREllrr 504
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 3369 -EKKKLHATMHEAL-SKQKEAEKEmLSKQKEMQELEK---KRLEQEIILADENQKLREKL-QQLEEAQKEQHTV 3436
Cdd:PRK04863 505 lREQRHLAEQLQQLrMRLSELEQR-LRQQQRAERLLAefcKRLGKNLDDEDELEQLQEELeARLESLSESVSEA 577
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2581-2871 |
6.26e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2581 QQQRKQLEDELAKVRSEMDILIQLKSKAEKETMSNTEKSKQLLEaeatKMRDVAEEAGKLRAIAEEAKHQRQVAEEEAar 2660
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELRE----EAQELREKRDELNEKVKELKEERDELNEKL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2661 qraeaeRILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAaedeaYQRKALEDEanqHKKEIEEKIVQLKKssdaEM 2740
Cdd:COG1340 88 ------NELREELDELRKELAELNKAGGSIDKLRKEIERLEWR-----QQTEVLSPE---EEKELVEKIKELEK----EL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2741 ERQKAMVDDTlKQRRVVEEEIRILKLNFEKASsgkldlelelNKLKNIAEETQQSKLR---AEEEAEKLRKLALEEEKRR 2817
Cdd:COG1340 150 EKAKKALEKN-EKLKELRAELKELRKEAEEIH----------KKIKELAEEAQELHEEmieLYKEADELRKEADELHKEI 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 2818 REAEEKVKKITAAEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEAEVQIV 2871
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2483-2704 |
6.61e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 42.66 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2483 EEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESALKQKDMA-EKELERQRKVADSTAQQKLTAEQELIRLRADFDNAEQ 2561
Cdd:PRK07735 2 DPEKDLEDLKKEAARRAKEEARKRLVAKHGAEISKLEEENREkEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2562 QRSLLEDELYRLKNEVIAAQQQRKQledELAKVRSEmdiliQLKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLR 2641
Cdd:PRK07735 82 TEEVTEEEKAKAKAKAAAAAKAKAA---ALAKQKRE-----GTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 2642 AIAEEAKHQRQVAEEEAARQRAEAERILKEKLAAISEATHLKTEAEIAL-KEKEAENERLRRAA 2704
Cdd:PRK07735 154 TEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKaKAKAAAAAKAKAAA 217
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2158-2436 |
6.87e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 43.28 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2158 SELMTLTSQYIKFITE---TQRRLEDEEKA---AKKLKAEEQKKMAEM---QAELDKQKQLAAahakaiakaekeaqelk 2228
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERAeadRQRLEQEKQQQLAAIsgsQSQLESTDQNAL----------------- 1600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2229 lmmkEEVNRREIAAVDAEKQKQNiqlelHELKNLSE--QQIKDKGQLVDEALQSRTKIEEEIYLIRIQ--LETTVKQKST 2304
Cdd:NF012221 1601 ----ETNGQAQRDAILEESRAVT-----KELTTLAQglDALDSQATYAGESGDQWRNPFAGGLLDRVQeqLDDAKKISGK 1671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2305 AESELKQlreraAEAERLRKVaQEEAEKLHKQVIEETQKKRIAEKELQhksEAEKEAAKQKQKALDDLENLKKQAEEAER 2384
Cdd:NF012221 1672 QLADAKQ-----RHVDNQQKV-KDAVAKSEAGVAQGEQNQANAEQDID---DAKADAEKRKDDALAKQNEAQQAESDANA 1742
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 2385 QVKQAEVEKERQIKVAhvaaqKSAAAELQSKhssfvEKTSKLEESLKQE-HGA 2436
Cdd:NF012221 1743 AANDAQSRGEQDASAA-----ENKANQAQAD-----AKGAKQDESDKPNrQGA 1785
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3037-3294 |
6.92e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3037 LKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRllkkdkdnSQKFLAEEAENMKRLAEDAARLSVESQEAA 3116
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ--------ARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3117 RLRQIAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAE 3196
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3197 RRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFERLNTSKEAGDLRDA 3276
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250
....*....|....*...
gi 1678729579 3277 IADLEKDKARLKKEAEEL 3294
Cdd:COG4372 261 EELELAILVEKDTEEEEL 278
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
3142-3263 |
7.01e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3142 QAIQES-SRLKAEAEMLQRQKDL---AQEQAQKLLEDKQLMQRRLEEETEEYQK---SLEAERRRQLEIVAEaekLKLQV 3214
Cdd:PRK11637 166 QARQETiAELKQTREELAAQKAEleeKQSQQKTLLYEQQAQQQKLEQARNERKKtltGLESSLQKDQQQLSE---LRANE 242
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1678729579 3215 SQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEKMTVVEKLEFER 3263
Cdd:PRK11637 243 SRLRDSIARAEREAKARAEREAREAARVRDKQKQAKRKGSTYKPTESER 291
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
868-977 |
7.18e-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: 39.43 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 868 QKKTFTKWVNKHLIKRAESQH------HVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMR-----FHKLQNVQIALDF 936
Cdd:cd21293 2 EKGSYVDHINRYLGDDPFLKQflpidpSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1678729579 937 LRHRQVKLVNIRNDDIADGNPKLTLGLIwtvilhFQISDIQ 977
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLI------SQIIKIQ 116
|
|
| vATP-synt_E |
pfam01991 |
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ... |
2481-2574 |
7.24e-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: 41.21 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2481 QAEEEAHK-KSLAQEDAEKQKEEAEREAKKRAKaeesalKQKDMAEKELERQRKVADSTAqqKLTAEQELIRLRAD---- 2555
Cdd:pfam01991 5 EAEEKAEEiRAKAEEEFAIEKAELVQEAEEKID------EIYEKKEKQAEMQKKIIISNA--KNEARLKVLEAREEilde 76
|
90 100
....*....|....*....|
gi 1678729579 2556 -FDNAEQQRSLLEDELYRLK 2574
Cdd:pfam01991 77 vFNEAEKKLAELEEDTDEYK 96
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
2458-2597 |
7.45e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 41.08 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2458 REEAEKELEKWRQKA-NEALRLRLQAEEEAHKKslaqedAEKQKEEAEREAKKRAKAEESALKQKdMAEKELERQRKVAD 2536
Cdd:COG1390 12 LEEAEAEAEEILEEAeEEAEKILEEAEEEAEEI------KEEILEKAEREAEREKRRIISSAELE-ARKELLEAKEELIE 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 2537 STAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKN---EVIAAQQQRKQLEDELAKVRSE 2597
Cdd:COG1390 85 EVFEE---ALEKLKNLPKDPEYKELLKKLLKEAAEELGSgdlVVYVNEKDKELLEELLKELKKK 145
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
3003-3433 |
7.50e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3003 LKQKFQVEQ-ELTKVKLKLDDTDKQKSLLDDELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKLRIEDENQRLLK 3081
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3082 KDKDNSQkfLAEEAENMKRLAEDAArlsVESQEAARLRQIAEDDLIQQRaladKMLKEKMQAIQESSRLKAEAEMLQRQK 3161
Cdd:PRK01156 268 ELEKNNY--YKELEERHMKIINDPV---YKNRNYINDYFKYKNDIENKK----QILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3162 DlAQEQAQKLLEDKQLMQRRLEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAAR 3241
Cdd:PRK01156 339 N-DYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3242 LHE--TEIAT--KEKMTVVEKLEFERLNTSKEAG--------------DLRDAIADLEKDKARLKKEAEELQNKSKEMAD 3303
Cdd:PRK01156 418 LQDisSKVSSlnQRIRALRENLDELSRNMEMLNGqsvcpvcgttlgeeKSNHIINHYNEKKSRLEEKIREIEIEVKDIDE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3304 AQQKQI---------EHEKTLLQQTFLTEREMLLKKEKLIEEEKKKLESQFEEEAKKSKALKDEQERQK----------- 3363
Cdd:PRK01156 498 KIVDLKkrkeyleseEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKrtswlnalavi 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3364 ---------QQMEEEKKKLH---ATMHEALSKQKEAEKEMLSKQKEMQElEKKRLEQEIILADENQKLREKLQQLEEAQK 3431
Cdd:PRK01156 578 slidietnrSRSNEIKKQLNdleSRLQEIEIGFPDDKSYIDKSIREIEN-EANNLNNKYNEIQENKILIEKLRGKIDNYK 656
|
..
gi 1678729579 3432 EQ 3433
Cdd:PRK01156 657 KQ 658
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
3182-3428 |
7.58e-03 |
|
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: 41.86 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3182 LEEETEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAARLHETEIATKEK-MTVVEKLE 3260
Cdd:pfam09728 30 LLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNKKLKEESKKLAKEEEEKrKELSEKFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3261 fERLNtskeagDLRDAIADLEKDKARLKKEAEELQNKSKEMADAQQKQIEHEKTLLQQTfltEREMLLKKEKLIEEEKKK 3340
Cdd:pfam09728 110 -STLK------DIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLLKTK---ELEVQLAEAKLQQATEEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3341 LESQFEEEAKKSKALKDEQERQKQQmeEEKKKLHATMHEAlsKQKEAE--------------KEMLSKQKEMQELEKKRL 3406
Cdd:pfam09728 180 EKKAQEKEVAKARELKAQVQTLSET--EKELREQLNLYVE--KFEEFQdtlnksnevfttfkKEMEKMSKKIKKLEKENL 255
|
250 260 270
....*....|....*....|....*....|..
gi 1678729579 3407 EQE----------IILADENQKLREKLQQLEE 3428
Cdd:pfam09728 256 TWKrkweksnkalLEMAEERQKLKEELEKLQK 287
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2669-2860 |
8.29e-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: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2669 LKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQKAmvd 2748
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2749 dtlKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKlaleeekrrrEAEEKVKKIT 2828
Cdd:COG1579 89 ---KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA----------ELDEELAELE 155
|
170 180 190
....*....|....*....|....*....|...
gi 1678729579 2829 AAEEEAARQRKIAQDEL-ERLKKKAEEARKQKD 2860
Cdd:COG1579 156 AELEELEAEREELAAKIpPELLALYERIRKRKN 188
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2440-2570 |
8.42e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.54 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2440 LQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRlrlQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEESAlk 2519
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQ---NYERELVLHAEDIKALQALREELNELKAEIAELKAEA-- 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1678729579 2520 qkDMAEKELERQRKvadSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDEL 2570
Cdd:pfam07926 81 --ESAKAELEESEE---SWEEQKKELEKELSELEKRIEDLNEQNKLLHDQL 126
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2691-2886 |
8.52e-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: 42.14 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2691 KEKEAENERLRRAAEDEAyqrkaleDEANQHKKEIEEKIVQLKKSSDAEMERQKAmvddtLKQRRVVEEEIRilklNFEK 2770
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAA-------KKEQERQKKLEQQAEEAEKQRAAEQARQKE-----LEQRAAAEKAAK----QAEQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2771 ASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEAARQRKIAQDELERLKK 2850
Cdd:TIGR02794 110 AAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKA 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 1678729579 2851 KAEEARKQKDEADVEAEVQIVA-AQQAALKCSTAEHQ 2886
Cdd:TIGR02794 190 KAEEAKAKAEAAKAKAAAEAAAkAEAEAAAAAAAEAE 226
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
2274-2413 |
8.81e-03 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 41.75 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2274 VDEALQSRTKIEEEIYLIRIQLETTVKQkSTAESELKQL--RERAAEAERLRKVAQEEAEKLH--------------KQV 2337
Cdd:COG0330 91 ITDPAKFLYNVENAEEALRQLAESALRE-VIGKMTLDEVlsTGRDEINAEIREELQEALDPYGievvdveikdidppEEV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2338 IEETQKKRIAEKE---LQHKSEAEKEAAKQKQKAlddlenlkkqaeEAERQVKQAEVEKERQIKVAH--VAAQKSAAAEL 2412
Cdd:COG0330 170 QDAMEDRMKAEREreaAILEAEGYREAAIIRAEG------------EAQRAIIEAEAYREAQILRAEgeAEAFRIVAEAY 237
|
.
gi 1678729579 2413 Q 2413
Cdd:COG0330 238 S 238
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2245-2415 |
9.09e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2245 AEKQKQNIQLELHELKNLSEQQIKDKGqlvdEALQSRTKieeeiyLIRIQlettvkqkstAESELKQLRERA-AEAERLR 2323
Cdd:PTZ00491 666 AAARHQAELLEQEARGRLERQKMHDKA----KAEEQRTK------LLELQ----------AESAAVESSGQSrAEALAEA 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2324 KVAQEEAEKLHKQVIEETQKKRIaekelqhksEAEKEAAKQKQKALDDLENLKKQAE---EAERQVKQAEVEKERQIKVA 2400
Cdd:PTZ00491 726 EARLIEAEAEVEQAELRAKALRI---------EAEAELEKLRKRQELELEYEQAQNEleiAKAKELADIEATKFERIVEA 796
|
170
....*....|....*....
gi 1678729579 2401 ----HVAAQKSAAAELQSK 2415
Cdd:PTZ00491 797 lgreTLIAIARAGPELQAK 815
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2143-2515 |
9.28e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2143 SDNIIQEYVTLRTRYSELMTLTSQYIKFITETQRRLEDEEKAAKKLKAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEK 2222
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2223 EAQELklmmKEEVNRREIAAVDAEKQKQNIQLELHELKNLSEQQIKDKGQLVdealQSRTKIEEEIYLIRIQLETTVKQK 2302
Cdd:COG4372 81 ELEEL----NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE----QQRKQLEAQIAELQSEIAEREEEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2303 STAESELKQLRERAAEAERLRKV-----AQEEAEKLHKQVIEETQKKRIAEKELQHKSEAEKEAAKQKQKALDDLENLKK 2377
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQAlseaeAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2378 QAEEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSKHSSFVEKTSKLEESLKQEHGAVLQLQQEAAHLKKQQEDAINA 2457
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1678729579 2458 REEAEKELEKWRQKANEALRLRLQAEEEAHKKSLAQEDAEKQKEEAEREAKKRAKAEE 2515
Cdd:COG4372 313 LEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2505-2897 |
9.41e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.33 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2505 REAKKRAKAEESALKQKDMAEKElerQRKVADSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDElyrlkneviaAQQQR 2584
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAE---KRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAE----------AEQRA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2585 KQLEDELAKVRSEMDiliqlKSKAEKETMSNTEKSKQLLEAEATKMRDVAEEAGKLRAIAEEAKhqrqvAEEEAARQRAE 2664
Cdd:COG3064 69 AELAAEAAKKLAEAE-----KAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKR-----KAEEEAKRKAE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2665 AERILKEKLAAISEATHLKTEAEIALKEKEAENERLRRAAEDEAYQRKALEDEANQHKKEIEEKIVQLKKSSDAEMERQK 2744
Cdd:COG3064 139 EERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2745 AMVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRKLALEEEKRRREAEEKV 2824
Cdd:COG3064 219 LAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLD 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678729579 2825 KKITAAEEEAARQRKIAQDELERLKKKAEEARKQKDEADVEAEVQIVAAQQAALKCSTAEHQVQSVLAQQKED 2897
Cdd:COG3064 299 DSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEA 371
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3024-3240 |
9.48e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3024 DKQKSLLDDELQRLKDEvddavkqRGQVEEELFKVKVQMEELLklklriEDENQRLLKKDKDNSQKFLAEEAENMKRLAE 3103
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKE-------QQQAEELQQKQAAEQERLK------QLEKERLAAQEQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 3104 DAARlsvESQEAARLRqiAEDDLIQQRALADKMLKEKMQAIQESSRLKAEAEMlqrQKDLAQEQAQKLledkqlmqrrle 3183
Cdd:PRK09510 136 EAAA---KAAAAAKAK--AEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAEAAAKA------------ 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1678729579 3184 eeTEEYQKSLEAERRRQLEIVAEAEKLKLQVSQLSEAQTKAEEEAKKFKKQADKIAA 3240
Cdd:PRK09510 196 --AAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKA 250
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
2181-2646 |
9.48e-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: 42.54 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2181 EEKAAKKlkAEEQKKMAEMQAELDKQKQLAAAHAKAIAKAEKEAQElklmMKEEVNRREIaavdaekQKQNIQLELHELK 2260
Cdd:pfam09730 23 QESASKE--AYYAQRILELQNELKQARAVLSNTQAENERLASLSQE----LKEECECVEL-------QRGRMRDEIKEYK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2261 NLSEQQIKDKGQLVDE--ALQSRTKI--EEEIYLIRIQLETTVKqkstaESELKQLRERAAEAERLRKVAQEEAEKLHKQ 2336
Cdd:pfam09730 90 VREARLLQDYSELEEEniSLQKQVSVlkQNQVEFEGLKHEITRK-----EEETELLNSQLEEAIRLREIAERQLDEALET 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2337 VIEETQKKRIAEKELQHK-SEAEKEAAKQKQKALDDLENLKKQAEEAERQVKQAEVEKERQIKVAHVAAQKSAAAELQSK 2415
Cdd:pfam09730 165 LKTEREQKNSLRKELSHYmTLNDFDYVSHLSISLDGLKFSEDEGAGTEPNNDGEAMDGGENGGGGLKNSGLDNRTSTPRK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2416 HSSFVEKTSKLEESLKQEHGAVLQ-LQQEAAHLKKQQEDAINAREEAEKELEKWRQKANEALRLRLQAEEeaHKKSLAQE 2494
Cdd:pfam09730 245 SEVFPPAPSLVSDLLSELNISEIQkLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTE--NLEAMRGL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2495 DAEKQKEEAEREAKKRAKAEESALKQKDMAEKE-LERQRKVADSTAqqkLTAEQELIRLRADFDNAEQQrslLEDELYRL 2573
Cdd:pfam09730 323 QASKERQDALDSEKDRDSHEDGDYYEVDINGPEiLECKYRVAVEEA---GELREELKALKARYNTLEER---YKEEKTRW 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678729579 2574 KNEVIAAQQQRKQLEDelakvrsemdiliqlKSKAEKETMSNtekskqlLEAEATKMRDVAEEA-GKLRAIAEE 2646
Cdd:pfam09730 397 EAEAQDLAEKIRQLEK---------------ASHQDQERIAH-------LEKELGKTRKVAGESeGSLSVAQDE 448
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
2794-2889 |
9.49e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 41.70 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678729579 2794 QSKLRAEEEAEKLRKLALEEEKRRREAEEKVKKITAAEEEA-ARQRKIAQDELERLKKKAEEARKQ----KDEADVEAEV 2868
Cdd:PRK06991 163 QARLRREREAAEARAAARAAASAAAAAAEASAAAAPAADDAeAKKRAIIAAALERARKKKEELAAQgagpKNTEGVSAAV 242
|
90 100
....*....|....*....|...
gi 1678729579 2869 --QIVAAQQAALKCSTAEHQVQS 2889
Cdd:PRK06991 243 qaQIDAAEARRKRLAEQRDAPDD 265
|
|
| |
