|
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 ... |
1055-1159 |
3.33e-76 |
|
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: 248.86 E-value: 3.33e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1055 DRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNI 1134
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1988774674 1135 RNDDIADGNPKLTLGLIWTIILHFQ 1159
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
1052-1170 |
1.54e-73 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 241.85 E-value: 1.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1052 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKL 1131
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1988774674 1132 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSE 1170
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
1052-1168 |
7.73e-70 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 231.41 E-value: 7.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1052 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKL 1131
Cdd:cd21236 12 DERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKL 91
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774674 1132 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 1168
Cdd:cd21236 92 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
1172-1277 |
2.52e-65 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 217.58 E-value: 2.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1172 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 1251
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1988774674 1252 PEDVDVPHPDEKSIITYVSSLYDAMP 1277
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
1173-1277 |
8.28e-63 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 210.33 E-value: 8.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 1252
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1988774674 1253 EDVDVPHPDEKSIITYVSSLYDAMP 1277
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
1052-1169 |
6.95e-62 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 208.35 E-value: 6.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1052 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKL 1131
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1988774674 1132 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 1169
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
1173-1277 |
4.20e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 194.05 E-value: 4.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 1252
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1988774674 1253 EDVDVPHPDEKSIITYVSSLYDAMP 1277
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
1057-1160 |
5.54e-51 |
|
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: 176.80 E-value: 5.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1057 VQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNIR 1135
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1988774674 1136 NDDIADGNPKLTLGLIWTIILHFQI 1160
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
1171-1277 |
9.81e-49 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 170.22 E-value: 9.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1171 DMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLL 1250
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1988774674 1251 DPEDVDVPHPDEKSIITYVSSLYDAMP 1277
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
1052-1156 |
1.03e-48 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 170.63 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1052 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLRHRQVK 1130
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRVH 90
|
90 100
....*....|....*....|....*.
gi 1988774674 1131 LVNIRNDDIADGNPKLTLGLIWTIIL 1156
Cdd:cd21246 91 LENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| S10_plectin |
pfam03501 |
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the ... |
7-99 |
7.24e-47 |
|
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the cytoskeletal muscle protein plectin as well as the ribosomal S10 protein. This domain may be involved in RNA binding.
Pssm-ID: 427337 Cd Length: 92 Bit Score: 164.23 E-value: 7.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 7 MPLRDLRAIYEILFRDGVMVAKKDkRPQIKHPEVqSVSNLQVIRAMGSLKSRGYVKETFAWKHFYWYLTNDGIVYLRDYL 86
Cdd:pfam03501 1 IPKENRKAIYEYLFKEGVLVAKKD-FNLPKHPEL-NVPNLQVIKAMQSLKSRGYVKEQFAWRHYYWYLTNEGIEYLREYL 78
|
90
....*....|...
gi 1988774674 87 HLPTEIVPATLQR 99
Cdd:pfam03501 79 HLPAEIVPATLKR 91
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
1173-1273 |
1.54e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 163.74 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 1252
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1988774674 1253 EDVDVPHPDEKSIITYVSSLY 1273
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
1053-1160 |
5.71e-45 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 159.85 E-value: 5.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1053 ERDRVQKKTFTKWVNKHLIKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLRHRQ 1128
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1988774674 1129 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 1160
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
1050-1156 |
1.15e-44 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 159.00 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1050 IEDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLrHRQ 1128
Cdd:cd21193 9 LQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL-KTK 87
|
90 100
....*....|....*....|....*...
gi 1988774674 1129 VKLVNIRNDDIADGNPKLTLGLIWTIIL 1156
Cdd:cd21193 88 VRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
1173-1273 |
4.46e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 156.79 E-value: 4.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 1252
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1988774674 1253 EDVDVPHPDEKSIITYVSSLY 1273
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
1029-1156 |
3.36e-42 |
|
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: 152.52 E-value: 3.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1029 SPEVDWDH--SLGEPEEKTWPNFIEDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-E 1105
Cdd:cd21317 1 LADDDWDNdnSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpT 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 1106 KGRMRFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1156
Cdd:cd21317 81 KGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
1026-1156 |
6.04e-42 |
|
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: 152.10 E-value: 6.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1026 RGASPEVDWDH--SLGEPEEKTWPNFIEDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLP 1103
Cdd:cd21318 5 RWESTERPWDEpaATAKLFECSRIKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLP 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 1104 R-EKGRMRFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1156
Cdd:cd21318 85 KpTRGRMRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
1053-1160 |
1.27e-41 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 150.03 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1053 ERDRVQKKTFTKWVNKHLIKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLRHRQ 1128
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQpiVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1988774674 1129 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 1160
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
1051-1273 |
1.43e-41 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 165.50 E-value: 1.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1051 EDERDRVQKKTFTKWVNKHLIKA-QRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLRHR 1127
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1128 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvngQSEDMTAKEKLLLWSQRMTDGYQ-GIRCDNFTTSWRDGKL 1206
Cdd:COG5069 83 GVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1207 FNAVIHKHYPRLINMGKVYQQTNLE--NLEQAFSVAEKDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLY 1273
Cdd:COG5069 160 FSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1908-1985 |
2.81e-40 |
|
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: 145.05 E-value: 2.81e-40
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774674 1908 LSWQYLMRDFTQIRSWNITMLKTMKPEEYRLIMRNLELHYQDFMRDSQDSQLFGPDDRMQVEDDYTKSTQHFDNLLRS 1985
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
1160-1275 |
1.47e-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: 144.43 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1160 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 1239
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774674 1240 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1275
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
1169-1273 |
6.19e-39 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 142.45 E-value: 6.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1169 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTR 1248
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1988774674 1249 LLDPEDVDVPHPDEKSIITYVSSLY 1273
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
1172-1277 |
9.79e-39 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 141.69 E-value: 9.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1172 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 1251
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1988774674 1252 PEDVDVPHPDEKSIITYVSSLYDAMP 1277
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
1057-1158 |
2.62e-38 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 140.61 E-value: 2.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1057 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLRHRQVKLVNI 1134
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1988774674 1135 RNDDIADGNPKLTLGLIWTIILHF 1158
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
1053-1160 |
3.59e-38 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 140.35 E-value: 3.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1053 ERDRVQKKTFTKWVNKHLIKAQ--RHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVK 1130
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1988774674 1131 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 1160
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
1055-1156 |
3.66e-38 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 139.83 E-value: 3.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1055 DRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLRHRQVKLVN 1133
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1988774674 1134 IRNDDIADGNPKLTLGLIWTIIL 1156
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2328-2907 |
3.30e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 155.48 E-value: 3.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2328 QEYVTLRTRYSEL-MTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQlaeahakAIAKAEKEAQE 2406
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL-------ELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2407 LKLKMQEEVSKREiaavDAEKQktnIQLELQELKNLSEQQIKDKSQqvdealhsRTKIEEEIRLIRIQLETTEKQKYTAE 2486
Cdd:COG1196 286 AQAEEYELLAELA----RLEQD---IARLEERRRELEERLEELEEE--------LAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2487 SELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQV 2566
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2567 KQAEIEKEKQIkvAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELE 2646
Cdd:COG1196 431 AELEEEEEEEE--EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2647 KWRQKANEALRLRL------QAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQ 2720
Cdd:COG1196 509 GVKAALLLAGLRGLagavavLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2721 QKLTAEQELIRLRADFDNAEQQRS---------LLEDELYRLKNEvaAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKE 2791
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADaryyvlgdtLLGRTLVAARLE--AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2792 tmsnTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALK 2871
Cdd:COG1196 667 ----RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
570 580 590
....*....|....*....|....*....|....*.
gi 1988774674 2872 EKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEE 2907
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
1172-1273 |
5.61e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 136.92 E-value: 5.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1172 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 1251
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1988774674 1252 PEDVDVPHPDEKSIITYVSSLY 1273
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
1052-1160 |
6.80e-36 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 133.89 E-value: 6.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1052 DERDRVQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVK 1130
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1988774674 1131 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 1160
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
1169-1273 |
1.18e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 133.26 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1169 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTR 1248
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1988774674 1249 LLDPEDVDVPHPDEKSIITYVSSLY 1273
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2413-2988 |
2.81e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 148.93 E-value: 2.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2413 EEVSKR----EIAAVDAEKQKTnIQLELQELK-NLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAES 2487
Cdd:COG1196 196 GELERQleplERQAEKAERYRE-LKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2488 ELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVK 2567
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2568 QAEIEKEKQIKVAHEAAQK-----SAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAE 2642
Cdd:COG1196 355 EAEAELAEAEEALLEAEAElaeaeEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2643 KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 2722
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2723 LTAEQELIRLRAD---FDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKS 2799
Cdd:COG1196 515 LLAGLRGLAGAVAvliGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2800 KQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAE--EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAEn 2877
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAArlEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2878 ERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEkassgKLD 2957
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE-----ELL 748
|
570 580 590
....*....|....*....|....*....|.
gi 1988774674 2958 LELELNKLKNIADETQQskiraEEEAEKLRK 2988
Cdd:COG1196 749 EEEALEELPEPPDLEEL-----ERELERLER 774
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2318-3073 |
5.52e-35 |
|
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: 148.67 E-value: 5.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2318 KLDSASDNIIQEYVTLRTRYSELMTLTSQY---IKFitdtqRRLDDEEKAAEKL-----KAEERKKMAEMQAELDKQKQL 2389
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLERQAekaERY-----KELKAELRELELAllvlrLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2390 AEAHAKAIAKAEKEAQELKLKMQE------------EVSKREIAAVDAEKQKTNiqlelQELKNLsEQQIKDKSQQVDEA 2457
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSEleeeieelqkelYALANEISRLEQQKQILR-----ERLANL-ERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2458 LHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEA 2537
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2538 EKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHgav 2617
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA--- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2618 lQLQQEAERLKKQQEDAENSREEAEKEL--------------------EKWRQKANEALRLRLQAedeahkktlaqeeae 2677
Cdd:TIGR02168 486 -QLQARLDSLERLQENLEGFSEGVKALLknqsglsgilgvlselisvdEGYEAAIEAALGGRLQA--------------- 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2678 kqkeeAEREAKKRAKAEESALKQKE-----MAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYR 2752
Cdd:TIGR02168 550 -----VVVENLNAAKKAIAFLKQNElgrvtFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2753 LK--NEVAAAQQQRKQLEDELAKVRSEMDIL----IQLKtKAEKETMSNTEKSKQLLEAEaAKMKDLAEEASRLRAISEE 2826
Cdd:TIGR02168 625 VLvvDDLDNALELAKKLRPGYRIVTLDGDLVrpggVITG-GSAKTNSSILERRREIEELE-EKIEELEEKIAELEKALAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2827 AKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEdQASQHKQEIE 2906
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2907 EKIVQLkkssEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKL 2986
Cdd:TIGR02168 782 AEIEEL----EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2987 RKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQ 3066
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
....*..
gi 1988774674 3067 VQSVLAQ 3073
Cdd:TIGR02168 938 IDNLQER 944
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
1176-1277 |
6.50e-35 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 130.63 E-value: 6.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1176 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 1254
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1988774674 1255 VDVPHPDEKSIITYVSSLYDAMP 1277
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2352-3594 |
7.29e-35 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 148.44 E-value: 7.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2352 TDTQRRLDDEEKAAEKLKAEERKKMAEMQAELdkqkqlaeaHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEkqktn 2431
Cdd:NF041483 90 ADAERELRDARAQTQRILQEHAEHQARLQAEL---------HTEAVQRRQQLDQELAERRQTVESHVNENVAWAE----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2432 iqlelqELKNLSEQQIKdksQQVDEalhSRTKIEEEIRLIRIQLE--TTE-KQKYTAESELKQlrdraAEAEKLRKLAQD 2508
Cdd:NF041483 156 ------QLRARTESQAR---RLLDE---SRAEAEQALAAARAEAErlAEEaRQRLGSEAESAR-----AEAEAILRRARK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2509 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQaeEAERQVKQAEIEKEKQIKVAHEAAQKS- 2587
Cdd:NF041483 219 DAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAAAKQl 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2588 AAAELQSKHMSfaeKTSKLEeslkqehgaVLQLQQEAERlkkqqeDAENSREEAEKELEKWRQkanEALRLRLQAEDEAh 2667
Cdd:NF041483 297 ASAESANEQRT---RTAKEE---------IARLVGEATK------EAEALKAEAEQALADARA---EAEKLVAEAAEKA- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2668 kKTLAQEEAEKQKEEAEREAKK-RAKAEESALKQKEMAEEELERQRKIAESTAQqkltaeqeliRLRAD-FDNAEQQRSL 2745
Cdd:NF041483 355 -RTVAAEDTAAQLAKAARTAEEvLTKASEDAKATTRAAAEEAERIRREAEAEAD----------RLRGEaADQAEQLKGA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2746 LEDELYRLKNEVAAAQQQRKQLEDELAKVRSE-MDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEAsrlrais 2824
Cdd:NF041483 424 AKDDTKEYRAKTVELQEEARRLRGEAEQLRAEaVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADADEL------- 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2825 eeakhqRQIAEEEAARQRAEAerilkeklaaISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQE 2904
Cdd:NF041483 497 ------RSTATAESERVRTEA----------IERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2905 IEEKIVQLKKS----------------------------SEAEMERQKAiVDDTLKQRRVVEEEIRILKLNFEK------ 2950
Cdd:NF041483 561 ETERAIAARQAeaaeeltrlhteaeerltaaeealadarAEAERIRREA-AEETERLRTEAAERIRTLQAQAEQeaerlr 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2951 ------ASSGKLDLE-----------LELNKLKNIADETQQsKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEE 3013
Cdd:NF041483 640 teaaadASAARAEGEnvavrlrseaaAEAERLKSEAQESAD-RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEET 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3014 AARQRKAALEELERLRKKAEE----ARKQKDEADKEAEKQIVVA-QQAAQKCSAAEQQvqsvlAQQIEDSIT--QKKLKE 3086
Cdd:NF041483 719 LGSARAEADQERERAREQSEEllasARKRVEEAQAEAQRLVEEAdRRATELVSAAEQT-----AQQVRDSVAglQEQAEE 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3087 EYEKakklakeaeaakekaereaalLRQQAEE-AERQKTaaeeeaanqaKAQEDAERLRKEAeFEAAKRAQAEAAALMQK 3165
Cdd:NF041483 794 EIAG---------------------LRSAAEHaAERTRT----------EAQEEADRVRSDA-YAERERASEDANRLRRE 841
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3166 QQADTEMAkhKKLAEQTLKQKFQvEQEltkvKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVK----VQ 3241
Cdd:NF041483 842 AQEETEAA--KALAERTVSEAIA-EAE----RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQ 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3242 MEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMR-KLAEDAARLSVEAQ-EAARLRQIAEDDLNQQRALAEKMLKE 3319
Cdd:NF041483 915 ADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGSAQQHAERIRTE 994
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3320 KMQAIQEASrlkAEAEMLQKQkdlAQEQAQKLL-EDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSqls 3398
Cdd:NF041483 995 AERVKAEAA---AEAERLRTE---AREEADRTLdEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTT--- 1065
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3399 eaqARAEEEAKKFKKQADKVATRLHETeiATQEKMTVVERleferlnTSKEADDL-----RKAIA---DLENEKARLKKE 3470
Cdd:NF041483 1066 ---TEAEAQADTMVGAARKEAERIVAE--ATVEGNSLVEK-------ARTDADELlvgarRDATAireRAEELRDRITGE 1133
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3471 AEELQNKSK-EMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQE 3549
Cdd:NF041483 1134 IEELHERARrESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVRE 1213
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*
gi 1988774674 3550 KKTLQATMDAalskqkEAEEEMLRKQKEMQELERQRleqERILAE 3594
Cdd:NF041483 1214 AEKIKAEAEA------EAKRTVEEGKRELDVLVRRR---EDINAE 1249
|
|
| PTZ00034 |
PTZ00034 |
40S ribosomal protein S10; Provisional |
5-97 |
1.37e-34 |
|
40S ribosomal protein S10; Provisional
Pssm-ID: 173331 Cd Length: 124 Bit Score: 130.53 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 5 MLMPLRDLRAIYEILFRDGVMVAKKDkRPQIKHPEVqSVSNLQVIRAMGSLKSRGYVKETFAWKHFYWYLTNDGIVYLRD 84
Cdd:PTZ00034 2 VYVPKANRKAIYRYLFKEGVIVCKKD-PKGPWHPEL-NVPNLHVMMLMRSLKSRGLVKEQFAWQHYYYYLTDEGIEYLRT 79
|
90
....*....|...
gi 1988774674 85 YLHLPTEIVPATL 97
Cdd:PTZ00034 80 YLHLPPDVFPATH 92
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
1157-1273 |
1.57e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 130.56 E-value: 1.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1157 HFQISDIQVNGQSEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQA 1236
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774674 1237 FSVAEKDLGVTRLLDPEDVDVPHPDEKSIITYVSSLY 1273
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2353-2988 |
5.61e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 146.05 E-value: 5.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2353 DTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAiAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTni 2432
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-- 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2433 qlELQELKNLSEQQIKDKSQQVDEALHSRTKIEEeirliriqlettekqKYTAESELKQLRDRAAEAEKLRKLAqdEAEK 2512
Cdd:PTZ00121 1358 --EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE---------------KKKADEAKKKAEEDKKKADELKKAA--AAKK 1418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2513 LRKQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKALEdleklrmqAEEAERQVKQAEiEKEKQIKVAHEAAQKSAAAEL 2592
Cdd:PTZ00121 1419 KADEAKKKAEEKKKA-DEAKKKAEEAKKADEAKKKAEE--------AKKAEEAKKKAE-EAKKADEAKKKAEEAKKADEA 1488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2593 QSKhmsfAEKTSKLEESLKQEHGAvlqlQQEAERLKKQQE--DAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKT 2670
Cdd:PTZ00121 1489 KKK----AEEAKKKADEAKKAAEA----KKKADEAKKAEEakKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2671 LAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRaDFDNAEQQRSLLEDEL 2750
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLK 1639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2751 YRLKNEVAAAQQQRKqlEDELAKVRSEmdiliQLKTKAEKEtmsnTEKSKQLLEAEAAKMKdlAEEASRLRAisEEAKHQ 2830
Cdd:PTZ00121 1640 KKEAEEKKKAEELKK--AEEENKIKAA-----EEAKKAEED----KKKAEEAKKAEEDEKK--AAEALKKEA--EEAKKA 1704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2831 RQIAEEEAARQRaEAERILKEKLAAISEATRLKTEAEialkEKEAENERLRRQAEDeayqrkalEDQASQHKQEIEEKIV 2910
Cdd:PTZ00121 1705 EELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEAE----EDKKKAEEAKKDEEE--------KKKIAHLKKEEEKKAE 1771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2911 QLKKSSEAEMErqKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAD----ETQQSKIRAEEEAEKL 2986
Cdd:PTZ00121 1772 EIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDsaikEVADSKNMQLEEADAF 1849
|
..
gi 1988774674 2987 RK 2988
Cdd:PTZ00121 1850 EK 1851
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
1033-1156 |
6.24e-34 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 129.78 E-value: 6.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1033 DWDH--SLGEPEEKTWPNFIEDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRM 1109
Cdd:cd21316 27 EWDNenSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRM 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1988774674 1110 RFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1156
Cdd:cd21316 107 RIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
1173-1273 |
2.41e-33 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 126.37 E-value: 2.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 1252
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1988774674 1253 EDVDVPHPDEKSIITYVSSLY 1273
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2783-3653 |
6.85e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 142.20 E-value: 6.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2783 QLKTKAEKETmsnTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAE---EEAARQRAEAERILKEKLAAISEA 2859
Cdd:PTZ00121 1083 AKEDNRADEA---TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEarkAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2860 TRLKTEAEIALKEKEAENERLRRQAEDeayQRKALEDQASQHKQEIE-----EKIVQLKKSSEAEMERQKAIVDDTLKQR 2934
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEaarkaEEERKAEEARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2935 RVVEEEIRIlklnfEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEA 3014
Cdd:PTZ00121 1237 KDAEEAKKA-----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3015 ARQRKA---------ALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSV--LAQQIEDSITQKK 3083
Cdd:PTZ00121 1312 EEAKKAdeakkkaeeAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3084 LKEEyekakklakeaeaakekaereaalLRQQAEEAERQktaaEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALM 3163
Cdd:PTZ00121 1392 KADE------------------------AKKKAEEDKKK----ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA 1443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3164 QKQQADTEMAKHKKLAEQtLKQKFQVEQELTKVKLKLDETDKQksvldEELQRLKDEVDDAVKQRGQVEEElfkvKVQME 3243
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEE-AKKKAEEAKKADEAKKKAEEAKKA-----DEAKKKAEEAKKKADEAKKAAEA----KKKAD 1513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3244 ELLKLKNKIEEENQRLIKKDKDSTQKLLAEE---AENMRKLAE----DAARLSVEAQEAARLRQIAEDDLNQQRALAEKM 3316
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEkkkADELKKAEElkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3317 LKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERkrqleimaEAERLRLQVSQ 3396
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK--------AEEENKIKAAE 1665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3397 LSEAQARAEEEAKKFKKqADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQN 3476
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKK-AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3477 KSKEMA--DAQQKKIEH---EKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfeeevKKAKALKDEQERQKQQMEQEKK 3551
Cdd:PTZ00121 1745 KAEEAKkdEEEKKKIAHlkkEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD-----KKIKDIFDNFANIIEGGKEGNL 1819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3552 TLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQK----LREKLQQLEDAQKDQHTRETDKVLHKDIi 3627
Cdd:PTZ00121 1820 VINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKeadfNKEKDLKEDDEEEIEEADEIEKIDKDDI- 1898
|
890 900
....*....|....*....|....*.
gi 1988774674 3628 hltTIETTKTVYNGQNVGDVVDGIDK 3653
Cdd:PTZ00121 1899 ---EREIPNNNMAGKNNDIIDDKLDK 1921
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
1056-1161 |
2.08e-32 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 124.49 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1056 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLRHRQ-VKLV 1132
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1988774674 1133 NIRNDDIADGNPKLTLGLIWTIILHFQIS 1161
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1057-1160 |
6.35e-32 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 122.40 E-value: 6.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1057 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLRHRQVKLVNI 1134
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1988774674 1135 RNDDIADGNPKLTLGLIWTIILHFQI 1160
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2506-3359 |
1.78e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 137.58 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2506 AQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRmQAEEAERQVKQAEIEKEKQIKVAHEAAQ 2585
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR-KAEDAKRVEIARKAEDARKAEEARKAED 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2586 -KSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDaenSREEAEKELEKWRQKANEALRLRLQAED 2664
Cdd:PTZ00121 1175 aKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA---KKAEAVKKAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2665 EAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEEL---ERQRKIAESTAQQKLTAEQELIRLRADFDNAEQ 2741
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2742 QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDiliQLKTKAEKEtmsntekskqllEAEAAKMKdlAEEASRLR 2821
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA---EKKKEEAKK------------KADAAKKK--AEEKKKAD 1394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2822 AISEEAKHQRQIAEE----EAARQRAEAeriLKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQ 2897
Cdd:PTZ00121 1395 EAKKKAEEDKKKADElkkaAAAKKKADE---AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2898 ASQHKQEIEEKIVQLKKSSEAEMERQKAivdDTLKQRrvveEEIRILKLNFEKASSGKLDLELELNKLKNIADETQqski 2977
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKA---DEAKKA----AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK---- 1540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2978 RAEE--EAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQ----RKAALEELERLRKKAEEARKQKDEADKEAEKQIV 3051
Cdd:PTZ00121 1541 KAEEkkKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3052 VAQQAAQkcsaaEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAA 3131
Cdd:PTZ00121 1621 KAEELKK-----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3132 NQAKAQEDAERLRKEAEFEAAkraqaeaaalmQKQQADTEMAKHKKLAEQTLKQKfqvEQELTKV-KLKLDETDKQKsvl 3210
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKK-----------KAEELKKAEEENKIKAEEAKKEA---EEDKKKAeEAKKDEEEKKK--- 1758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3211 deeLQRLKDEVDDAVKQRGQVEEELFKvkvqmEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSV 3290
Cdd:PTZ00121 1759 ---IAHLKKEEEKKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDS 1830
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774674 3291 EAQEAArlrqiaeDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQ 3359
Cdd:PTZ00121 1831 AIKEVA-------DSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEK 1892
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
1057-1160 |
1.88e-31 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 120.88 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1057 VQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNIR 1135
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1988774674 1136 NDDIADGNPKLTLGLIWTIILHFQI 1160
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
1172-1270 |
2.18e-31 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 120.61 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1172 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 1251
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1988774674 1252 PEDVDVPHPDEKSIITYVS 1270
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
1160-1275 |
5.54e-31 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 119.94 E-value: 5.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1160 ISDIQvngqSEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 1239
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774674 1240 AEKDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLYDA 1275
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
1053-1162 |
1.54e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 118.45 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1053 ERDRVQKKTFTKWVNKHLIKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLRHRQ 1128
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1988774674 1129 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 1162
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
1172-1270 |
2.22e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 118.01 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1172 MTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD 1251
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1988774674 1252 PEDVDVPHPDEKSIITYVS 1270
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
1176-1278 |
3.96e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 117.34 E-value: 3.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1176 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLDPE 1253
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1988774674 1254 DVDVPHPDEKSIITYVSSLYDAMPR 1278
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
1056-1158 |
6.39e-30 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 116.43 E-value: 6.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1056 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 1132
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1988774674 1133 NIRNDDIADGNPKLTLGLIWTIILHF 1158
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
1176-1277 |
1.25e-29 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 115.44 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1176 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 1254
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1988774674 1255 VDVPHPDEKSIITYVSSLYDAMP 1277
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
1178-1273 |
2.40e-29 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 114.75 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1178 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED-VD 1256
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1988774674 1257 VPHPDEKSIITYVSSLY 1273
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2512-3122 |
2.69e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 129.67 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2512 KLRKqvsEETQKK-RQAEEELKRKSEAEKEAAKQkqkaledLEKLRMQAEEAER--QVKQAEIEKEKQIKVAH------- 2581
Cdd:COG1196 171 KERK---EEAERKlEATEENLERLEDILGELERQ-------LEPLERQAEKAERyrELKEELKELEAELLLLKlreleae 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2582 EAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQ 2661
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2662 AEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQ 2741
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2742 QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLR 2821
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2822 AISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQH 2901
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2902 KQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEE 2981
Cdd:COG1196 561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2982 EAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCS 3061
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 3062 AAEQQVQSVLAQQIEdsITQKKLKEEYEKAKKLAKEAEAAKEKAEReaalLRQQAEEAERQ 3122
Cdd:COG1196 721 LEEEALEEQLEAERE--ELLEELLEEEELLEEEALEELPEPPDLEE----LERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2497-3353 |
4.62e-29 |
|
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: 129.02 E-value: 4.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2497 AEAEKLRKLAQDEAEKLR-KQVSEETQKK-RQAEEELKRKSEAEKEAAKQkqkaledLEKLRMQAEEAER------QVKQ 2568
Cdd:TIGR02168 152 AKPEERRAIFEEAAGISKyKERRKETERKlERTRENLDRLEDILNELERQ-------LKSLERQAEKAERykelkaELRE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2569 AEIE---KEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAEN--SREEAEK 2643
Cdd:TIGR02168 225 LELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeiSRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2644 ELEKWRQKANEALRLRLQAEDEAHKKTLAQEEaekqkeeaeREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKL 2723
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELA---------EELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2724 TAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDiliqlkTKAEKETMSNTEKSKQLL 2803
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE------EAELKELQAELEELEEEL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2804 EAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEaerilKEKLAAISEATRLKTEAEIALKEKEAEN------ 2877
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR-----LDSLERLQENLEGFSEGVKALLKNQSGLsgilgv 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2878 --ERLRRQAEDE----AYQRKALEDQASQHKQEIEEKIVQLKKSS-------EAEMERQKAIVDDTLKQRRVVEEEIRIL 2944
Cdd:TIGR02168 525 lsELISVDEGYEaaieAALGGRLQAVVVENLNAAKKAIAFLKQNElgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2945 KLNFEKASSGKLDLELELNKL---KNIADETQQSKIRAEEE-------------------AEKLRKLALEEEKRRREAEE 3002
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYLLGGVlvvDDLDNALELAKKLRPGYrivtldgdlvrpggvitggSAKTNSSILERRREIEELEE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3003 KVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDeadkEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQiedSITQK 3082
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELE----ELSRQISALRKDLARLEAEVEQLEERIAQL---SKELT 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3083 KLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTaaeEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAAL 3162
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK---ALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3163 MQKQQADTEMAKHKKLAEQTLK---QKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVK 3239
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESlaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3240 vqmEELLKLKNKIEEENQRLikkdkdstQKLLAEEAENMRKLAEDAarlSVEAQEAARLRQIAEDDLNQQRALAEKmLKE 3319
Cdd:TIGR02168 915 ---RELEELREKLAQLELRL--------EGLEVRIDNLQERLSEEY---SLTLEEAEALENKIEDDEEEARRRLKR-LEN 979
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1988774674 3320 K--------MQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE 3353
Cdd:TIGR02168 980 KikelgpvnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2686-3605 |
1.21e-27 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 124.31 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2686 EAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRadfDNAEQQRSLLEDELYRLKNEVAAAQQQRK 2765
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALE---YYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2766 QLEDELAKVRSEMDILIQLKTKAEKETmsntEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEA 2845
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKL----AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2846 ERILKEKLAAISEATRLKTEAEIALKEKEaENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKa 2925
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKELK-ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2926 ivddtlKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIaDETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVK 3005
Cdd:pfam02463 395 ------EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI-LEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3006 KIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVaqqaaqkcsaaeQQVQSVLAQQIEDSITQKKLK 3085
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA------------LIKDGVGGRIISAHGRLGDLG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3086 EEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQK 3165
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3166 QQADTEMAKHKKLAEQTLKQKFQveqelTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEEL 3245
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLK-----ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3246 lKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRklaedaarlsveaqeaARLRQIAEDDLNQQRALAEKMLKEKMQAIQ 3325
Cdd:pfam02463 691 -KEEILRRQLEIKKKEQREKEELKKLKLEAEELL----------------ADRVQEAQDKINEELKLLKQKIDEEEEEEE 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3326 EASRLKAEAEMLQKQkdlaQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAE 3405
Cdd:pfam02463 754 KSRLKKEEKEEEKSE----LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3406 EEAKKFKKQADKVATRLHETEIATQEKMTVverLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQ 3485
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERL---EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEES 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3486 QKKIEHEKTVLQQTFMTEKEmlLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTL------------ 3553
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEE--AEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELgkvnlmaieefe 984
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 3554 --QATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQ 3605
Cdd:pfam02463 985 ekEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFF 1038
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
1056-1158 |
2.29e-27 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 109.11 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1056 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 1132
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1988774674 1133 NIRNDDIADGNPKLTLGLIWTIILHF 1158
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
1158-1275 |
4.06e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 109.40 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1158 FQISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAF 1237
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1988774674 1238 SVAEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1275
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
1038-1160 |
5.95e-27 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 108.69 E-value: 5.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1038 LGEPEEKTWPNFIEDERDRVQKKTFTKWVNKHLIKAQRHV--TDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKL 1114
Cdd:cd21247 1 MDTEYEKGHIRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1988774674 1115 QNVQIALDFLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 1160
Cdd:cd21247 81 ENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| COG5045 |
COG5045 |
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis]; |
5-105 |
6.11e-27 |
|
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227378 Cd Length: 105 Bit Score: 108.09 E-value: 6.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 5 MLMPLRDLRAIYEILFRDGVMVAKKDKRpQIKHPEVQsVSNLQVIRAMGSLKSRGYVKETFAWKHFYWYLTNDGIVYLRD 84
Cdd:COG5045 1 MLVPKENRYKIHQRLFQKGVAVAKKDFN-LGKHRELE-IPNLHVIKAMQSLISYGYVKTIHVWRHSYYTLTPEGVEYLRE 78
|
90 100
....*....|....*....|.
gi 1988774674 85 YLHLPTEIVPATLQRIRKPAA 105
Cdd:COG5045 79 YLVLPDEGVPSTEAPAVSPTQ 99
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
1160-1275 |
7.46e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 108.63 E-value: 7.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1160 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 1239
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774674 1240 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1275
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2836-3619 |
2.23e-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: 120.55 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2836 EEAA------RQRAEAERilkeKLAAISEA-TRLkteaEIALKEKEAENERLRRQAEdEAYQRKALEDQASQHK------ 2902
Cdd:TIGR02168 162 EEAAgiskykERRKETER----KLERTRENlDRL----EDILNELERQLKSLERQAE-KAERYKELKAELRELElallvl 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2903 --QEIEEKIVQLKkSSEAEMERQKAIVDDTLKqrrVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAE 2980
Cdd:TIGR02168 233 rlEELREELEELQ-EELKEAEEELEELTAELQ---ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2981 EEAEKLRKlaleeekrrreaeeKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKC 3060
Cdd:TIGR02168 309 ERLANLER--------------QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3061 SAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDA 3140
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3141 ERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQE----LTKVKLKLD----------ETDKQ 3206
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkaLLKNQSGLSgilgvlseliSVDEG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3207 KS-----VLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKL 3281
Cdd:TIGR02168 535 YEaaieaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3282 A----------------EDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAI---QEASRLKAEAEMLQKQKD 3342
Cdd:TIGR02168 615 RkalsyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILerrREIEELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3343 LAQEQAQKLLEDkqlmQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRL 3422
Cdd:TIGR02168 695 ELEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3423 HETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKsKEMADAQQKKIEHEKTVLQQTFMT 3502
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3503 EKEMLLKKEKLIEDEKKRLEsQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQ--E 3580
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAqlE 928
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1988774674 3581 LERQRLEQEriLAEENQKLREKLQ-QLEDAQKDQHTRETD 3619
Cdd:TIGR02168 929 LRLEGLEVR--IDNLQERLSEEYSlTLEEAEALENKIEDD 966
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
1056-1161 |
2.71e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 107.04 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1056 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLRHRQVKLV 1132
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1988774674 1133 NIRNDDIADGNPKLTLGLIWTIILHFQIS 1161
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2355-3228 |
2.96e-26 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 120.08 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2355 QRRLDDEEKAAE----KLKAEERKKMAEMQAELDKQ---KQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEK 2427
Cdd:pfam02463 153 ERRLEIEEEAAGsrlkRKKKEALKKLIEETENLAELiidLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2428 QKTNIQLELQELKNLSEQQIKDKSQQVDEalhsrtKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQ 2507
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIE------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2508 DEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKS 2587
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2588 AAA------ELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQ 2661
Cdd:pfam02463 387 SSAaklkeeELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2662 AEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQ-----KLTAEQELIRLRADF 2736
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISahgrlGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2737 DNAEQQRSLLEDELYRLKNEVAA-------AQQQRKQLEDELAKVRS----EMDILIQLKTKAEKETMSNTEKSKQLLEA 2805
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRAltelplgARKLRLLIPKLKLPLKSiavlEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2806 EAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKlaaiseaTRLKTEAEIALKEKEAENERLRRQAE 2885
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTK-------ELLEIQELQEKAESELAKEEILRRQL 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2886 DEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRilklnfEKASSGKLDLELELNKL 2965
Cdd:pfam02463 700 EIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR------LKKEEKEEEKSELSLKE 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2966 KNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKE 3045
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3046 AEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAErqkta 3125
Cdd:pfam02463 854 EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE----- 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3126 AEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMaKHKKLAEQTLKQKFQVEQELTKVKLKLDETDK 3205
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKV-NLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007
|
890 900
....*....|....*....|...
gi 1988774674 3206 QKSVLDEELQRLKDEVDDAVKQR 3228
Cdd:pfam02463 1008 IRAIIEETCQRLKEFLELFVSIN 1030
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2355-2914 |
3.53e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 120.25 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2355 QRRLDDEEKAAEKL--KAEERKKMAEMQAELDKQKQLAEAHAKAiAKAEKEAQELKlKMQEEVSKREIAAVDAEKQKTNI 2432
Cdd:PTZ00121 1370 EKKKEEAKKKADAAkkKAEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAK-KKAEEKKKADEAKKKAEEAKKAD 1447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2433 QLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAE----SELKQLRDRAAEAEKLRKL--A 2506
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkaAEAKKKADEAKKAEEAKKAdeA 1527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2507 QDEAEKLRKQVSEETQKKRQAEEELK----RKSEaEKEAAKQKQKALEDLEKLRMQAEEAeRQVKQAEIEK-----EKQI 2577
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKaeelKKAE-EKKKAEEAKKAEEDKNMALRKAEEA-KKAEEARIEEvmklyEEEK 1605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2578 KVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGavlQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALR 2657
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA---EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2658 lrlqAEDEAHKKtlaqeeaekqKEEAEREAKKRAKAEEsaLKQKEmaEEELERQRKIAESTAQQKLTAEQELIRLRADFD 2737
Cdd:PTZ00121 1683 ----AEEDEKKA----------AEALKKEAEEAKKAEE--LKKKE--AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2738 NAEQQRSLLEDelyrlKNEVaaaQQQRKQLEDELAKVRSEMDILIQ--LKTKAEKETMSNTEKSKQLL------------ 2803
Cdd:PTZ00121 1745 KAEEAKKDEEE-----KKKI---AHLKKEEEKKAEEIRKEKEAVIEeeLDEEDEKRRMEVDKKIKDIFdnfaniieggke 1816
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2804 ---------EAEAAKMKDLAEEASRLRAISEE-AKHQRQIAEEEAARQRAEA----ERILKEKLAAISEATRLKTEAEIA 2869
Cdd:PTZ00121 1817 gnlvindskEMEDSAIKEVADSKNMQLEEADAfEKHKFNKNNENGEDGNKEAdfnkEKDLKEDDEEEIEEADEIEKIDKD 1896
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1988774674 2870 LKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKK 2914
Cdd:PTZ00121 1897 DIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIKISK 1941
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2246-2915 |
5.23e-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: 119.01 E-value: 5.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2246 KIQAVPITDSKTLKEQLAQEKK--LLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVspLKKTKLDSAS 2323
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2324 DNIIQEYVTLRTRYSELmtltSQYIKFITDTQRRLDDEEKAAEKLKAEERKK-------MAEMQAELDKQKQLAEAHAKA 2396
Cdd:TIGR02168 284 EELQKELYALANEISRL----EQQKQILRERLANLERQLEELEAQLEELESKldelaeeLAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2397 IAKAEKEAQELKLKM---QEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEE-EIRLIR 2472
Cdd:TIGR02168 360 LEELEAELEELESRLeelEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2473 IQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAE---EELKRKSEAEKEAAKQK---- 2545
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLErlqENLEGFSEGVKALLKNQsgls 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2546 ----------------QKALEDLEKLRMQA---EEAERQVKQAEIEKEKQI-KVAHEAAQKSAAAELQSKHM-------- 2597
Cdd:TIGR02168 520 gilgvlselisvdegyEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELgRVTFLPLDSIKGTEIQGNDReilknieg 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2598 ---------SFAEKTSKLEESL--------------------------------------------KQEHGAVLQLQQEA 2624
Cdd:TIGR02168 600 flgvakdlvKFDPKLRKALSYLlggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsAKTNSSILERRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2625 ERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMA 2704
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2705 EEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSL-------LEDELYRLKNEVAAAQQQRKQLEDELAKVRSE 2777
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealdeLRAELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2778 MDILIQlKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAIS 2857
Cdd:TIGR02168 840 LEDLEE-QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 2858 EATRLKTEAEIALKEKEAE----NERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKS 2915
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2638-3272 |
1.24e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 117.73 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2638 REEAEKELEKWRQKANEALR-LRLQAEDEAHKKTLAQEEAekqkeeaeREAKKRAKAEESALKQKEMAEEELERQRKIAE 2716
Cdd:COG1196 195 LGELERQLEPLERQAEKAERyRELKEELKELEAELLLLKL--------RELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2717 STAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNT 2796
Cdd:COG1196 267 AELEE---LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2797 EKSKQLLEAEAAKMKDLAEEASRL----RAISEEAKHQRQIAEEEAARQRAEAErILKEKLAAISEATRLKTEAEIALKE 2872
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALleaeAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2873 KEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRI-LKLNFEKA 2951
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLlLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2952 SSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKK 3031
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3032 AEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAqqiEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAAL 3111
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL---GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3112 LRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQ 3191
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3192 ELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQR---GQV----EEELFKVKVQMEELLKLKNKIEEENQRL---IK 3261
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIealGPVnllaIEEYEELEERYDFLSEQREDLEEARETLeeaIE 819
|
650
....*....|..
gi 1988774674 3262 K-DKDSTQKLLA 3272
Cdd:COG1196 820 EiDRETRERFLE 831
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
1176-1275 |
1.38e-25 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 103.90 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1176 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED- 1254
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1988774674 1255 VDVPHPDEKSIITYVSSLYDA 1275
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
1172-1278 |
1.55e-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: 103.91 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1172 MTAKEKLLLWSQRMTDGY-QGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQT--NLENLEQAFSVAEKDLGVTR 1248
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEfdKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1988774674 1249 -LLDPEDVDvpHPDEKSIITYVSSLYDAMPR 1278
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2399-3329 |
3.65e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 116.31 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2399 KAEKEAQELKL-KMQEEVSKREIAAVDAEKQKTNIQL------ELQELKN-LSEQQIKDKSQQVDEALHSRTKIEEEIRL 2470
Cdd:TIGR02168 171 KERRKETERKLeRTRENLDRLEDILNELERQLKSLERqaekaeRYKELKAeLRELELALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2471 IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALE 2550
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2551 DLEKLrmQAEEAERQVKQAEIEKEKQikvaheaAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQ 2630
Cdd:TIGR02168 331 KLDEL--AEELAELEEKLEELKEELE-------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2631 QEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAqeeaekqkeeaereakKRAKAEESALKQKEMAEEELER 2710
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE----------------ELEEELEELQEELERLEEALEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2711 QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDeLYRLKNEVAAAQQQRKQLED---ELAKVRS--EMDILIQLK 2785
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEG-FSEGVKALLKNQSGLSGILGvlsELISVDEgyEAAIEAALG 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2786 TKAEKETMSNTEKSKQLLEA--EAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRA--------EAERILKEKLAA 2855
Cdd:TIGR02168 545 GRLQAVVVENLNAAKKAIAFlkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAkdlvkfdpKLRKALSYLLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2856 ISEATRLKTEAEIALKEKEAEN------ERLRRQAedeayqrkaledqasqhkqeieekiVQLKKSSEAEMERqkaivdd 2929
Cdd:TIGR02168 625 VLVVDDLDNALELAKKLRPGYRivtldgDLVRPGG-------------------------VITGGSAKTNSSI------- 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2930 tLKQRRvveeEIRILKLNFEKASSGKLDLELELNKLKNIADEtqqskirAEEEAEKLRKLALEEEKRRREAEEKVKKIAA 3009
Cdd:TIGR02168 673 -LERRR----EIEELEEKIEELEEKIAELEKALAELRKELEE-------LEEELEQLRKELEELSRQISALRKDLARLEA 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3010 AEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQqiedsitQKKLKEEYE 3089
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-------LDELRAELT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3090 KAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEaakraqaEAAALMQKQQAD 3169
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-------LEALLNERASLE 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3170 TEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDdavKQRGQVEEElfkVKVQMEELLKLK 3249
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID---NLQERLSEE---YSLTLEEAEALE 960
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3250 NKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEdaarlsveaqeaarLRQIAE--DDLNQQRALAEKMLKEKMQAIQEA 3327
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKELGPVNLAAIEE--------------YEELKEryDFLTAQKEDLTEAKETLEEAIEEI 1026
|
..
gi 1988774674 3328 SR 3329
Cdd:TIGR02168 1027 DR 1028
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
1160-1275 |
8.19e-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: 102.50 E-value: 8.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1160 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 1239
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774674 1240 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1275
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
1060-1157 |
1.04e-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: 101.24 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1060 KTFTKWVNKHLIKA-QRHVTDLYEDLRDGHNLISLLEVLSGETLPREK---GRMRFHKLQNVQIALDFLRHRQVKLVNIR 1135
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1988774674 1136 NDDIADGnPKLTLGLIWTIILH 1157
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2532-3474 |
1.29e-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: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2532 KRKSEAEK--EAAKQKQKALED-LEKLRMQAEEAERQVKQAEieKEKQIKVAHEAAQKS-AAAELQSKHmsfaEKTSKLE 2607
Cdd:TIGR02168 172 ERRKETERklERTRENLDRLEDiLNELERQLKSLERQAEKAE--RYKELKAELRELELAlLVLRLEELR----EELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2608 ESLKQehgavlqLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREA 2687
Cdd:TIGR02168 246 EELKE-------AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2688 KKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQL 2767
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2768 EDELAKVRSEMDiliQLKTKAEKETmsnTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAER 2847
Cdd:TIGR02168 399 NNEIERLEARLE---RLEDRRERLQ---QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2848 ILKEKLAAISEATRLKTEAEIAlkekeaenERLRRQAEDEAYQRKALEDQASQHKQEIEE--KIVQLKKSSEAEME---- 2921
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSL--------ERLQENLEGFSEGVKALLKNQSGLSGILGVlsELISVDEGYEAAIEaalg 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2922 -RQKAIVDDTLKQrrvVEEEIRILKlnfeKASSGKLDLeLELNKLKniADETQQSKIRAEEEAEKLRKLALEEEKRRREA 3000
Cdd:TIGR02168 545 gRLQAVVVENLNA---AKKAIAFLK----QNELGRVTF-LPLDSIK--GTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3001 EEKVKKIAAAEEEAARQRKAaleeLERLRKKAEEARKQKDEADKEAEKQIVVAqqaaqkcsAAEQQVQSVLAQQIEdsit 3080
Cdd:TIGR02168 615 RKALSYLLGGVLVVDDLDNA----LELAKKLRPGYRIVTLDGDLVRPGGVITG--------GSAKTNSSILERRRE---- 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3081 qkkLKEeyekakklakeaeaakekaereaalLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAA 3160
Cdd:TIGR02168 679 ---IEE-------------------------LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3161 ALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKV 3240
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3241 QMEELLKLKNKIEEENQRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSVEaqeaarlrqiaeddLNQQRALAEKM---- 3316
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESL-ERRIAATERRLEDLEEQIEELSEDIESLAAE--------------IEELEELIEELesel 875
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3317 ---LKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKsLEVERKRQLEIMAEAERLRLQ 3393
Cdd:TIGR02168 876 ealLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLE 954
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3394 VsqlseaqarAEEEAKKFKKQADKVATRLHETEIATQE----KMTVVErlEFERLNT-----SKEADDLRKAIADLENEK 3464
Cdd:TIGR02168 955 E---------AEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAIE--EYEELKErydflTAQKEDLTEAKETLEEAI 1023
|
970
....*....|
gi 1988774674 3465 ARLKKEAEEL 3474
Cdd:TIGR02168 1024 EEIDREARER 1033
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2780-3613 |
1.32e-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: 114.68 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2780 ILIQLKtKAEKETMSNTEKSKQLLEAEA-AKMKDLAEEASR--LRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAI 2856
Cdd:pfam02463 137 FLVQGG-KIEIIAMMKPERRLEIEEEAAgSRLKRKKKEALKklIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2857 SEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKalEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIvddtlkqrrv 2936
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE--EIESSKQEIEKEEEKLAQVLKENKEEEKEKKL---------- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2937 VEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAAR 3016
Cdd:pfam02463 284 QEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3017 QRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQkcsaaEQQVQSVLAQQIEDSITQKKLKEEyekakkLAK 3096
Cdd:pfam02463 364 LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK-----EAQLLLELARQLEDLLKEEKKEEL------EIL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3097 EAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHK 3176
Cdd:pfam02463 433 EEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3177 K-LAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEEL-------FKVKVQMEELLKL 3248
Cdd:pfam02463 513 LaLIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTElplgarkLRLLIPKLKLPLK 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3249 KNKIEEENQRLIKKDKDSTqKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEAS 3328
Cdd:pfam02463 593 SIAVLEIDPILNLAQLDKA-TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3329 RLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERL--RLQVSQLSEAQARAEE 3406
Cdd:pfam02463 672 TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKinEELKLLKQKIDEEEEE 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3407 EAKKFKKQADKVATRLHETEiatQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQ 3486
Cdd:pfam02463 752 EEKSRLKKEEKEEEKSELSL---KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEE 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3487 KKIEHEKtvlqqtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKtLQATMDAALSKQKE 3566
Cdd:pfam02463 829 KIKEEEL---------EELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKL-KDELESKEEKEKEE 898
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 1988774674 3567 AEEEMLRKQKEMQELERQRLEQERI--LAEENQKLREKLQQLEDAQKDQ 3613
Cdd:pfam02463 899 KKELEEESQKLNLLEEKENEIEERIkeEAEILLKYEEEPEELLLEEADE 947
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2796-3471 |
1.49e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 114.26 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2796 TEKSKQL--LEAEAAKmkdlaeeASRLRAISEEAKhQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEK 2873
Cdd:COG1196 196 GELERQLepLERQAEK-------AERYRELKEELK-ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2874 EAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAivdDTLKQRRVVEEEIRILKLNFEKASS 2953
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE---ELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2954 GKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLrkkaE 3033
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL----E 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3034 EARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLR 3113
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3114 QQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAaLMQKQQADTEMAKHKKLAEQTLKQKFQVEQEL 3193
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA-LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3194 TKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNK-IEEENQRLIKKDKDSTQKLLA 3272
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRrAVTLAGRLREVTLEGEGGSAG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3273 EEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLL 3352
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3353 EDKQLMQQRLEEETEEYHKSLEVErkrqlEIMAEAERLRLQVSQLSeaqaraeeeakkfkkqadKVATRlheteiATQEK 3432
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLE-----ELERELERLEREIEALG------------------PVNLL------AIEEY 790
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1988774674 3433 MTVVERLEF--ERLNT-SKEADDLRKAIADLENEKARLKKEA 3471
Cdd:COG1196 791 EELEERYDFlsEQREDlEEARETLEEAIEEIDRETRERFLET 832
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
1178-1273 |
1.58e-24 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 101.07 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1178 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED-VD 1256
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1988774674 1257 VPHPDEKSIITYVSSLY 1273
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2685-3558 |
5.13e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 112.46 E-value: 5.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2685 REAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKltaeQELIRLRADFDNAEQQRSL-----LEDELYRLKNEVAA 2759
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKA----ERYKELKAELRELELALLVlrleeLREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2760 AQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtmsntekskqlLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAA 2839
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2840 RQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHkQEIEEKIVQLKKSSEAE 2919
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL-ETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2920 MERQKAIvDDTLKQ--RRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRR 2997
Cdd:TIGR02168 399 NNEIERL-EARLERleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2998 REAEEKVKKIaaaeeeaaRQRKAALEEL-ERLRKKAEEARKQKDEADKEAEKQIVVAQQ--AAQKCSAAeqqVQSVLAQQ 3074
Cdd:TIGR02168 478 DAAERELAQL--------QARLDSLERLqENLEGFSEGVKALLKNQSGLSGILGVLSELisVDEGYEAA---IEAALGGR 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3075 IEDSITQKKlkeeyekAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKR 3154
Cdd:TIGR02168 547 LQAVVVENL-------NAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3155 AQAEAAALMQKQQADTEMAKHKK-------LAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQ 3227
Cdd:TIGR02168 620 YLLGGVLVVDDLDNALELAKKLRpgyrivtLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKA 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3228 RGQVEEELfkvkVQMEELLKLKNKIEEENQRLIkkdkDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLN 3307
Cdd:TIGR02168 700 LAELRKEL----EELEEELEQLRKELEELSRQI----SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3308 QQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKL---LEDKQLMQQRLEEETEEYHKSLEVERKRQLEIM 3384
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3385 AEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEK 3464
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3465 ARLKKEAEELQnkskemadaqqKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFE----------EEVKKAKA 3534
Cdd:TIGR02168 932 EGLEVRIDNLQ-----------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaiEEYEELKE 1000
|
890 900
....*....|....*....|....
gi 1988774674 3535 LKDEQERQKQQMEQEKKTLQATMD 3558
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEAIE 1024
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
1176-1276 |
5.31e-24 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 99.46 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1176 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPEDV 1255
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1988774674 1256 DVPHPDEKSIITYVSSLYDAM 1276
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
1057-1160 |
6.42e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 99.28 E-value: 6.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1057 VQKKTFTKWVNKHLIKAQRH--VTDLYEDLRDGHNLISLLEVLSGETLP-REKGRMRFHKLQNVQIALDFLRHRQ-VKLV 1132
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1988774674 1133 NIRNDDIADGNPKLTLGLIWTIILHFQI 1160
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2258-2852 |
1.02e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.57 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2258 LKEQLAQEKKLLEEIEQNKDKVDECQKyakayidTIKDYELQLVAYKAQVEplvsplkktKLDSASDNIIQEYVTLRTRY 2337
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEA-------ELAELEAELEELRLELE---------ELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2338 SELmtltSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSK 2417
Cdd:COG1196 298 ARL----EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2418 REiAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAA 2497
Cdd:COG1196 374 LA-EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2498 EA-EKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQ 2576
Cdd:COG1196 453 ELeEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2577 IKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKqehgavlqlQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAL 2656
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK---------AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2657 RLRLQAEDEAHKKTLAQEEAEKQKEEAERE-AKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRAD 2735
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLEaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2736 fdnAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAE 2815
Cdd:COG1196 684 ---LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1988774674 2816 EASRLRAISEEAKhqRQI---------AEEEAARQRAEAERILKEK 2852
Cdd:COG1196 761 DLEELERELERLE--REIealgpvnllAIEEYEELEERYDFLSEQR 804
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
1173-1273 |
1.39e-23 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 98.27 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 1252
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1988774674 1253 EDV---DVphPDEKSIITYVSSLY 1273
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2471-3367 |
1.45e-23 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 111.22 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2471 IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQ---------DEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEA 2541
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEetenlaeliIDLEELKLQELKLKEQAKKALEYYQLKEKLELEE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2542 AKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHE-------AAQKSAAAELQSKHMSFAEKTSKLEESLKQEh 2614
Cdd:pfam02463 224 EYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEeklaqvlKENKEEEKEKKLQEEELKLLAKEEEELKSEL- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2615 gavLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEdeahkktlaqeeaekqkeeaerEAKKRAKAE 2694
Cdd:pfam02463 303 ---LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE----------------------IKREAEEEE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2695 ESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKV 2774
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2775 RSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKhqRQIAEEEAARQRAEAERILKEKLA 2854
Cdd:pfam02463 438 SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS--RQKLEERSQKESKARSGLKVLLAL 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2855 AISEATRLKTEAEIALKEKEAENERLRRQ---AEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTL 2931
Cdd:pfam02463 516 IKDGVGGRIISAHGRLGDLGVAVENYKVAistAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIA 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2932 KQRRVVE-EEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKiaAA 3010
Cdd:pfam02463 596 VLEIDPIlNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL--TK 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3011 EEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQaAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEK 3090
Cdd:pfam02463 674 ELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE-AEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3091 AKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADT 3170
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3171 EMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQrgQVEEELFKVKVQMEELLKLKN 3250
Cdd:pfam02463 833 EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE--SKEEKEKEEKKELEEESQKLN 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3251 KIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAArlSVEAQEAARLRQIAEDDLNQQrALAEKMLKEKMQAIQEASRL 3330
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEAD--EKEKEENNKEEEEERNKRLLL-AKEELGKVNLMAIEEFEEKE 987
|
890 900 910
....*....|....*....|....*....|....*..
gi 1988774674 3331 KAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETE 3367
Cdd:pfam02463 988 ERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
1160-1275 |
1.59e-23 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 98.99 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1160 ISDIQVngqsEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSV 1239
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774674 1240 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1275
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2623-3619 |
5.16e-23 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 109.53 E-value: 5.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2623 EAERLKKQQEDAENSREEAEKELEKWRQKANEALR------------LRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKR 2690
Cdd:NF041483 23 EMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRslasrpaydgadIGYQAEQLLRNAQIQADQLRADAERELRDARAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2691 AK------AEESALKQKEMAEEELERQRKIAESTAQQKLTAEQ---------ELIRLRADfdnaEQQRSLLEDELYRLKN 2755
Cdd:NF041483 103 TQrilqehAEHQARLQAELHTEAVQRRQQLDQELAERRQTVEShvnenvawaEQLRARTE----SQARRLLDESRAEAEQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2756 EVAAA--------QQQRKQLEDELAKVRSEMD-ILIQLKTKAEK----------ETMSNTEKSKQLLEAEAAKMKDLAEE 2816
Cdd:NF041483 179 ALAAAraeaerlaEEARQRLGSEAESARAEAEaILRRARKDAERllnaastqaqEATDHAEQLRSSTAAESDQARRQAAE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2817 ASR------------LRAISEEAKHQRQIAEEEAARQRAEAE-------RILKEKLA-----AISEATRLKTEAEIALKE 2872
Cdd:NF041483 259 LSRaaeqrmqeaeeaLREARAEAEKVVAEAKEAAAKQLASAEsaneqrtRTAKEEIArlvgeATKEAEALKAEAEQALAD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2873 KEAENERLRRQAEDEAyQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRilKLNFEKAS 2952
Cdd:NF041483 339 ARAEAEKLVAEAAEKA-RTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEAD--RLRGEAAD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2953 SGkldlelelNKLKNIA-DETQQSKIRA---EEEAEKLRKLAleeekrrreaeekvkkiaaaeeeaARQRKAALEELERL 3028
Cdd:NF041483 416 QA--------EQLKGAAkDDTKEYRAKTvelQEEARRLRGEA------------------------EQLRAEAVAEGERI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3029 RKKA-EEARKQKDEADKEAEKQIVVAQQAAQKC-SAAEQQVQSVLAQQIEDSITQKKLKEEyekakklakeaeaakekae 3106
Cdd:NF041483 464 RGEArREAVQQIEEAARTAEELLTKAKADADELrSTATAESERVRTEAIERATTLRRQAEE------------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3107 reaaLLRQQAEEAERQKTaaeeeaanqaKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQ-QADTEMAKHKKLAEQTLKq 3185
Cdd:NF041483 525 ----TLERTRAEAERLRA----------EAEEQAEEVRAAAERAARELREETERAIAARQaEAAEELTRLHTEAEERLT- 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3186 kfQVEQELTKVKlklDETDKQKSVLDEELQRLKDEVDDAVKQ-RGQVEEELFKVKVQMEE------------LLKLKNKI 3252
Cdd:NF041483 590 --AAEEALADAR---AEAERIRREAAEETERLRTEAAERIRTlQAQAEQEAERLRTEAAAdasaaraegenvAVRLRSEA 664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3253 EEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQ-EAARLRQIAEDDLNQQRALAEkmlKEKMQAIQEASRLK 3331
Cdd:NF041483 665 AAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQeEAARRRREAEETLGSARAEAD---QERERAREQSEELL 741
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3332 AEAemlQKQKDLAQEQAQKLLED------------KQLMQQ------RLEEETEEYHKSLE------VERKRQlEIMAEA 3387
Cdd:NF041483 742 ASA---RKRVEEAQAEAQRLVEEadrratelvsaaEQTAQQvrdsvaGLQEQAEEEIAGLRsaaehaAERTRT-EAQEEA 817
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3388 ERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAtqEKMTVVERLefeRLNTSKEADDLR----KAIADLENE 3463
Cdd:NF041483 818 DRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVS--EAIAEAERL---RSDASEYAQRVRteasDTLASAEQD 892
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3464 KARLKKEAEELQNKSKEMADAQQKKIEHEKTVlqqtfmtekemllkkekliEDEKKRLESQFEEEVKKAKALKDEQERQK 3543
Cdd:NF041483 893 AARTRADAREDANRIRSDAAAQADRLIGEATS-------------------EAERLTAEARAEAERLRDEARAEAERVRA 953
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3544 QQMEQEKKTLQATMDAALSKQKEAEEEMLRKQkemQELERQRLEQERILAE---ENQKLREKLQQ-----LEDAQKDQHT 3615
Cdd:NF041483 954 DAAAQAEQLIAEATGEAERLRAEAAETVGSAQ---QHAERIRTEAERVKAEaaaEAERLRTEAREeadrtLDEARKDANK 1030
|
....
gi 1988774674 3616 RETD 3619
Cdd:NF041483 1031 RRSE 1034
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
1173-1277 |
5.86e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 96.78 E-value: 5.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQRMTDGYqGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 1252
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1988774674 1253 EDVDVPHPDEKSIITYVSSLYDAMP 1277
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2136-2896 |
4.61e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 106.29 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2136 VKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRE 2215
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2216 LEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKD 2295
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2296 YELQLVAYKAQVEPLVSplKKTKLDSASDNIIQEYVTLRTRYSELMtltsqyikfITDTQRRLDDEEKAAEKLKAEErkk 2375
Cdd:TIGR02168 391 LELQIASLNNEIERLEA--RLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEEL--- 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2376 mAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL--KLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKS-- 2451
Cdd:TIGR02168 457 -ERLEEALEELREELEEAEQALDAAERELAQLqaRLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEgy 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2452 -QQVDEALHSR-----TKIEEEIRLIRIQLETTEKQKYTAeSELKQLRDRAAEAEKLRKLAQ------------------ 2507
Cdd:TIGR02168 536 eAAIEAALGGRlqavvVENLNAAKKAIAFLKQNELGRVTF-LPLDSIKGTEIQGNDREILKNiegflgvakdlvkfdpkl 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2508 -----------------DEAEKLRKQVSEE---------------------------TQKKRQAEEELKRKSEAEKEAAK 2543
Cdd:TIGR02168 615 rkalsyllggvlvvddlDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELEEKIA 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2544 QKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIkvaheaaqksaaaelqskhmsfaektSKLEESLKQEHGAVLQLQQE 2623
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQI--------------------------SALRKDLARLEAEVEQLEER 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2624 AERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAhkktlaqeEAEKQKEEAEREAKKRAKAEESALKQK-- 2701
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI--------EQLKEELKALREALDELRAELTLLNEEaa 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2702 ------EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVR 2775
Cdd:TIGR02168 821 nlrerlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2776 SEMDILIQLKTKAEKETMSNTEKSKQL-LEAEAAKMKdLAEEASRLRA----ISEEAKHQRQIAEEEAARQRAEAERiLK 2850
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLeLRLEGLEVR-IDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKR-LE 978
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 1988774674 2851 EKLAAISEATRLkteaeiALKEKEAENER---LRRQAEDEAYQRKALED 2896
Cdd:TIGR02168 979 NKIKELGPVNLA------AIEEYEELKERydfLTAQKEDLTEAKETLEE 1021
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
1056-1161 |
7.12e-22 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 94.38 E-value: 7.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1056 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 1132
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1988774674 1133 NIRNDDIADGNPKLTLGLIWTIILHFQIS 1161
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
1056-1161 |
1.09e-21 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 94.00 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1056 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 1132
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1988774674 1133 NIRNDDIADGNPKLTLGLIWTIILHFQIS 1161
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2836-3558 |
2.06e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.86 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2836 EEAA------RQRAEAERilkeKLAAISEatRLkTEAEIALKEKEAENERLRRQAEDeayQRKALEDQASQHKQEIEEKI 2909
Cdd:COG1196 162 EEAAgiskykERKEEAER----KLEATEE--NL-ERLEDILGELERQLEPLERQAEK---AERYRELKEELKELEAELLL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2910 VQLKKSsEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKl 2989
Cdd:COG1196 232 LKLREL-EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2990 aleeekrrreaeekvkkiaaaeeeaarQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQS 3069
Cdd:COG1196 310 ---------------------------RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3070 VLAQQIEDSITQKKLKEEyekakklakeaeaakekaereaaLLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEF 3149
Cdd:COG1196 363 AEEALLEAEAELAEAEEE-----------------------LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3150 EAakraqaeaaalmQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRG 3229
Cdd:COG1196 420 EE------------ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3230 QveeelfkvKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQ 3309
Cdd:COG1196 488 E--------AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3310 RALAEKMLKEKM--QAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEA 3387
Cdd:COG1196 560 AAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3388 ERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARL 3467
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3468 KKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLiEDEKKRLESQFE----------EEVKKAKALKD 3537
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL-ERELERLEREIEalgpvnllaiEEYEELEERYD 798
|
730 740
....*....|....*....|.
gi 1988774674 3538 EQERQKQQMEQEKKTLQATMD 3558
Cdd:COG1196 799 FLSEQREDLEEARETLEEAIE 819
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2238-2713 |
2.23e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.45 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2238 ADAKQRQEKIQAVPITDSKTLKE----QLAQEKKLLEEIE---QNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPL 2310
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEaaekKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2311 VSPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDD-EEKAAEKLKAEERKKMAE---MQAELDKQ 2386
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEaKKKAEEAKKADEAKKKAEeakKKADEAKK 1504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2387 KQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEE 2466
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2467 EIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSeetQKKRQAEEELKRKSEAEKEAAKQKQ 2546
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE---QLKKKEAEEKKKAEELKKAEEENKI 1661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2547 KAledlEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKsaaaelqskhmsfAEKTSKLEESLKQEHGAVlqlqQEAER 2626
Cdd:PTZ00121 1662 KA----AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-------------AEEAKKAEELKKKEAEEK----KKAEE 1720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2627 LKKQQEDAENSREEAEKELEKWRQKANEAlrlrlqAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEE 2706
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEA------KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
....*..
gi 1988774674 2707 ELERQRK 2713
Cdd:PTZ00121 1795 EVDKKIK 1801
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3016-3612 |
3.54e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.09 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3016 RQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSvLAQQIEDsitqkkLKEEYEKAKKLA 3095
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE-LELELEE------AQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3096 KEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKH 3175
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3176 KKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEE 3255
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3256 NQRLIKKDKDSTQKLLAEEAEnmrklaEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAE 3335
Cdd:COG1196 458 EEALLELLAELLEEAALLEAA------LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3336 MLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQA 3415
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3416 DKVATRLHETEIATQEkmtVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTV 3495
Cdd:COG1196 612 DARYYVLGDTLLGRTL---VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3496 LQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLrkQ 3575
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL--E 766
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1988774674 3576 KEMQELERQR----------LEQERILAEENQKLREKLQQLEDAQKD 3612
Cdd:COG1196 767 RELERLEREIealgpvnllaIEEYEELEERYDFLSEQREDLEEARET 813
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2351-3397 |
6.22e-21 |
|
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: 102.56 E-value: 6.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2351 ITDTQRRLDDEEKAAEKLKAE---------------------------ERKKMAEMQAELDKQKQLAEAHAKAIAKAEKE 2403
Cdd:pfam01576 105 IQDLEEQLDEEEAARQKLQLEkvtteakikkleedillledqnsklskERKLLEERISEFTSNLAEEEEKAKSLSKLKNK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2404 AQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKnlseQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKY 2483
Cdd:pfam01576 185 HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ----EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2484 TAESELKQLRDRAAEAEK---LRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKlrmqAE 2560
Cdd:pfam01576 261 NALKKIRELEAQISELQEdleSERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKK----AL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2561 EAERQVKQAEIEKEKQikvaheaAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREE 2640
Cdd:pfam01576 337 EEETRSHEAQLQEMRQ-------KHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2641 AEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQrkiaestAQ 2720
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE-------TR 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2721 QKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtmsnTEKSK 2800
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE----LEALT 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2801 QLLEAEAAKMKDLAEEASRLRA----ISEEAKHQRQIAEEEAARQRaEAERILKEKLAAISEATRLKTEAEIALKEKEAE 2876
Cdd:pfam01576 559 QQLEEKAAAYDKLEKTKNRLQQelddLLVDLDHQRQLVSNLEKKQK-KFDQMLAEEKAISARYAEERDRAEAEAREKETR 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2877 NERLRRQAEDEAYQRKALEDQASQHKQEIEEkIVQLKKS---SEAEMERQKAIVDDTLKQRRVVEEEiriLKLNFEKASS 2953
Cdd:pfam01576 638 ALSLARALEEALEAKEELERTNKQLRAEMED-LVSSKDDvgkNVHELERSKRALEQQVEEMKTQLEE---LEDELQATED 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2954 GKLDLELELNKLKNIADETQQSKiraEEEAEKLRKLALeeekrrreaeEKVKKIAAAEEEAARQRKAALE-------ELE 3026
Cdd:pfam01576 714 AKLRLEVNMQALKAQFERDLQAR---DEQGEEKRRQLV----------KQVRELEAELEDERKQRAQAVAakkklelDLK 780
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3027 RLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEdsiTQKKLKeeyekakklakeaeaakekae 3106
Cdd:pfam01576 781 ELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKE---SEKKLK--------------------- 836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3107 reaallrqqAEEAErqktaaeeeaanQAKAQED---AERLRKEAEFEaakraqaeaaalmqKQQADTEMAKHKKLAEQTL 3183
Cdd:pfam01576 837 ---------NLEAE------------LLQLQEDlaaSERARRQAQQE--------------RDELADEIASGASGKSALQ 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3184 KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKV---KVQMEELLK-LKNKIEEENQRL 3259
Cdd:pfam01576 882 DEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSesaRQQLERQNKeLKAKLQEMEGTV 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3260 IKKDKDSTQKLLAeeaenmrKLAEDAARLSVEAQEaarlRQIAEDDLNQqralAEKMLKEKMQAIQEASRlkaeaemlqk 3339
Cdd:pfam01576 962 KSKFKSSIAALEA-------KIAQLEEQLEQESRE----RQAANKLVRR----TEKKLKEVLLQVEDERR---------- 1016
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 3340 QKDLAQEQAQKL-LEDKQLMQQrLEEETEEYHKSLEVERK--RQLEIMAE-AERLRLQVSQL 3397
Cdd:pfam01576 1017 HADQYKDQAEKGnSRMKQLKRQ-LEEAEEEASRANAARRKlqRELDDATEsNESMNREVSTL 1077
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
1807-1873 |
7.09e-21 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 89.24 E-value: 7.09e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774674 1807 QLKPRNptTSIKGKLPIQAVCDFKQQEITVHKGDECALLNNSQPFKWKVLNRSGHEAMVPSVCFIVP 1873
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
1173-1273 |
8.32e-21 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 90.48 E-value: 8.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDP 1252
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1988774674 1253 EDVDV--PHPDEKSIITYVSSLY 1273
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
1174-1273 |
1.22e-20 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 89.93 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1174 AKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPE 1253
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1988774674 1254 D-VDVPHPDEKSIITYVSSLY 1273
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
1173-1272 |
1.63e-20 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 89.46 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINmgkvYQQTNLENLE----QAFSVAEKdLGVTR 1248
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVD----YESLDPLDIKennkKAFEAFAS-LGVPR 75
|
90 100
....*....|....*....|....*
gi 1988774674 1249 LLDPED-VDVPHPDEKSIITYVSSL 1272
Cdd:cd21255 76 LLEPADmVLLPIPDKLIVMTYLCQL 100
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2363-3603 |
2.77e-20 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 100.25 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2363 KAAEKLKAEERKKMAEMQ-AELD-KQKQLAE----------AHAKAIAKAEKEAQELKLKMQ--EEVSKREIAAVDAEKQ 2428
Cdd:pfam01576 10 KEEELQKVKERQQKAESElKELEkKHQQLCEeknalqeqlqAETELCAEAEEMRARLAARKQelEEILHELESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2429 KTNiqlELQELKNLSEQQIKDKSQQVDEALHSRTK--------------IEEEIRLIRIQLETTEKQKYTAESELKQLRD 2494
Cdd:pfam01576 90 RSQ---QLQNEKKKMQQHIQDLEEQLDEEEAARQKlqlekvtteakikkLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2495 RAAEAEKLRKLAQDEAEKLRKQVSE------ETQKKRQAEEELKRKSEAEKEAAKqkqkalEDLEKLRMQAEEAERQVKQ 2568
Cdd:pfam01576 167 NLAEEEEKAKSLSKLKNKHEAMISDleerlkKEEKGRQELEKAKRKLEGESTDLQ------EQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2569 AEIE-KEKQIKVAHEAAQKSAAaelQSKHMSFAEKTSKLEESLKQEHGAvlqlQQEAERLKKQ-QEDAENSREEAEKELE 2646
Cdd:pfam01576 241 KEEElQAALARLEEETAQKNNA---LKKIRELEAQISELQEDLESERAA----RNKAEKQRRDlGEELEALKTELEDTLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2647 KwrQKANEALRLRLQAEDEAHKKTLAqeeaekqkeeaerEAKKRAKAEESALKQK-----EMAEEELERQRKIAESTAQQ 2721
Cdd:pfam01576 314 T--TAAQQELRSKREQEVTELKKALE-------------EETRSHEAQLQEMRQKhtqalEELTEQLEQAKRNKANLEKA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2722 KLTAEQELIRLRADF-------DNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMS 2794
Cdd:pfam01576 379 KQALESENAELQAELrtlqqakQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2795 NTEKSKQLLEAEAAKMKDLAEE-------ASRLRAISEE-AKHQRQIAEEEAARQRAEaerilkeklaaiseatRLKTEA 2866
Cdd:pfam01576 459 LSKDVSSLESQLQDTQELLQEEtrqklnlSTRLRQLEDErNSLQEQLEEEEEAKRNVE----------------RQLSTL 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2867 EIALKEkeaenerLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEA--EMERQKAIVDDTLKQRRVVEEEIRIL 2944
Cdd:pfam01576 523 QAQLSD-------MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAydKLEKTKNRLQQELDDLLVDLDHQRQL 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2945 KLNFEKASSgKLDLELElnKLKNIADETQQSKIRAEEEAEKLRKLALEEEKrrreaeekvkkiaaaeeeaarqrkaALEE 3024
Cdd:pfam01576 596 VSNLEKKQK-KFDQMLA--EEKAISARYAEERDRAEAEAREKETRALSLAR-------------------------ALEE 647
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3025 LERLRKKAEEARKQKdEADKEaekQIVVAQQAAQKCSAAEQQVQSVLAQQIEDsitqkklkeeyekakklakeaeaakek 3104
Cdd:pfam01576 648 ALEAKEELERTNKQL-RAEME---DLVSSKDDVGKNVHELERSKRALEQQVEE--------------------------- 696
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3105 aereaalLRQQAEEAERQKTAAeeeaanqakaqEDAeRLRKEAEFEAAKRAQAeaaalmQKQQADTEMAKHKKlaEQTLK 3184
Cdd:pfam01576 697 -------MKTQLEELEDELQAT-----------EDA-KLRLEVNMQALKAQFE------RDLQARDEQGEEKR--RQLVK 749
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3185 QKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELlklknkieeenQRLIKKDK 3264
Cdd:pfam01576 750 QVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL-----------QRELEEAR 818
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3265 DSTQKLLAEEAENMRKLAedaarlSVEAQeaarLRQIAEDDLNQQRAlaekmlkeKMQAIQEASRLKAEAEMLQKQKDLA 3344
Cdd:pfam01576 819 ASRDEILAQSKESEKKLK------NLEAE----LLQLQEDLAASERA--------RRQAQQERDELADEIASGASGKSAL 880
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3345 QEQAQKLleDKQLMQqrLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHE 3424
Cdd:pfam01576 881 QDEKRRL--EARIAQ--LEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQE 956
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3425 TEIATQEKmtvverleferlntskeaddLRKAIADLEnekARLKKEAEELQNKSKEMADAQQKKIEHEKTVlqqtfmteK 3504
Cdd:pfam01576 957 MEGTVKSK--------------------FKSSIAALE---AKIAQLEEQLEQESRERQAANKLVRRTEKKL--------K 1005
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3505 EMLLkkekliedekkrlesQFEEEVKKAKALKDEQERQKQQMEQEKKTLQatmdaalskqkEAEEEMLRKQKEMQELERQ 3584
Cdd:pfam01576 1006 EVLL---------------QVEDERRHADQYKDQAEKGNSRMKQLKRQLE-----------EAEEEASRANAARRKLQRE 1059
|
1290 1300
....*....|....*....|..
gi 1988774674 3585 ---RLEQERILAEENQKLREKL 3603
Cdd:pfam01576 1060 lddATESNESMNREVSTLKSKL 1081
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
1177-1274 |
3.66e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 88.94 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1177 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD-PEDV 1255
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1988774674 1256 DVPHPDEKSIITYVSSLYD 1274
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2361-2982 |
6.71e-20 |
|
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: 98.99 E-value: 6.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2361 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVS------KREIAAVDAEKQKT--NI 2432
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrvKEKIGELEAEIASLerSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2433 QLELQELKNLSEQQIKDKSQqVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 2512
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAE-IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2513 LRKQVSEETQKKRQAEEELKRKSE-------------AEKEAAKQKQKALED-LEKLRMQAEEAERQVKQ--AEIEKEKQ 2576
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEelqrlseeladlnAAIAGIEAKINELEEeKEDKALEIKKQEWKLEQlaADLSKYEQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2577 IKVA------------HEAAQKSAAAELQSKHMSFAEKTSK-----LEESLKQEHGAVLQLQQEAERLKKQQEDAENSR- 2638
Cdd:TIGR02169 470 ELYDlkeeydrvekelSKLQRELAEAEAQARASEERVRGGRaveevLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRl 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2639 --------EEAEKELEKWRQ-KANEA--LRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKA-------------E 2694
Cdd:TIGR02169 550 nnvvveddAVAKEAIELLKRrKAGRAtfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlvvedI 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2695 ESALKQK------EMAEEELERQRKI------AESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 2762
Cdd:TIGR02169 630 EAARRLMgkyrmvTLEGELFEKSGAMtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQ 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2763 QRKQLEDELAKVRSEMDILIQLKTKAE---KETMSNTEKSKQLLEAEAAKMKDLAEEASRLraisEEAKHQRQIAEEEAA 2839
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKerlEELEEDLSSLEQEIENVKSELKELEARIEEL----EEDLHKLEEALNDLE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2840 RQRAEAE--------RILKEKLAAISEATRlktEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQ 2911
Cdd:TIGR02169 786 ARLSHSRipeiqaelSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 2912 LKKsSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEE 2982
Cdd:TIGR02169 863 KEE-LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
1058-1158 |
9.95e-20 |
|
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: 87.25 E-value: 9.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1058 QKKTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLRHRQVKLVN 1133
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1988774674 1134 IRNDDIADGNPKLTLGLIWTIILHF 1158
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2344-3048 |
2.48e-19 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 96.96 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2344 TSQYIKFITDTQRRLDDEEKAAEKLKAE---ERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREi 2420
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSLHGKAELLTLRsqlLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2421 AAVDAEKQKTNIQLELQELKNLsEQQIKDKSQQVDEALHSRTKIEEEIRLIRIqlettEKQKYTAESELK-QLRDRAAEA 2499
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRAQ-EAVLEETQERINRARKAAPLAAHIKAVTQI-----EQQAQRIHTELQsKMRSRAKLL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2500 EKLRKLAQDEAEKLRKQVSEETQkkRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKV 2579
Cdd:TIGR00618 328 MKRAAHVKQQSSIEEQRRLLQTL--HSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2580 AHEAAQksAAAELQskhmsfaektsklEESLKQEHGAVLQLQQEAerlkkQQEDAENSREEAEKELEKWRQKANEALRLR 2659
Cdd:TIGR00618 406 QREQAT--IDTRTS-------------AFRDLQGQLAHAKKQQEL-----QQRYAELCAAAITCTAQCEKLEKIHLQESA 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2660 LQAEDEAHK-KTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRK-IAESTAQQKLTAEQELIRLRADFD 2737
Cdd:TIGR00618 466 QSLKEREQQlQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdNPGPLTRRMQRGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2738 NAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEA 2817
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2818 SRLRAISEEAKHQRQIAEEEAARQRAE---AERILKEKLAAISEATRLKTEA-EIALKEKEAENERLRRQAEDEAYQRKA 2893
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQltlTQERVREHALSIRVLPKELLASrQLALQKMQSEKEQLTYWKEMLAQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2894 LEDQ------ASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvveEEIRILKLNFEKASSGKLDLELELNKLKN 2967
Cdd:TIGR00618 706 LRELethieeYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR---TVLKARTEAHFNNNEEVTAALQTGAELSH 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2968 IADETqQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQ--------RKAALEELERLRKKAEEARKQK 3039
Cdd:TIGR00618 783 LAAEI-QFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEqflsrleeKSATLGEITHQLLKYEECSKQL 861
|
....*....
gi 1988774674 3040 DEADKEAEK 3048
Cdd:TIGR00618 862 AQLTQEQAK 870
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2695-3608 |
2.67e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 97.06 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2695 ESALKQKEMAEEELERQRKIAESTAQQkltaeqeLIRLRADFDNAEQQRSLL----EDELYRLKNEVAAAQQQRKQLEDE 2770
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQ-------LERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2771 LAKVRSEMDILIQLKTKAEKETmsntEKSKQLLEAEAAKMKDLAEEasrlraisEEAKHQRQIAEEEAarQRAEAERILK 2850
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRL----EEIEQLLEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2851 EKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHK-------QEIEEKIVQLKKSSEAEMERQ 2923
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeledlrAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2924 KAIvDDTLKQRRVVEEEIRILKLNFEKASSGKLDLElelNKLKNIADETQQSKIRAEEEAEKLRKLaleeekrrreaEEK 3003
Cdd:TIGR02169 392 EKL-EKLKREINELKRELDRLQEELQRLSEELADLN---AAIAGIEAKINELEEEKEDKALEIKKQ-----------EWK 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3004 VKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEAdkEAEKQIVvaqQAAQKCSAAEQQVQSVLAQQIEDSITQ-K 3082
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA--EAQARAS---EERVRGGRAVEEVLKASIQGVHGTVAQlG 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3083 KLKEEYEKAKKLAKEAeaakekaereaallRQQAEEAErqktaaeeeaanqakAQEDAERLrkeaefeaakraqaeaaal 3162
Cdd:TIGR02169 532 SVGERYATAIEVAAGN--------------RLNNVVVE---------------DDAVAKEA------------------- 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3163 mqkqqadTEMAKHKKLAEQTLkqkfqveqeLTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKV-- 3240
Cdd:TIGR02169 564 -------IELLKRRKAGRATF---------LPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVve 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3241 QMEELLKLKNKIeeenqRLIKKDKDSTQK--LLAEEAENMRKLAEDAARLSVEAQE-AARLR--QIAEDDLNQQRALAEK 3315
Cdd:TIGR02169 628 DIEAARRLMGKY-----RMVTLEGELFEKsgAMTGGSRAPRGGILFSRSEPAELQRlRERLEglKRELSSLQSELRRIEN 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3316 MLKEKMQAIQEASR----LKAEAEMLQKQkdlaQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLR 3391
Cdd:TIGR02169 703 RLDELSQELSDASRkigeIEKEIEQLEQE----EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3392 LQVSQLseAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEA 3471
Cdd:TIGR02169 779 EALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3472 EELQNKSKEMaDAQQKKIEhektvlqqtfmtekemllKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 3551
Cdd:TIGR02169 857 ENLNGKKEEL-EEELEELE------------------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774674 3552 tLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERIlAEENQKLREKLQQLED 3608
Cdd:TIGR02169 918 -RLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV-QAELQRVEEEIRALEP 972
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
1176-1272 |
2.88e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 85.83 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1176 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN----LENLEQAFSVAEKDLGVTRLLD 1251
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1988774674 1252 PEDVDVPHPDEKSIITYVSSL 1272
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2560-3617 |
3.16e-19 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 96.78 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2560 EEAERQVKQAEIEKEKQIKVAHEAAQKsaaaELQSKHMSFAEKTSKLEESLKQEHgavlQLQQEAERLKKQQEDAENSRE 2639
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELK----ELEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMRARLAARKQELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2640 EAEKELEKwrqkanealrlRLQAEDEAHKKTLAQeeaekqkeeaereaKKRAKAEESALKQkEMAEEELERQR-KIAEST 2718
Cdd:pfam01576 75 EILHELES-----------RLEEEEERSQQLQNE--------------KKKMQQHIQDLEE-QLDEEEAARQKlQLEKVT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2719 AQQKLTAEQELIRLRADFDNAEQ-QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILiQLKTKAEKETMSNTE 2797
Cdd:pfam01576 129 TEAKIKKLEEDILLLEDQNSKLSkERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDL-EERLKKEEKGRQELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2798 KSKQLLEAEAAkmkDLAEEASRLRAISEEAKHQRQIAEEE----------AARQRAEAERILKEKLAAISEATR------ 2861
Cdd:pfam01576 208 KAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEElqaalarleeETAQKNNALKKIRELEAQISELQEdleser 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2862 -LKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEkivqLKKSSEAEMERQKAIVDD-TLKQRRVVE- 2938
Cdd:pfam01576 285 aARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTE----LKKALEEETRSHEAQLQEmRQKHTQALEe 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2939 -----EEIRILKLNFEKAssgKLDLELELNKLKNIADETQQSKIRAEEEAEKLrklaleeekrrreaEEKVKKIAAAEEE 3013
Cdd:pfam01576 361 lteqlEQAKRNKANLEKA---KQALESENAELQAELRTLQQAKQDSEHKRKKL--------------EGQLQELQARLSE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3014 AARQRKAALEELERLRKKAEEARKQKDEADKEAEKqivvaqqAAQKCSAAEQQVQSvlAQQIEDSITQKKLKeeyekakk 3093
Cdd:pfam01576 424 SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK-------LSKDVSSLESQLQD--TQELLQEETRQKLN-------- 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3094 lakEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfeAAKRAQAEAAALMQKQQADTEMA 3173
Cdd:pfam01576 487 ---LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAG--TLEALEEGKKRLQRELEALTQQL 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3174 KHKKLAEQTL-KQKFQVEQELTKVKLKLDET--------DKQK---SVLDEE---LQRLKDEVDDAVKQRGQVEEELFKV 3238
Cdd:pfam01576 562 EEKAAAYDKLeKTKNRLQQELDDLLVDLDHQrqlvsnleKKQKkfdQMLAEEkaiSARYAEERDRAEAEAREKETRALSL 641
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3239 KVQMEELLKLKNKIEEENQRL------IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDdlnqqral 3312
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLraemedLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATED-------- 713
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3313 AEKMLKEKMQAiqeasrLKAEAEM-LQKQKDLAQEQAQKLLedKQLMQQRLEEETEEYHKSLEVERKRQLEImaEAERLR 3391
Cdd:pfam01576 714 AKLRLEVNMQA------LKAQFERdLQARDEQGEEKRRQLV--KQVRELEAELEDERKQRAQAVAAKKKLEL--DLKELE 783
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3392 LQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKmtvverleferLNTSKEADdlrKAIADLENEKARLKkea 3471
Cdd:pfam01576 784 AQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI-----------LAQSKESE---KKLKNLEAELLQLQ--- 846
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3472 EELQNKSKEMADAQQKKIEHEKTVLQQTfmTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 3551
Cdd:pfam01576 847 EDLAASERARRQAQQERDELADEIASGA--SGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTT 924
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 3552 TLQATMDAAlSKQKEAEEEMLRKQKE----MQELERQ-RLEQERILAeenqKLREKLQQLEDaQKDQHTRE 3617
Cdd:pfam01576 925 ELAAERSTS-QKSESARQQLERQNKElkakLQEMEGTvKSKFKSSIA----ALEAKIAQLEE-QLEQESRE 989
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2333-3263 |
5.36e-19 |
|
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: 96.27 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2333 LRTRYSELMTLTS-----QYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL 2407
Cdd:TIGR00606 171 LKQKFDEIFSATRyikalETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2408 KLKMQE-EVSKREIAAVDAE-KQKTNIQLELQELKNLSEQQIKDKSQQVDEAL------HSRTKIEEEIRLIRIQLETTE 2479
Cdd:TIGR00606 251 KNRLKEiEHNLSKIMKLDNEiKALKSRKKQMEKDNSELELKMEKVFQGTDEQLndlyhnHQRTVREKERELVDCQRELEK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2480 KQKytaeselkqlrdraaeaeKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEdleklrmQA 2559
Cdd:TIGR00606 331 LNK------------------ERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFE-------RG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2560 EEAERQVKQA-EIEKEKQIKVAHEAAQKsaAAELQSKHMSFAEKTSKLEESLKqehGAVLQLQQEAERLKKQQEDAENSR 2638
Cdd:TIGR00606 386 PFSERQIKNFhTLVIERQEDEAKTAAQL--CADLQSKERLKQEQADEIRDEKK---GLGRTIELKKEILEKKQEELKFVI 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2639 EEAE------KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEmaeeelERQR 2712
Cdd:TIGR00606 461 KELQqlegssDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH------TTTR 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2713 KIAESTAQQKLTAEQ-----------ELIRLRADFDNAEQqrslLEDELYRLKNEVaaaqqqrKQLEDELAKVRSEMDIL 2781
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEqirkiksrhsdELTSLLGYFPNKKQ----LEDWLHSKSKEI-------NQTRDRLAKLNKELASL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2782 IQLKTKAEKETMSNTEKSKQLLEA--EAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEA 2859
Cdd:TIGR00606 604 EQNKNHINNELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVC 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2860 TR-LKTEAEIALKEKEAENerLRRQAEDEayqRKALEDQASQHKQEIEEKIVqLKKSSEAEMERQKAIVDDTLKQRRVVE 2938
Cdd:TIGR00606 684 QRvFQTEAELQEFISDLQS--KLRLAPDK---LKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPELRNKLQKVN 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2939 EEIRILKLNFEKASS--GKLDLELELNKLKnIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAAR 3016
Cdd:TIGR00606 758 RDIQRLKNDIEEQETllGTIMPEEESAKVC-LTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQH 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3017 QRKAALEELERLRKKAEEARKQ----KDEADKEAEKQIVVAQQAAQKCSAAEQQVQ-SVLAQQIEDSITQKK-------- 3083
Cdd:TIGR00606 837 ELDTVVSKIELNRKLIQDQQEQiqhlKSKTNELKSEKLQIGTNLQRRQQFEEQLVElSTEVQSLIREIKDAKeqdsplet 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3084 -LKEEYEKAKKLAKEAEAAKEKAEREAALLRqqaeeaERQKTAAEEEAANQAKAQEDAERlrkeaefeaakraqaeaaal 3162
Cdd:TIGR00606 917 fLEKDQQEKEELISSKETSNKKAQDKVNDIK------EKVKNIHGYMKDIENKIQDGKDD-------------------- 970
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3163 mQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEvdDAVKqrgQVEEELFKVKVQM 3242
Cdd:TIGR00606 971 -YLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRE--NELK---EVEEELKQHLKEM 1044
|
970 980
....*....|....*....|....*
gi 1988774674 3243 EELLKLKNKIE----EENQRLIKKD 3263
Cdd:TIGR00606 1045 GQMQVLQMKQEhqklEENIDLIKRN 1069
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2119-2866 |
7.18e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.52 E-value: 7.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2119 LKQYEDCLREVHTVPSDVKEVETYRAKLKKMRTEAEDE----QPVFDSLEEELKKAS-----AVSDKMVRVHSER---DV 2186
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRleeiEQLLEELNKKIKDLGeeeqlRVKEKIGELEAEIaslER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2187 ELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQAVPITDSKTLKEQLAQEK 2266
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2267 KLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSplKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQ 2346
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA--KINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2347 YIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQK------------------------QLAEAHAKAIAKAEK 2402
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggraveevlkasiqgvhgtvaqlgSVGERYATAIEVAAG 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2403 EAQELKLKMQEEVSKREIAAVDAEKQK-------TNIQLELQELKNLSEQQIKD--------------------KSQQVD 2455
Cdd:TIGR02169 547 NRLNNVVVEDDAVAKEAIELLKRRKAGratflplNKMRDERRDLSILSEDGVIGfavdlvefdpkyepafkyvfGDTLVV 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2456 EALHSRTKIEEEIRLIRIQLETTEKQ----------------KYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSE 2519
Cdd:TIGR02169 627 EDIEAARRLMGKYRMVTLEGELFEKSgamtggsraprggilfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2520 ETQKKRQAEEELKRKSeaekeaaKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEkqikvAHEAAQKSAAAELQSKHmsf 2599
Cdd:TIGR02169 707 LSQELSDASRKIGEIE-------KEIEQLEQEEEKLKERLEELEEDLSSLEQEIE-----NVKSELKELEARIEELE--- 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2600 aEKTSKLEESL-----KQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELekwrqkaNEALRLRLQAEDEAHKKtlaqe 2674
Cdd:TIGR02169 772 -EDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL-------NRLTLEKEYLEKEIQEL----- 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2675 eAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAEstaqqkltAEQELIRLRADFDNAEQQRSLLEDELYRLK 2754
Cdd:TIGR02169 839 -QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD--------LESRLGDLKKERDELEAQLRELERKIEELE 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2755 NEVAAAQQQRKQLEDELAKVRSEMDILIQLKtKAEKETMSNT---EKSKQLLEAEAAKMKDLaeEASRLRAISEEAKHQR 2831
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEElslEDVQAELQRVEEEIRAL--EPVNMLAIQEYEEVLK 986
|
810 820 830
....*....|....*....|....*....|....*
gi 1988774674 2832 QIAEEEAARQRAEAERilKEKLAAISEATRLKTEA 2866
Cdd:TIGR02169 987 RLDELKEKRAKLEEER--KAILERIEEYEKKKREV 1019
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2466-3224 |
8.31e-19 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 95.42 E-value: 8.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2466 EEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEaAKQK 2545
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ-TQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2546 QKALEDLEKLRMQAEEAERQVKQ--AEIEKEKQIKVAHEAAQKsaAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQ-Q 2622
Cdd:TIGR00618 242 HAYLTQKREAQEEQLKKQQLLKQlrARIEELRAQEAVLEETQE--RINRARKAAPLAAHIKAVTQIEQQAQRIHTELQsK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2623 EAERLKKQQEDAENSREEAekELEKWRQKANEALRLRLQAEDEAHKKTLaqeeaekqkeeaEREAKKRAKAEESALKQKE 2702
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQS--SIEEQRRLLQTLHSQEIHIRDAHEVATS------------IREISCQQHTLTQHIHTLQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2703 MAEEELERQRKIAeSTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILI 2782
Cdd:TIGR00618 386 QQKTTLTQKLQSL-CKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2783 QLKTKAEKETMSNTEkskQLLEAEAAKMKdlaeeasrlraisEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEA-TR 2861
Cdd:TIGR00618 465 AQSLKEREQQLQTKE---QIHLQETRKKA-------------VVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPlTR 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2862 LKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEiEEKIVQLKKSSEAEMERQKAIVDDTLKQrrvVEEEI 2941
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQDL---TEKLS 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2942 RILKLNFEKASSGKLDLELELNKLKNIADETQQSKiraEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAA 3021
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ---ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLA 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3022 LEELERLRKKA---EEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIED-SITQKKLKEEYEKAKKLAKE 3097
Cdd:TIGR00618 682 LQKMQSEKEQLtywKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAlNQSLKELMHQARTVLKARTE 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3098 AEAAKEKAEREAALLRQQAEEAERQktaaeeEAANQAKAQEDAERLR-KEAEFEAAKRAQAEAAALMQKQQADTEMAKHK 3176
Cdd:TIGR00618 762 AHFNNNEEVTAALQTGAELSHLAAE------IQFFNRLREEDTHLLKtLEAEIGQEIPSDEDILNLQCETLVQEEEQFLS 835
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1988774674 3177 KLAEQTLKQkfqveQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDA 3224
Cdd:TIGR00618 836 RLEEKSATL-----GEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2256-2827 |
8.89e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 95.13 E-value: 8.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2256 KTLKEQLAQEKKLLEEIEQNKDKVDECQKYakayIDTIKDYELQLVAYKAQVEPLVSPLKKTKLDSASDNIIQEYVTLRT 2335
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLRE----INEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2336 R-YSELMTLTSQYIKFITDTQRRLDDEEKAAEKLK--AEERKKMAEMQAELDKQKQLAEahaKAIAKAEKEAQELKLKMq 2412
Cdd:PRK03918 255 RkLEEKIRELEERIEELKKEIEELEEKVKELKELKekAEEYIKLSEFYEEYLDELREIE---KRLSRLEEEINGIEERI- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2413 EEVSKREIAAVDAEKQKTNIQLELQELKNLSE--QQIKDKSQQVDEaLHSRTKIEEEIRLIRiQLETTEKQKYTAESELK 2490
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHElyEEAKAKKEELER-LKKRLTGLTPEKLEK-ELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2491 QLRDRAAEAEKLRKLAQDEAEKLRK----------QVSEETQKKRQAE--EELKRKSEAEKEAAKQKQKALEDLEKLRMQ 2558
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKELLEEytAELKRIEKELKEIEEKERKLRKELRELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2559 AEEAERQVKQAEIEKekQIKVAHEAAQKSAAAELQSKhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLK---------- 2628
Cdd:PRK03918 489 LKKESELIKLKELAE--QLKELEEKLKKYNLEELEKK----AEEYEKLKEKLIKLKGEIKSLKKELEKLEelkkklaele 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2629 KQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEeaeREAKKRAKAEESAlkqkEMAEEEL 2708
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELE---REEKELKKLEEEL----DKAFEEL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2709 ERQRKIAEStaqqkltAEQELIRLRADFDNAEQQRslLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDiliqlKTKA 2788
Cdd:PRK03918 636 AETEKRLEE-------LRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLE-----KLKE 701
|
570 580 590
....*....|....*....|....*....|....*....
gi 1988774674 2789 EKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEA 2827
Cdd:PRK03918 702 ELEEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3273-3610 |
6.23e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.31 E-value: 6.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3273 EEAEnmRKLAEDAARLsveaqeaARLRQIAE------DDLNQQRALAEKMlkekmQAIQEASRLKaEAEMLQKQKDLAQE 3346
Cdd:COG1196 175 EEAE--RKLEATEENL-------ERLEDILGelerqlEPLERQAEKAERY-----RELKEELKEL-EAELLLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3347 QAQKLLEDKQLMQQRLEEETEEY---HKSLEVERKRQLEIMAEAERLRLQVSQLSEAQAraeeeakkfkkQADKVATRLH 3423
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELaelEAELEELRLELEELELELEEAQAEEYELLAELA-----------RLEQDIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3424 ETEIATQEKMtvvERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEKTVLQQTFMTE 3503
Cdd:COG1196 309 ERRRELEERL---EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE-AEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3504 KEMLLKKEKLIEDEKKRLESQfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELER 3583
Cdd:COG1196 385 AEELLEALRAAAELAAQLEEL-EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340
....*....|....*....|....*..
gi 1988774674 3584 QRLEQERILAEENQKLREKLQQLEDAQ 3610
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAA 490
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
1173-1272 |
6.33e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 82.21 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 1252
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1988774674 1253 ED-VDVPHPDEKSIITYVSSL 1272
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
1059-1156 |
8.36e-18 |
|
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: 82.00 E-value: 8.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1059 KKTFTKWVNKHL-IKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLRHRQV-KLVNI 1134
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1988774674 1135 RNDDI-ADGNPKLTLGLIWTIIL 1156
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
1173-1271 |
9.24e-18 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 81.51 E-value: 9.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQRMTDGYqgiRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLD 1251
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENpLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1988774674 1252 PEDVDVPHPDEKSIITYVSS 1271
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
1169-1274 |
1.09e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 81.92 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1169 SEDMTAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTR 1248
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1988774674 1249 LLDPEDV-DVPHPDEKSIITYVSSLYD 1274
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
1175-1285 |
1.49e-17 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 81.58 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1175 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 1254
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|..
gi 1988774674 1255 -VDVPHPDEKSIITYVSSLYdampRTDVHDGM 1285
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY----RCLVQKGL 110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2420-3236 |
2.38e-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: 90.51 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2420 IAAVDAEKQKTNIQLELQElKNLSEQQ--IKDKSQQVDEALHSRTKIEE--EIRLIRIQLETTE--KQKYTAESELKQLR 2493
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVE-ENIERLDliIDEKRQQLERLRREREKAERyqALLKEKREYEGYEllKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2494 DRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALE-DLEKLRMQAEEAERQVKQAEiE 2572
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELEDAE-E 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2573 KEKQIKVAHEAaQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKA 2652
Cdd:TIGR02169 323 RLAKLEAEIDK-LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2653 NEALRLRLQAEDEAHKKTlaqeeaekQKEEAEREAKKRAKAEESALK-QKEMAEEELERQRKIAESTAQQKLTAEQELIR 2731
Cdd:TIGR02169 402 NELKRELDRLQEELQRLS--------EELADLNAAIAGIEAKINELEeEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2732 LRADFDNAEQQRSLLEDELYRLKNEVAAAQQ-------QRKQLEDELAKVRSEMDILIQLKTKAEK-------------- 2790
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEErvrggraVEEVLKASIQGVHGTVAQLGSVGERYATaievaagnrlnnvv 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2791 -ETMSNTEKSKQLLEAEAA---------KMKDLAEEASRLRA----------ISEEAKHQRQIA----------EEEAAR 2840
Cdd:TIGR02169 554 vEDDAVAKEAIELLKRRKAgratflplnKMRDERRDLSILSEdgvigfavdlVEFDPKYEPAFKyvfgdtlvveDIEAAR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2841 QRAEAERI------LKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKK 2914
Cdd:TIGR02169 634 RLMGKYRMvtlegeLFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2915 SSEAEMERQKAIvDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKL-RKLALEE 2993
Cdd:TIGR02169 714 ASRKIGEIEKEI-EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2994 EKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQ 3073
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3074 qiedsiTQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQED-AERLRKEAEFEAA 3152
Cdd:TIGR02169 873 ------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEElSEIEDPKGEDEEI 946
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3153 KRAQAEAAALMQKQQADTEmakhkklAEQTLKQ-KFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQV 3231
Cdd:TIGR02169 947 PEEELSLEDVQAELQRVEE-------EIRALEPvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
....*
gi 1988774674 3232 EEELF 3236
Cdd:TIGR02169 1020 FMEAF 1024
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2137-2984 |
3.09e-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: 90.42 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2137 KEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQREL 2216
Cdd:pfam02463 265 EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2217 EQLGRQLGYYRESydwlirwIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDY 2296
Cdd:pfam02463 345 KELEIKREAEEEE-------EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2297 ELQLVAYKAQVEPLVSPLKKTKLdsasdnIIQEYVTLRTRYSELMTLTSqyikfitdtQRRLDDEEKAAEKLKAEERKKM 2376
Cdd:pfam02463 418 EDLLKEEKKEELEILEEEEESIE------LKQGKLTEEKEELEKQELKL---------LKDELELKKSEDLLKETQLVKL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2377 AEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVskREIAAVDAEKQKTNIQLELQELKNLSeqqikdkSQQVDE 2456
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG--GRIISAHGRLGDLGVAVENYKVAIST-------AVIVEV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2457 ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAeAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSE 2536
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSI-AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2537 AEKEAAKQKQKALEDLEKLRMQAE-EAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHG 2615
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEgLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2616 AVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlaqeeaekqkeeAEREAKKRAKAEE 2695
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK-------------SELSLKEKELAEE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2696 SALKQKEMAEEELERQRKIAESTaqqkLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEvaaAQQQRKQLEDELAKVR 2775
Cdd:pfam02463 780 REKTEKLKVEEEKEEKLKAQEEE----LRALEEELKEEAELLEEEQLLIEQEEKIKEEELE---ELALELKEEQKLEKLA 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2776 SEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAA 2855
Cdd:pfam02463 853 EEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLK 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2856 ISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEdqASQHKQEIEEKIVQLKKSSEAEMERQKAivddTLKQRR 2935
Cdd:pfam02463 933 YEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL--GKVNLMAIEEFEEKEERYNKDELEKERL----EEEKKK 1006
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 1988774674 2936 VVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAE 2984
Cdd:pfam02463 1007 LIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDD 1055
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
1175-1274 |
5.69e-17 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 79.62 E-value: 5.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1175 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 1254
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1988774674 1255 VDV--PHPDEKSIITYVSSLYD 1274
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2361-2827 |
6.65e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 88.94 E-value: 6.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2361 EEKAAEKLKAEERKKMA--------EMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqEEVSKREIAAVDAEKQKTNI 2432
Cdd:PRK02224 223 ERYEEQREQARETRDEAdevleeheERREELETLEAEIEDLRETIAETEREREELA----EEVRDLRERLEELEEERDDL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2433 QLELQelknLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 2512
Cdd:PRK02224 299 LAEAG----LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2513 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAEL 2592
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKC 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2593 --------QSKHMSFAEKTSKLEESLKQEhgaVLQLQQEAERLKKQQEDAENSReEAEKELEKWRQKANEALRLRLQAED 2664
Cdd:PRK02224 455 pecgqpveGSPHVETIEEDRERVEELEAE---LEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2665 EAHKKTLAQEEAEKQKEEAEREAK-KRAKAEESALKQKEMAE-------------EELERQRKIAESTAQQKlTAEQELI 2730
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEeKREAAAEAEEEAEEAREevaelnsklaelkERIESLERIRTLLAAIA-DAEDEIE 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2731 RL---RADFDNAEQQR-----------SLLEDELYrlKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtMSNT 2796
Cdd:PRK02224 610 RLrekREALAELNDERrerlaekrerkRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAE-IGAV 686
|
490 500 510
....*....|....*....|....*....|.
gi 1988774674 2797 EKSKQLLEAEAAKMKDLAEEASRLRAISEEA 2827
Cdd:PRK02224 687 ENELEELEELRERREALENRVEALEALYDEA 717
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
1175-1281 |
9.52e-17 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 79.32 E-value: 9.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1175 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 1254
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*....
gi 1988774674 1255 VDV--PHPDEKSIITYVSSLYDAMPRTDV 1281
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRRHEM 111
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2461-3372 |
1.47e-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: 88.20 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2461 RTKIEEEIRLIriqlETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKqvseETQKKRQAEEELKRKSEAE-K 2539
Cdd:TIGR02169 155 RRKIIDEIAGV----AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRR----EREKAERYQALLKEKREYEgY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2540 EAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKtskleeslkqehgavLQ 2619
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---------------LR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2620 LQQEAERLKKQQEDAENSREEAEKELEKW--RQKANEALRLRLQAEDEAHKKTLAqeeaekqkeeaeREAKKRAKAEESA 2697
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAeeRLAKLEAEIDKLLAEIEELEREIE------------EERKRRDKLTEEY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2698 LKQKEmaEEELERQRKIAESTAQQklTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSE 2777
Cdd:TIGR02169 360 AELKE--ELEDLRAELEEVDKEFA--ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2778 MDILIQLKTKAEKETMSNTEKSKQL---LEAEAAKMKDLAEEASRLRaiSEEAKHQRQIAEEEAARQRAE--------AE 2846
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQEWKLEQLaadLSKYEQELYDLKEEYDRVE--KELSKLQRELAEAEAQARASEervrggraVE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2847 RILKEKL----AAISEATRLKTEAEIALkEKEAENERLRRQAEDEAYQRKALEdQASQHK---------QEIEEKIVQLK 2913
Cdd:TIGR02169 514 EVLKASIqgvhGTVAQLGSVGERYATAI-EVAAGNRLNNVVVEDDAVAKEAIE-LLKRRKagratflplNKMRDERRDLS 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2914 KSSEA----------EMERQ-----KAIVDDTLkqrrVVE--EEIRILKLNFEKASsgkldLELEL-----------NKL 2965
Cdd:TIGR02169 592 ILSEDgvigfavdlvEFDPKyepafKYVFGDTL----VVEdiEAARRLMGKYRMVT-----LEGELfeksgamtggsRAP 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2966 KNIADETQQSKIRAEEEAEKLRKLaleeekrrreaeekvkkiaaaeeeaARQRKAALEELERLRKKAEEARkqkdEADKE 3045
Cdd:TIGR02169 663 RGGILFSRSEPAELQRLRERLEGL-------------------------KRELSSLQSELRRIENRLDELS----QELSD 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3046 AEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDsitQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTA 3125
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEED---LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH 790
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3126 AEEEAANQAKAQEDAERLRKEAEFEaaKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDEtdk 3205
Cdd:TIGR02169 791 SRIPEIQAELSKLEEEVSRIEARLR--EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE--- 865
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3206 qksvLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKlLAEEAENMRKLAEDA 3285
Cdd:TIGR02169 866 ----LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIEDPK 940
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3286 ARLSVEAQEAARLRQIAEDDLNQQRALaEKMLKEKMQAIQEAsrlkaeAEMLQKQKDLaQEQAQKLLEDKQLMQQRLEEE 3365
Cdd:TIGR02169 941 GEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEY------EEVLKRLDEL-KEKRAKLEEERKAILERIEEY 1012
|
....*..
gi 1988774674 3366 TEEYHKS 3372
Cdd:TIGR02169 1013 EKKKREV 1019
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3276-3587 |
1.49e-16 |
|
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: 87.49 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3276 ENMRKLAEDAARLSVEAQEAARLRQIAED---DLNQQRALAEKMlKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLL 3352
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEkarEVERRRKLEEAE-KARQAEMDRQAAIYAEQERMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3353 EDKQLMQQRLEEETEEYHKSLEVERkRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEK 3432
Cdd:pfam17380 358 RKRELERIRQEEIAMEISRMRELER-LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3433 MtvvERLEFERlntSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKtvlQQTFMTEKEMLLKKEK 3512
Cdd:pfam17380 437 V---RRLEEER---AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE---QRRKILEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3513 LIEDEKKR--LESQFEEEVK----KAKALKDEQERQKQQMEQEKKTLQATMDAALSKQK-----EAEEEMLRKQKEmQEL 3581
Cdd:pfam17380 508 MIEEERKRklLEKEMEERQKaiyeEERRREAEEERRKQQEMEERRRIQEQMRKATEERSrleamEREREMMRQIVE-SEK 586
|
....*.
gi 1988774674 3582 ERQRLE 3587
Cdd:pfam17380 587 ARAEYE 592
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2459-3083 |
1.62e-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: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2459 HSRTKIEEEIRliriQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRqaeEELKRKSEAE 2538
Cdd:pfam12128 241 PEFTKLQQEFN----TLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKR---DELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2539 KEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAeLQSKHMSFAEKTSKLEESLKQEHGAVL 2618
Cdd:pfam12128 314 DAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LTGKHQDVTAKYNRRRSKIKEQNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2619 QLQQEaeRLKKQQEDAENSREEAEKELEK----WRQKANEALRlRLQAEDEAHKKTLAqeeaekqkeeaerEAKKR---A 2691
Cdd:pfam12128 393 AGIKD--KLAKIREARDRQLAVAEDDLQAleseLREQLEAGKL-EFNEEEYRLKSRLG-------------ELKLRlnqA 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2692 KAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQ-------- 2763
Cdd:pfam12128 457 TATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtl 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2764 ----RKQL---EDELAKVRSEmdiliQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEE 2836
Cdd:pfam12128 537 lhflRKEApdwEQSIGKVISP-----ELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEE 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2837 EAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSS 2916
Cdd:pfam12128 612 ALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQL 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2917 EAEMERQKAIVDDTLKQRRvveeEIRILKLNFEKASSGKLDLELELNKlkniadetqqSKIRAEEEAEKLRKLALEEEKR 2996
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKR----EARTEKQAYWQVVEGALDAQLALLK----------AAIAARRSGAKAELKALETWYK 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2997 RREAEEKVKKIaaAEEEAARQRKAALEELERLRKKAEEARKQKD--EADKEAEKQIVVAQQAAQKCSAAEQQVQsvLAQQ 3074
Cdd:pfam12128 758 RDLASLGVDPD--VIAKLKREIRTLERKIERIAVRRQEVLRYFDwyQETWLQRRPRLATQLSNIERAISELQQQ--LARL 833
|
....*....
gi 1988774674 3075 IEDSITQKK 3083
Cdd:pfam12128 834 IADTKLRRA 842
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
1175-1276 |
2.20e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 78.20 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1175 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 1254
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1988774674 1255 -VDVPHPDEKSIITYVSSLYDAM 1276
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2357-2988 |
2.69e-16 |
|
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: 86.70 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2357 RLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSK------------------R 2418
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdlikennatrhlcnllK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2419 EIAAVDAEK----------------------------------QKTNIQLEL-----------QELKNLSEQQIKDKSQQ 2453
Cdd:pfam05483 162 ETCARSAEKtkkyeyereetrqvymdlnnniekmilafeelrvQAENARLEMhfklkedhekiQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2454 VDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKR 2533
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2534 KSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSaAAELQSKHMSFAEKTSKLEESLKQE 2613
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN-EDQLKIITMELQKKSSELEEMTKFK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2614 HGAVLQLqQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKK-RAK 2692
Cdd:pfam05483 401 NNKEVEL-EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlKTE 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2693 AEESALKQKEM---AEEELERQRKIAESTAQQKLtaeqELIRLRADFDNAEQQRSlledelyRLKNEVAAAQQQRKQLED 2769
Cdd:pfam05483 480 LEKEKLKNIELtahCDKLLLENKELTQEASDMTL----ELKKHQEDIINCKKQEE-------RMLKQIENLEEKEMNLRD 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2770 ELAKVRSEM-DILIQLKTKAEKETMSNTEKSKQLLEAEaAKMKDLAEEASRLRA-ISEEAKHQRQIAEE-EAARQRAEAE 2846
Cdd:pfam05483 549 ELESVREEFiQKGDEVKCKLDKSEENARSIEYEVLKKE-KQMKILENKCNNLKKqIENKNKNIEELHQEnKALKKKGSAE 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2847 -------RILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQA-EDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEA 2918
Cdd:pfam05483 628 nkqlnayEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKlLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVA 707
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2919 EMERQKAIVDDTLKQRrvvEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRK 2988
Cdd:pfam05483 708 LMEKHKHQYDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKM 774
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3270-3617 |
7.41e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.76 E-value: 7.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3270 LLAEEAENMRKLAEDAARlsveAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQ-EASRLKAEAEMLQKQkdlaQEQA 3348
Cdd:COG1196 194 ILGELERQLEPLERQAEK----AERYRELKEELKELEAELLLLKLRELEAELEELEaELEELEAELEELEAE----LAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3349 QKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQAraeeeakkfkkqadkvatrlhetEIA 3428
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE-----------------------ELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3429 TQEkmtvvERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLL 3508
Cdd:COG1196 323 EEL-----AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3509 KKEKLIEDEkkRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQ 3588
Cdd:COG1196 398 LAAQLEELE--EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340
....*....|....*....|....*....
gi 1988774674 3589 ERILAEENQKLREKLQQLEDAQKDQHTRE 3617
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2389-2851 |
7.65e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 85.20 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2389 LAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLsEQQIKDKSQQVDEALHSRTKIEEEI 2468
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEL-EEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2469 RLIRIQLETTEkqkytAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKA 2548
Cdd:COG4717 126 QLLPLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2549 LEDLEKLRMQAEEAERQVKQ------AEIEKEKQIKVAHEAAQK-----------SAAAELQSKHMSFAEKTSKLEESLK 2611
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEeleeleEELEQLENELEAAALEERlkearlllliaAALLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2612 QEHG----AVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKAnEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREA 2687
Cdd:COG4717 281 LVLGllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELL-AALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2688 KKRAKAEESALKQKEM-----AEEELERQRKIAESTAQQKLTAEQELI--RLRADFDNAEQQ-----RSLLEDELYRLKN 2755
Cdd:COG4717 360 EEELQLEELEQEIAALlaeagVEDEEELRAALEQAEEYQELKEELEELeeQLEELLGELEELlealdEEELEEELEELEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2756 EVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtmsntekskQLLEAEAAKMKDLAEEASRLRAISEE-AKHQRQIA 2834
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEEDGELAELL---------QELEELKAELRELAEEWAALKLALELlEEAREEYR 510
|
490
....*....|....*..
gi 1988774674 2835 EEEAARQRAEAERILKE 2851
Cdd:COG4717 511 EERLPPVLERASEYFSR 527
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2891-3614 |
8.49e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 85.41 E-value: 8.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2891 RKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKassgkLDLELELNKLKNIAD 2970
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQ-----LKEKLELEEEYLLYL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2971 ETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQI 3050
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3051 VVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAkekaereaaLLRQQAEEAERQKTAAEEEA 3130
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE---------LEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3131 ANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEqtlkqkfqveqeltkvKLKLDETDKQKSVL 3210
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELE----------------ILEEEEESIELKQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3211 DEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRlIKKDKDSTQKLLAEEAENMRKLAEDAARLSV 3290
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR-QKLEERSQKESKARSGLKVLLALIKDGVGGR 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3291 EAQEAARLRQIAEDDLNQQRALAEKmlkekmqAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYH 3370
Cdd:pfam02463 524 IISAHGRLGDLGVAVENYKVAISTA-------VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3371 KSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAtQEKMTVVERLEFERLNTSKEA 3450
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL-EEGLAEKSEVKASLSELTKEL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3451 DDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVK 3530
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3531 KAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQErILAEENQKLREKLQQLEDAQ 3610
Cdd:pfam02463 756 RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA-ELLEEEQLLIEQEEKIKEEE 834
|
....
gi 1988774674 3611 KDQH 3614
Cdd:pfam02463 835 LEEL 838
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1987-2773 |
1.19e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.12 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1987 EKGQQNETLC--KNYISELKDLRLRIEDCEAgtvarirkpveKEPLKEYIQKTTEQKKVQGELDGLKKDLDKVSVKTQEV 2064
Cdd:TIGR02169 195 EKRQQLERLRreREKAERYQALLKEKREYEG-----------YELLKEKEALERQKEAIERQLASLEEELEKLTEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2065 lasPQPSASAPVLRSELDLTVQKMDHAHMLSsvYLEKLKTVEMVIRNTQGAEGVLKQYEDCLREvhTVPSDVKEVETYRA 2144
Cdd:TIGR02169 264 ---EKRLEEIEQLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2145 KLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLG 2224
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2225 YYRESYDWLIRWIADAKQRQEKIQavpiTDSKTLKEQLAQEKKLLEEIEQNKDKVDEcQKYAK-----AYIDTIKDYELQ 2299
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELE----EEKEDKALEIKKQEWKLEQLAADLSKYEQ-ELYDLkeeydRVEKELSKLQRE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2300 LVAYKAQVEPLV--SPLKKTKLDSASDNIIQEYVTLRtrysELMTLTSQYIKFI-TDTQRRL-----DDEEKAAEKLK-A 2370
Cdd:TIGR02169 492 LAEAEAQARASEerVRGGRAVEEVLKASIQGVHGTVA----QLGSVGERYATAIeVAAGNRLnnvvvEDDAVAKEAIElL 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2371 EERK----------KMAEMQAELDKqkqLAEAHAKAIAK-----AEKEAQELKLKMQEEVSKREIAAvdAEKQKTNIQL- 2434
Cdd:TIGR02169 568 KRRKagratflplnKMRDERRDLSI---LSEDGVIGFAVdlvefDPKYEPAFKYVFGDTLVVEDIEA--ARRLMGKYRMv 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2435 ----ELQELK-------NLSEQQIKDKSQQVDEALHSRTKIEEeirlIRIQLETTEKQKYTAESELKQLRDRAAEAEKLR 2503
Cdd:TIGR02169 643 tlegELFEKSgamtggsRAPRGGILFSRSEPAELQRLRERLEG----LKRELSSLQSELRRIENRLDELSQELSDASRKI 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2504 KLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEaEKEAAKQKQKAL--------EDLEKLRMQAEEAER-------QVKQ 2568
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ-EIENVKSELKELearieeleEDLHKLEEALNDLEArlshsriPEIQ 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2569 AEIEKEKQIKVAHEAAQKSAAAELQSKHM--SFAEKTSKLEESLKQE---------------HGAVLQLQQEAERLKKQQ 2631
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLekEYLEKEIQELQEQRIDlkeqiksiekeienlNGKKEELEEELEELEAAL 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2632 EDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlaqeeaekQKEEAEREAKKRAKAEESALKQKEMAEEELERQ 2711
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK---------RKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 2712 RKIAESTAQQKLTAEQELIRLRADFDN-AEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAK 2773
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMlAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
1178-1273 |
1.34e-15 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 75.86 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1178 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEkDLGVTRLLDPED-VD 1256
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1988774674 1257 VPHPDEKSIITYVSSLY 1273
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
1055-1154 |
1.59e-15 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 75.65 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1055 DRVQKKTFTKWVNKHLIKAQ-RHVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLRHR-QV 1129
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 1988774674 1130 KLVNIRNDDIADGNPKLTLGLIWTI 1154
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2123-2944 |
1.65e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.73 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2123 EDCLREVHTVPSDVKEVETY----RAKLKKMRTEAEDEQPvFDSLEEELkkasavsdkmvrvhseRDVELDHFRQQLSSL 2198
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIidekRQQLERLRREREKAER-YQALLKEK----------------REYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2199 QDRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKiqavpitdsKTLKEQLAQEKKLLE---EIEQN 2275
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD---------LGEEEQLRVKEKIGEleaEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2276 KDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKKTKLDSASdnIIQEYVTLRTRYSELmtltsqyikfitdtQ 2355
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK--LTEEYAELKEELEDL--------------R 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2356 RRLDDEEKAAeklkAEERKKMAEMQAELDKqkqlaeahakaiakaekeaqelkLKMQEEVSKREIAAVDAEKQKTNIQLE 2435
Cdd:TIGR02169 371 AELEEVDKEF----AETRDELKDYREKLEK-----------------------LKREINELKRELDRLQEELQRLSEELA 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2436 lqELKNlseqQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKL-- 2513
Cdd:TIGR02169 424 --DLNA----AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAea 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2514 RKQVSEETQKKRQAEEELKRKSE-------AE-KEAAKQKQKALEDLEKLRMQA---EEAERQVKQAEIEKEKQI----- 2577
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASIqgvhgtvAQlGSVGERYATAIEVAAGNRLNNvvvEDDAVAKEAIELLKRRKAgratf 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2578 ----KVAHEAAQKSAAA-----------------------------------ELQSKHMSFAEKTSkLEESLKQEHGAV- 2617
Cdd:TIGR02169 578 lplnKMRDERRDLSILSedgvigfavdlvefdpkyepafkyvfgdtlvvediEAARRLMGKYRMVT-LEGELFEKSGAMt 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2618 -------------LQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRlqaeDEAHKKTlaqeeaekqkeeae 2684
Cdd:TIGR02169 657 ggsraprggilfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL----SDASRKI-------------- 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2685 REAKKRAkaeESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 2764
Cdd:TIGR02169 719 GEIEKEI---EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPE 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2765 KQLE-DELAKVRSEMD-ILIQLKTKAEKETMSNT--EKSKQLLEAEAAKMKDlaEEASRLRAISEEAKHQRQIAEEEAAR 2840
Cdd:TIGR02169 796 IQAElSKLEEEVSRIEaRLREIEQKLNRLTLEKEylEKEIQELQEQRIDLKE--QIKSIEKEIENLNGKKEELEEELEEL 873
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2841 QRAEAERI--LKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASqhkqEIEEKIVQLKKSSEA 2918
Cdd:TIGR02169 874 EAALRDLEsrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEE 949
|
890 900
....*....|....*....|....*.
gi 1988774674 2919 EMerqkaIVDDTLKQRRVVEEEIRIL 2944
Cdd:TIGR02169 950 EL-----SLEDVQAELQRVEEEIRAL 970
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
1177-1274 |
2.18e-15 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 75.30 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1177 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLD-PEDV 1255
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1988774674 1256 DVPHPDEKSIITYVSSLYD 1274
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2346-2966 |
2.33e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 84.01 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2346 QYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKaIAKAEKEAQElklkmqeevskreiaavDA 2425
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMAD-IRRRESQSQE-----------------DL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2426 EKQKTNIQLELQELKNLSEQQIKDKSQQVDE---ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRdraaeaekL 2502
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIEQlrkMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMH--------F 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2503 RKLAQDEAEKLRKQVSEETQKKRQ---AEEELkrksEAEKEAAKQKQKALedlekLRMQAEEAERQVKQAEIEKEKQIKV 2579
Cdd:pfam15921 216 RSLGSAISKILRELDTEISYLKGRifpVEDQL----EALKSESQNKIELL-----LQQHQDRIEQLISEHEVEITGLTEK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2580 AHEAaqKSAAAELQSKhMSFAEKTSKLEESLKQEH-----GAVLQLQQEAERLKKQQEDaenSREEAEKELEKWRQKANE 2654
Cdd:pfam15921 287 ASSA--RSQANSIQSQ-LEIIQEQARNQNSMYMRQlsdleSTVSQLRSELREAKRMYED---KIEELEKQLVLANSELTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2655 ALRLRLQAE------DEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESA-----------LKQKEMAEEELERQRKIAES 2717
Cdd:pfam15921 361 ARTERDQFSqesgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGnsitidhlrreLDDRNMEVQRLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2718 TAQQKLtaEQELIRLRADFDNAEQQRSL---LEDELYRLKNEVAAAQQQRKQLEDELAKVrSEMDILIQLKTKAEKETMS 2794
Cdd:pfam15921 441 ECQGQM--ERQMAAIQGKNESLEKVSSLtaqLESTKEMLRKVVEELTAKKMTLESSERTV-SDLTASLQEKERAIEATNA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2795 NTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQR-QIAEE----EAARQRAEAerilKEKLAAISEATRLKTEAEIA 2869
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKdkviEILRQQIEN----MTQLVGQHGRTAGAMQVEKA 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2870 LKEKEAENERLRRQaedeayQRKALEDQASQHKQEIEEKIVQLK----KSSEAEMERQKAIVDdtLKQRR---------- 2935
Cdd:pfam15921 594 QLEKEINDRRLELQ------EFKILKDKKDAKIRELEARVSDLElekvKLVNAGSERLRAVKD--IKQERdqllnevkts 665
|
650 660 670
....*....|....*....|....*....|....*.
gi 1988774674 2936 -----VVEEEIRILKLNFEKASSgklDLELELNKLK 2966
Cdd:pfam15921 666 rnelnSLSEDYEVLKRNFRNKSE---EMETTTNKLK 698
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
1058-1158 |
3.00e-15 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 74.64 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1058 QKKTFTKWVNKHLIK--AQRHVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMRfhklQNVQIALDFLRHRQV 1129
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1988774674 1130 KLVNIRNDDIADGNPKLTLGLIWTIILHF 1158
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2232-2908 |
4.41e-15 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 82.85 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2232 WLIRWIADAKQRQEKIQ---AVPITDSKTLKE-QLAQEK---KLLEEIEQNKDKVDE----------CQKYAKAYIDTIK 2294
Cdd:pfam05483 93 WKVSIEAELKQKENKLQenrKIIEAQRKAIQElQFENEKvslKLEEEIQENKDLIKEnnatrhlcnlLKETCARSAEKTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2295 DYELQ-------LVAYKAQVEPLVSPLKKTKLdSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRL--------- 2358
Cdd:pfam05483 173 KYEYEreetrqvYMDLNNNIEKMILAFEELRV-QAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVsllliqite 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2359 -DDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQ 2437
Cdd:pfam05483 252 kENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2438 ELKNLSEQQIKDKSQQ---VDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLR 2514
Cdd:pfam05483 332 EKEAQMEELNKAKAAHsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2515 KQVSEETQ---KKRQAE---EELKRKSEAEKEAAKQKQKALEDLEkLRMQAEEAERQVKQAEIEKEKqikvaheaaqksa 2588
Cdd:pfam05483 412 KILAEDEKlldEKKQFEkiaEELKGKEQELIFLLQAREKEIHDLE-IQLTAIKTSEEHYLKEVEDLK------------- 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2589 aAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRlqAEDEAHK 2668
Cdd:pfam05483 478 -TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR--DELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2669 KTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMA--EEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLL 2746
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2747 EDELYRLKNEVAAAQQQRKQLEDELAKVrsemdilIQLKTKAEKETMSNTEKSKQLLEaEAAKM-----KDLAEEASRLR 2821
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDNYQKE-------IEDKKISEEKLLEEVEKAKAIAD-EAVKLqkeidKRCQHKIAEMV 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2822 AISEEAKHQRQIAEEEaarqRAEAERILKEKLaaiSEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQH 2901
Cdd:pfam05483 707 ALMEKHKHQYDKIIEE----RDSELGLYKNKE---QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKEN 779
|
....*..
gi 1988774674 2902 KQEIEEK 2908
Cdd:pfam05483 780 TAILKDK 786
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3346-3617 |
7.01e-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: 7.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3346 EQAQKLLEDkqlMQQRLE------EETEEYHKSLEVERKRQL---EIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQAD 3416
Cdd:COG1196 175 EEAERKLEA---TEENLErledilGELERQLEPLERQAEKAEryrELKEELKELEAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3417 KVATRLHETEIATQEKMTVVERLEFERLNTSKEA--DDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKT 3494
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEaqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3495 VLQQTfmTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRK 3574
Cdd:COG1196 332 LEELE--EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1988774674 3575 QKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRE 3617
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2907-3590 |
8.48e-15 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 82.08 E-value: 8.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2907 EKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASsgkLDLELELNKLKNIADETQQSKIRAEEEAEKL 2986
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVS---LKLEEEIQENKDLIKENNATRHLCNLLKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2987 RKLAlEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELerlRKKAEEARKQKDEADKEAEKQIVVAQQAAQK-CSAAEQ 3065
Cdd:pfam05483 165 ARSA-EKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL---RVQAENARLEMHFKLKEDHEKIQHLEEEYKKeINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3066 QVQSVLAQQIEDSITQKKLkeeyekakklakeaeaakekaereAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRK 3145
Cdd:pfam05483 241 QVSLLLIQITEKENKMKDL------------------------TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3146 EaeFEAAKRAQAEAAALMQKQQADTEMAKhKKLAEQTLKQKFQVEqELTKVK----LKLDETDKQKSVLDEELQRLKDEV 3221
Cdd:pfam05483 297 E--LEDIKMSLQRSMSTQKALEEDLQIAT-KTICQLTEEKEAQME-ELNKAKaahsFVVTEFEATTCSLEELLRTEQQRL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3222 DDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLiKKDKDSTQKLLaEEAENMRKLAEDaarLSVEAQEAARLRQI 3301
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEEL-KKILAEDEKLL-DEKKQFEKIAEE---LKGKEQELIFLLQA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3302 AEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQ-KQKDLAQEQAQKLLEDKQLMQQR--LEEETEEYHKSLEVERK 3378
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHCDKLLLENKELTQEAsdMTLELKKHQEDIINCKK 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3379 RQLEIMAEAERLRLQVSQLseaQARAEEEAKKFKKQADKVATRLHETE-------IATQEKMTVVERLEFERLNTSKEAD 3451
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNL---RDELESVREEFIQKGDEVKCKLDKSEenarsieYEVLKKEKQMKILENKCNNLKKQIE 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3452 DLRKAIADLENEKARLKKEAEElQNKSKEMADAQQKKIEHEKTVLQQTFmteKEMLLKKEKLIEDeKKRLESQFEEEVKK 3531
Cdd:pfam05483 605 NKNKNIEELHQENKALKKKGSA-ENKQLNAYEIKVNKLELELASAKQKF---EEIIDNYQKEIED-KKISEEKLLEEVEK 679
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774674 3532 AKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRlEQER 3590
Cdd:pfam05483 680 AKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNK-EQEQ 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2176-2912 |
8.83e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 82.27 E-value: 8.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2176 KMVRVHSERDVELDHFRQQLSSL-QDRWKAVFTQIDLRQRE-----LEQLGRQLGYYRESYDWLIRwiadakqrqeKIQA 2249
Cdd:COG4913 133 KRFFVIADGPLDLEDFEEFAHGFdIRALKARLKKQGVEFFDsfsayLARLRRRLGIGSEKALRLLH----------KTQS 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2250 V-PITDSKTL-KEQLAQEKKLLEEIEQnkdkvdecqkyAKAYIDTIKDYELQLVAYKAQVEPLvSPLKKTKldsasdnii 2327
Cdd:COG4913 203 FkPIGDLDDFvREYMLEEPDTFEAADA-----------LVEHFDDLERAHEALEDAREQIELL-EPIRELA--------- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2328 QEYVTLRTRYSELMTLtsqyikfitDTQRRLDDEEKAAEKLKAEERkkmaEMQAELDKQKQLAEAHAKAIAKAEKEAQEL 2407
Cdd:COG4913 262 ERYAAARERLAELEYL---------RAALRLWFAQRRLELLEAELE----ELRAELARLEAELERLEARLDALREELDEL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2408 KLKMQE------EVSKREIAavDAEKQKTNIQLELQELKNL----------SEQQIKDKSQQVDEALHSRTKIEEEIRLI 2471
Cdd:COG4913 329 EAQIRGnggdrlEQLEREIE--RLERELEERERRRARLEALlaalglplpaSAEEFAALRAEAAALLEALEEELEALEEA 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2472 RIQLETTEKQkytAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKrqaEEELK--------RKSEAEKEAA- 2542
Cdd:COG4913 407 LAEAEAALRD---LRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD---EAELPfvgelievRPEEERWRGAi 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2543 ---------------KQKQKALEDLE----KLRMQAEEAERQVKQAEIEKEK------QIKVAHEAAQKSAAAELQsKHM 2597
Cdd:COG4913 481 ervlggfaltllvppEHYAAALRWVNrlhlRGRLVYERVRTGLPDPERPRLDpdslagKLDFKPHPFRAWLEAELG-RRF 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2598 SFAEKTSklEESLKQEHGAVL---QLQQEAERLKKQQEDAENSR----EEAEKELEKWRQKANEalrlrLQAEDEAHKKT 2670
Cdd:COG4913 560 DYVCVDS--PEELRRHPRAITragQVKGNGTRHEKDDRRRIRSRyvlgFDNRAKLAALEAELAE-----LEEELAEAEER 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2671 LAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERqrkiaestaqqkltAEQELIRLRADFDNAEQqrslLEDEL 2750
Cdd:COG4913 633 LEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE--------------LEAELERLDASSDDLAA----LEEQL 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2751 YRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQ 2830
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER 774
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2831 RQIAEEEAARQRAEAERILKE--------------KLAAISE-ATRLKTEAEIALKEKEAENERLRRQAEDEayQRKALE 2895
Cdd:COG4913 775 IDALRARLNRAEEELERAMRAfnrewpaetadldaDLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIE--FVADLL 852
|
810
....*....|....*..
gi 1988774674 2896 DQASQHKQEIEEKIVQL 2912
Cdd:COG4913 853 SKLRRAIREIKERIDPL 869
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2685-2942 |
8.97e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 81.71 E-value: 8.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2685 REAKKRAKAEESALKQ-KEMAEEELERQRKIAES-TAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 2762
Cdd:pfam17380 288 QQQEKFEKMEQERLRQeKEEKAREVERRRKLEEAeKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2763 QRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKH-QRQIAEEEAARq 2841
Cdd:pfam17380 368 EEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQrEVRRLEEERAR- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2842 raEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQE-IEEKivQLKKSSEAEM 2920
Cdd:pfam17380 447 --EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmIEEE--RKRKLLEKEM 522
|
250 260
....*....|....*....|...
gi 1988774674 2921 E-RQKAIVDDtlKQRRVVEEEIR 2942
Cdd:pfam17380 523 EeRQKAIYEE--ERRREAEEERR 543
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1632-1821 |
1.11e-14 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 76.33 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1632 LHAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDIQALGDRLVRDGHPGKKTVESFT 1711
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1712 AALQTQWSWILQLCCCIEAHLKENTAYYQFFADVKEAQDKMKKMQENMKkkySCDRSTTATRLEDLLQDAAEEKEQLNEF 1791
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 1988774674 1792 KTVVAGLNKRSRSIIQLKPRNPTTSIKGKL 1821
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5047-5085 |
1.37e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.43 E-value: 1.37e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1988774674 5047 LLEAQIATGGIIDPEESHRLPVEVAYNRGFFDEEMNEIL 5085
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2436-2845 |
1.42e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 81.32 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2436 LQELKNLSEQQIKDKSQqvdealhsrtKIEEEirliRIQLETTEKQKytaesELKQlRDRAAEAEKLRKLAQDE-----A 2510
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE----------KMEQE----RLRQEKEEKAR-----EVER-RRKLEEAEKARQAEMDRqaaiyA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2511 EKLRKQVSEETQKKRQAEEELKRkseaEKEAAKQKQKALE-----DLEKLRMQAEEAERQVKQaEIEKEKQIKVAHEAAQ 2585
Cdd:pfam17380 338 EQERMAMERERELERIRQEERKR----ELERIRQEEIAMEisrmrELERLQMERQQKNERVRQ-ELEAARKVKILEEERQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2586 KSAaaelqSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENsreeaEKELEKWRQKANEALRLRLQAEde 2665
Cdd:pfam17380 413 RKI-----QQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQER-----QQQVERLRQQEEERKRKKLELE-- 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2666 ahkktlaqeeaekqkeeaeREAKKRAKAEEsaLKQKEMAEEELERQRKIAEStaqqkltaeqelirlradfdnaEQQRSL 2745
Cdd:pfam17380 481 -------------------KEKRDRKRAEE--QRRKILEKELEERKQAMIEE----------------------ERKRKL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2746 LEDELYRLKNEVAAAQQQRKQLEdelakvrsemdiliqlktkaEKETMSNTEKSKQLLEaeaaKMKDLAEEASRLRAISE 2825
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAEE--------------------ERRKQQEMEERRRIQE----QMRKATEERSRLEAMER 573
|
410 420
....*....|....*....|
gi 1988774674 2826 EAKHQRQIAEEEAARQRAEA 2845
Cdd:pfam17380 574 EREMMRQIVESEKARAEYEA 593
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3314-3613 |
1.77e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 80.94 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3314 EKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEdkQLMQQRLEEETEEyhKSLEVERKRQLEimaEAERLR-- 3391
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFE--KMEQERLRQEKEE--KAREVERRRKLE---EAEKARqa 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3392 -------LQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQ-EKMTVVERLEFERLNTS----KEADDLRKAIAD 3459
Cdd:pfam17380 328 emdrqaaIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEiSRMRELERLQMERQQKNervrQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3460 LENEKARLKKEAEELQNKSKEMADAQQKKIEhektVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQ 3539
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVR----RLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK 483
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774674 3540 ERQKQQMEQEKKTLQATMDAalSKQKEAEEEMLRKQKEMQELERQRL---EQERILAEENqklREKLQQLEDAQKDQ 3613
Cdd:pfam17380 484 RDRKRAEEQRRKILEKELEE--RKQAMIEEERKRKLLEKEMEERQKAiyeEERRREAEEE---RRKQQEMEERRRIQ 555
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3271-3583 |
1.90e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3271 LAEEAENmrklAEDAARLSVEAQEA-ARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQ 3349
Cdd:COG1196 205 LERQAEK----AERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3350 KLLEDKQLMQQRLEEETEEYHKSLEVERKR-------QLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRL 3422
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERrreleerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3423 HETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMT 3502
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3503 EKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELE 3582
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
.
gi 1988774674 3583 R 3583
Cdd:COG1196 521 G 521
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2413-2896 |
2.98e-14 |
|
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: 80.06 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2413 EEVSKREIAAVDAEKQKTNIQlELQELKNLSEQQIKDKSQQVDEALHSRTkIEEEIRLIRIqletteKQKYTAESELKQL 2492
Cdd:NF033838 38 EEVRGGNNPTVTSSGNESQKE-HAKEVESHLEKILSEIQKSLDKRKHTQN-VALNKKLSDI------KTEYLYELNVLKE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2493 RDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEeelKRKSEAEKEAAKQKQKALEDL-----EKLRMQAEEAERQVK 2567
Cdd:NF033838 110 KSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEAT---KKVEEAEKKAKDQKEEDRRNYptntyKTLELEIAESDVEVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2568 QAEIEKEKQikvaheaaqksaaaelqskhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEK 2647
Cdd:NF033838 187 KAELELVKE-----------------------EAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2648 WRQKANEALrlrlqaEDEAHKKTLAQEEAEKQKEEAEREAKKR--AKAEESALKQKEMAEEELERQRKIAEstAQQKLTA 2725
Cdd:NF033838 244 KLKEAVEKN------VATSEQDKPKRRAKRGVLGEPATPDKKEndAKSSDSSVGEETLPSPSLKPEKKVAE--AEKKVEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2726 EQElirlRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELakvrsemdiliqlkTKAEKETMSNTEKSKQLLEA 2805
Cdd:NF033838 316 AKK----KAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELEL--------------VKEEAKEPRNEEKIKQAKAK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2806 EAAKMKdlaeEASRLraisEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAEN---ERLRR 2882
Cdd:NF033838 378 VESKKA----EATRL----EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQpkaEKPAD 449
|
490
....*....|....
gi 1988774674 2883 QAEDEAYQRKALED 2896
Cdd:NF033838 450 QQAEEDYARRSEEE 463
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2435-2914 |
3.15e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 80.34 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2435 ELQELKNLsEQQIKDKSQQVD-----EALHSR-TKIEEEIRLIRIQLETTekQKYTAESELKQLRDRAAEAEKLRKLAQD 2508
Cdd:COG4913 233 HFDDLERA-HEALEDAREQIEllepiRELAERyAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2509 EAEKLRKQVSEETQKKRQAEEEL-----KRKSEAEKEAAkQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEA 2583
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIrgnggDRLEQLEREIE-RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2584 AQkSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQ----EDAENSREEAEKEL-------------- 2645
Cdd:COG4913 389 AA-ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEALgldeaelpfvgeli 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2646 ------EKWRQKANEAL---RLRLQAEDEAHKKTLAQEEAEKQKE-------EAEREAKKRAKAEESALKQK-------- 2701
Cdd:COG4913 468 evrpeeERWRGAIERVLggfALTLLVPPEHYAAALRWVNRLHLRGrlvyervRTGLPDPERPRLDPDSLAGKldfkphpf 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2702 -EMAEEELERQRKIA--ESTAQQK-----LTAE------------QELIRLRAD----FDNAEQqRSLLEDELYRLKNEV 2757
Cdd:COG4913 548 rAWLEAELGRRFDYVcvDSPEELRrhpraITRAgqvkgngtrhekDDRRRIRSRyvlgFDNRAK-LAALEAELAELEEEL 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2758 AAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKE--------TMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKH 2829
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAELEELEE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2830 QRQIAEEEAARQRAEAERI------LKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAY-QRKALEDQASQHK 2902
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAeeeldeLQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEeRIDALRARLNRAE 786
|
570
....*....|..
gi 1988774674 2903 QEIEEKIVQLKK 2914
Cdd:COG4913 787 EELERAMRAFNR 798
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
1173-1270 |
3.38e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 71.64 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLD 1251
Cdd:cd21230 1 TPKQRLLGWIQ---NKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1988774674 1252 PEDVDVPHPDEKSIITYVS 1270
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2332-2976 |
3.71e-14 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 79.80 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2332 TLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDkqkqlaeahakAIAKAEKEAQELKLKM 2411
Cdd:pfam07111 52 SLELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELD-----------ALAVAEKAGQAEAEGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2412 QEEVSKREIAAVDAEKQKtniQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTekqkytaeselkq 2491
Cdd:pfam07111 121 RAALAGAEMVRKNLEEGS---QRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETK------------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2492 lrdRAAEAEKLrKLAQDEAEKLRKQVSeETQKKRQAEEELkrkseaekeaakqkqkaLEDLEKLRMQAEEAERQVKQAEI 2571
Cdd:pfam07111 185 ---RAGEAKQL-AEAQKEAELLRKQLS-KTQEELEAQVTL-----------------VESLRKYVGEQVPPEVHSQTWEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2572 EKEKQIKVAHEAaqKSAAAELQSkhmsfaekTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSR--EEAEKELEKWR 2649
Cdd:pfam07111 243 ERQELLDTMQHL--QEDRADLQA--------TVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEfpKKCRSLLNRWR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2650 QKANeALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERqrkIAESTAQQKLTAEQEL 2729
Cdd:pfam07111 313 EKVF-ALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVER---MSAKGLQMELSRAQEA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2730 -IRLRADFDNAEQQRSL-----------LEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAE--KETMSN 2795
Cdd:pfam07111 389 rRRQQQQTASAEEQLKFvvnamsstqiwLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQlrQESCPP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2796 TEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQiAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEA 2875
Cdd:pfam07111 469 PPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2876 ENERLRRQ--AEDEAYQRKALEDQASQHKQEIEEKIVQL------------KKSSEAEMERQKAIVDDTLKQRRVVEE-- 2939
Cdd:pfam07111 548 EVARQGQQesTEEAASLRQELTQQQEIYGQALQEKVAEVetrlreqlsdtkRRLNEARREQAKAVVSLRQIQHRATQEke 627
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1988774674 2940 ---EIRILKLNFEKASSGKLDLEL-ELNKLKNIADETQQSK 2976
Cdd:pfam07111 628 rnqELRRLQDEARKEEGQRLARRVqELERDKNLMLATLQQE 668
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2543-2895 |
4.01e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 79.78 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2543 KQKQKALEDLEKLRMQAE------EAERQVKQAEIEKEKQIKVAHEAAqksaaaeLQSKHMSFAEKTSKLEESLKQEhga 2616
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEkeekarEVERRRKLEEAEKARQAEMDRQAA-------IYAEQERMAMERERELERIRQE--- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2617 vlQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAedeAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 2696
Cdd:pfam17380 357 --ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA---ARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2697 AlKQKEMAEEELERQRKIaESTAQQKLTAEQELIRLRADfdnaeqqrslledelyrlknevaAAQQQRKQLEDElakvrs 2776
Cdd:pfam17380 432 A-RQREVRRLEEERAREM-ERVRLEEQERQQQVERLRQQ-----------------------EEERKRKKLELE------ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2777 emdiliqlktKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIA-EEEAARQRAEAER---ILKEK 2852
Cdd:pfam17380 481 ----------KEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAiYEEERRREAEEERrkqQEMEE 550
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1988774674 2853 LAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAyQRKALE 2895
Cdd:pfam17380 551 RRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
1173-1273 |
5.65e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 71.64 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 1252
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1988774674 1253 ED-VDVPHPDEKSIITYVSSLY 1273
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4733-4771 |
6.85e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 68.51 E-value: 6.85e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1988774674 4733 LLEAQAATGFIVDPLKNETLTVDEAVRKGVVGPEIHDKL 4771
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2599-3077 |
7.28e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 78.66 E-value: 7.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2599 FAEKTSKLEEsLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANealRLRLQAEDEAHKKTLAQEEAEK 2678
Cdd:COG4717 73 LKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ---LLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2679 qkeeaeREAKKRAKAEESALKQKEMAEEELER-QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEV 2757
Cdd:COG4717 149 ------EELEERLEELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2758 AAAQQQRKQLEDELA------KVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKmkdLAEEASRLRAISEEAKHQR 2831
Cdd:COG4717 223 EELEEELEQLENELEaaaleeRLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF---LVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2832 QIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAyqrKALEDQASQhkQEIEEKIVQ 2911
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA---EELEEELQL--EELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2912 LKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLeLELNKLKNIADETQQSKIRAEEEAEKLRKLal 2991
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEEELEEL-- 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2992 eeekrrreaeekvkkiaAAEEEAARQRKAALE---ELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQ 3068
Cdd:COG4717 452 -----------------REELAELEAELEQLEedgELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
....*....
gi 1988774674 3069 SVLAQQIED 3077
Cdd:COG4717 515 PPVLERASE 523
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2134-2919 |
9.38e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 78.68 E-value: 9.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2134 SDVKEVETYRAKLKKMRTEAEdeqPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRwkavftqidlrq 2213
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHE---AMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ------------ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2214 reLEQLGRQLGYYRESydwlirwIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQnkdkvdECQKYAKAYiDTI 2293
Cdd:pfam01576 231 --IAELRAQLAKKEEE-------LQAALARLEEETAQKNNALKKIRELEAQISELQEDLES------ERAARNKAE-KQR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2294 KDYELQLVAYKAQVEplvsplkkTKLDSAsdNIIQEyvtlrtryselmtLTSQYIKFITDTQRRLDDEEKAAEKLKAEER 2373
Cdd:pfam01576 295 RDLGEELEALKTELE--------DTLDTT--AAQQE-------------LRSKREQEVTELKKALEEETRSHEAQLQEMR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2374 KKMA----EMQAELDKQKQLAEAHAKAIAKAEKEAQELklkmQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKD 2449
Cdd:pfam01576 352 QKHTqaleELTEQLEQAKRNKANLEKAKQALESENAEL----QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2450 KSQQVDEAlhsrTKIEEEIRLIRIQLETTEKQKYTAESELKQL---------------RDRAAEAEKLRKLaQDEAEKLR 2514
Cdd:pfam01576 428 RAELAEKL----SKLQSELESVSSLLNEAEGKNIKLSKDVSSLesqlqdtqellqeetRQKLNLSTRLRQL-EDERNSLQ 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2515 KQVSEETQKKRQAEE----------ELKRKSEAEKEAAKQ----KQKALEDLEKLRMQAEEAERQVKQAEIEKEkqiKVA 2580
Cdd:pfam01576 503 EQLEEEEEAKRNVERqlstlqaqlsDMKKKLEEDAGTLEAleegKKRLQRELEALTQQLEEKAAAYDKLEKTKN---RLQ 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2581 HEAAQKSAAAELQSKHMSFAEKTS-KLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALR-- 2657
Cdd:pfam01576 580 QELDDLLVDLDHQRQLVSNLEKKQkKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERtn 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2658 --LRLQAEDEAHKKtlaqeeaeKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTaqqKLTAEQELIRLRAD 2735
Cdd:pfam01576 660 kqLRAEMEDLVSSK--------DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDA---KLRLEVNMQALKAQ 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2736 FDN--------AEQQRSLLEDELYRLKNEVAAAQQQRKQLEDelAKVRSEMDiLIQLKTKAEKETMSNTEKSKQLLEAEa 2807
Cdd:pfam01576 729 FERdlqardeqGEEKRRQLVKQVRELEAELEDERKQRAQAVA--AKKKLELD-LKELEAQIDAANKGREEAVKQLKKLQ- 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2808 AKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERiLKEKLAAiseatrlkteAEIALKEKEAENERLRRQAEDE 2887
Cdd:pfam01576 805 AQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQ-LQEDLAA----------SERARRQAQQERDELADEIASG 873
|
810 820 830
....*....|....*....|....*....|..
gi 1988774674 2888 AYQRKALEDQasqhKQEIEEKIVQLKKSSEAE 2919
Cdd:pfam01576 874 ASGKSALQDE----KRRLEARIAQLEEELEEE 901
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4400-4438 |
1.11e-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: 1.11e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1988774674 4400 LLEAQAASGFIVDPVRNQCLSVDEAVKSGVVGPELHEKL 4438
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
1051-1157 |
1.14e-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: 70.39 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1051 EDERDrvqKKTFTKWVNKHLIKAQRHvtDLYEDLRDGhnlISLLEVL--------SGETLPREKGRMRFHKLQNVQIALD 1122
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPLIN--NLYEDLRDG---LVLLQVLdkiqpgcvNWKKVNKPKPLNKFKKVENCNYAVD 72
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774674 1123 FLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 1157
Cdd:cd21219 73 LAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3026-3621 |
1.26e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 78.47 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3026 ERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQsVLAQQIEDSITQKKLKEEyEKAKKLAKEAEAAKEKA 3105
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAE-LIIDLEELKLQELKLKEQ-AKKALEYYQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3106 EREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQ 3185
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE-KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3186 KFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKD 3265
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3266 STQKLLAEEAENmRKLAEDAARLSVEAQEAARLRQIAEDDL---NQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKD 3342
Cdd:pfam02463 382 ESERLSSAAKLK-EEELELKSEEEKEAQLLLELARQLEDLLkeeKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3343 LAQEQAQKLLEDKqlmQQRLEEETEEYHKSLEVERK-----RQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADK 3417
Cdd:pfam02463 461 LKDELELKKSEDL---LKETQLVKLQEQLELLLSRQkleerSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3418 VATRLHETEIATQEKMTVVERLEFERLN----TSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEK 3493
Cdd:pfam02463 538 VENYKVAISTAVIVEVSATADEVEERQKlvraLTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3494 TVLQQTFMTEKEMLLKKEKLIE-------------------DEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQ 3554
Cdd:pfam02463 618 DDKRAKVVEGILKDTELTKLKEsakakesglrkgvsleeglAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774674 3555 ATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKV 3621
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3177-3609 |
1.54e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 77.50 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3177 KLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEeelfkvkvQMEELLKLKNKIEEEN 3256
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP--------LYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3257 QRLikkdkdstQKLLAEEAEnMRKLAEDAARLSVEAQEAarlrqiaeddlnqQRALAEKMLKEKMQAIQEASRLKAEAEM 3336
Cdd:COG4717 146 ERL--------EELEERLEE-LRELEEELEELEAELAEL-------------QEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3337 LQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEE---------- 3406
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3407 ------------EAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEEL 3474
Cdd:COG4717 284 gllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3475 QNKSKEmadaqqkkiEHEKTVLQQTFMTEKEMLLKKEKL------IEDEKKRLESQFEEEVKKAKALKDEQErqKQQMEQ 3548
Cdd:COG4717 364 QLEELE---------QEIAALLAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEELLEALD--EEELEE 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 3549 EKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQEriLAEENQKLREKLQQLEDA 3609
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE--LLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2686-2918 |
2.17e-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: 75.57 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2686 EAKKRAKAEESALKQK-EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 2764
Cdd:COG4942 20 DAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2765 KQLEDELAKVRSEMdiliqlktkaekETMSNTEKSKQLLEAEaakmkDLAEEASRLRAISEEAKHQRQIAEE------EA 2838
Cdd:COG4942 100 EAQKEELAELLRAL------------YRLGRQPPLALLLSPE-----DFLDAVRRLQYLKYLAPARREQAEElradlaEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2839 ARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEA 2918
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3020-3618 |
2.36e-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: 77.32 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3020 AALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQ------KCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKK 3093
Cdd:TIGR00618 170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctpcmpDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3094 LAKEAEAAkekaereaalLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfeaakraqaeaaaLMQKQQADTEMA 3173
Cdd:TIGR00618 250 EAQEEQLK----------KQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP-------------LAAHIKAVTQIE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3174 KHKKLAEQTLKQKfqvEQELTKVKLKLDETDKQKSVLDEE------LQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLK 3247
Cdd:TIGR00618 307 QQAQRIHTELQSK---MRSRAKLLMKRAAHVKQQSSIEEQrrllqtLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHT 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3248 LKNKIEEENQRLikkdKDSTQKLLAEEAENMRKLAEDAARlSVEAQEAARLR---QIAEDDLNQQRALAEKMLKEKMQAI 3324
Cdd:TIGR00618 384 LQQQKTTLTQKL----QSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKkqqELQQRYAELCAAAITCTAQCEKLEK 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3325 QEASR----LKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQ-----VS 3395
Cdd:TIGR00618 459 IHLQEsaqsLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQrgeqtYA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3396 QLSEAQARAEEEAKKFKKQA----DKVATRLHETEIATQEKMTVVERLEferlNTSKEADDLRKAIADLENEKARLKKEA 3471
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRaslkEQMQEIQQSFSILTQCDNRSKEDIP----NLQNITVRLQDLTEKLSEAEDMLACEQ 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3472 EELQNKSKEMADAQQKKIE----HEKTVLQQTFMTEKEMLLKKEK------LIEDEKKRLESQFEEEVKKAKALKDEQER 3541
Cdd:TIGR00618 615 HALLRKLQPEQDLQDVRLHlqqcSQELALKLTALHALQLTLTQERvrehalSIRVLPKELLASRQLALQKMQSEKEQLTY 694
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774674 3542 QKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRET 3618
Cdd:TIGR00618 695 WKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
1076-1155 |
2.57e-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: 69.54 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1076 HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM----RFHKLQNVQIALDFLRHRQV----KLVNIRNDDIADGNPKLT 1147
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1988774674 1148 LGLIWTII 1155
Cdd:cd21223 105 LALLWRII 112
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
1173-1273 |
2.58e-13 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 69.29 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKdLGVTRLLDP 1252
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1988774674 1253 ED-VDVPHPDEKSIITYVSSLY 1273
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2925-3621 |
2.99e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2925 AIVDDTLKQRRVVEEEIRILKlnFEKASSGKLDLELELNKLKniadETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKV 3004
Cdd:PRK03918 139 AILESDESREKVVRQILGLDD--YENAYKNLGEVIKEIKRRI----ERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3005 KKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVqSVLAQQIEDSITQKKL 3084
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI-EELEEKVKELKELKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3085 KEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKE-AEFEAAKRAQaeaaalm 3163
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRlEELEERHELY------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3164 qkqqadtEMAKHKKLAEQTLKQKFQVEqELTKVKLKLDETDKQKSVLDEELQRLKDEvddavkqRGQVEEELFKVKVQME 3243
Cdd:PRK03918 365 -------EEAKAKKEELERLKKRLTGL-TPEKLEKELEELEKAKEEIEEEISKITAR-------IGELKKEIKELKKAIE 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3244 ELLKLKNKIEEENQRLIKKDKdstQKLLAEEAENMRKLAEDAARLsveaqeAARLRQIaeddlnqqralaEKMLKEKMQA 3323
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHR---KELLEEYTAELKRIEKELKEI------EEKERKL------------RKELRELEKV 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3324 IQEASRLKAEAEMLQKQKDLAQEQAQKLLEDkqlmqqrLEEETEEYHKSLEverkRQLEIMAEAERLRLQVSQLSEAQAR 3403
Cdd:PRK03918 489 LKKESELIKLKELAEQLKELEEKLKKYNLEE-------LEKKAEEYEKLKE----KLIKLKGEIKSLKKELEKLEELKKK 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3404 AEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMAD 3483
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAE 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3484 AQqKKIEhektvlqqtfMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQatmdaalsK 3563
Cdd:PRK03918 638 TE-KRLE----------ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE--------K 698
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774674 3564 QKEAEEEMLRKQKEMQELERQRleqerilaEENQKLREKLQQLEDAQKDQHTRETDKV 3621
Cdd:PRK03918 699 LKEELEEREKAKKELEKLEKAL--------ERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2405-2964 |
3.52e-13 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 76.22 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2405 QELKlKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQ-QIKDKSQQVDEAlHSRTKIE-EEIRLIRIQLETTEKQK 2482
Cdd:pfam05701 42 LELE-KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEElKLNLERAQTEEA-QAKQDSElAKLRVEEMEQGIADEAS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2483 YTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQ----VSEETQKKRQAEEELKrkseaekeAAKQKQKALEDLEKLRMQ 2558
Cdd:pfam05701 120 VAAKAQLEVAKARHAAAVAELKSVKEELESLRKEyaslVSERDIAIKRAEEAVS--------ASKEIEKTVEELTIELIA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2559 AEEAERQVKQAEIEKEKqikvaheaaQKSAAAelqskhMSFAEKTSKLEESLKqehgavlQLQQEAERLKKQQEdaenSR 2638
Cdd:pfam05701 192 TKESLESAHAAHLEAEE---------HRIGAA------LAREQDKLNWEKELK-------QAEEELQRLNQQLL----SA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2639 EEAEKELEkwrqkANEALRLRLQAEDEAHKktlaqeeaekqKEEAEREAKKRAKAEESALKQKEM---AEEELERQRKIA 2715
Cdd:pfam05701 246 KDLKSKLE-----TASALLLDLKAELAAYM-----------ESKLKEEADGEGNEKKTSTSIQAAlasAKKELEEVKANI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2716 EstaqqKLTAEQELIRLRAdfdnaeqqrSLLEDELYRLKNEVAAAQQQR-------KQLEDELAKVRSEMDiLIQLKTKA 2788
Cdd:pfam05701 310 E-----KAKDEVNCLRVAA---------ASLRSELEKEKAELASLRQREgmasiavSSLEAELNRTKSEIA-LVQAKEKE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2789 EKETMsnTEKSKQLLEA--EAAKMKDLAEEA-SRLRAISEEAKHQRqiAEEEAARQRAEAerILKEKLAAIsEATRLKTE 2865
Cdd:pfam05701 375 AREKM--VELPKQLQQAaqEAEEAKSLAQAArEELRKAKEEAEQAK--AAASTVESRLEA--VLKEIEAAK-ASEKLALA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2866 AEIALKEKEAENERLRRQA----------EDEAYQRKALEDQASQHKQeIEEKIVQLKKSSEAEMeRQKAIVDDTLKQRR 2935
Cdd:pfam05701 448 AIKALQESESSAESTNQEDsprgvtlsleEYYELSKRAHEAEELANKR-VAEAVSQIEEAKESEL-RSLEKLEEVNREME 525
|
570 580
....*....|....*....|....*....
gi 1988774674 2936 VVEEEIRILKLNFEKASSGKLDLELELNK 2964
Cdd:pfam05701 526 ERKEALKIALEKAEKAKEGKLAAEQELRK 554
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2356-2895 |
3.59e-13 |
|
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: 76.32 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2356 RRLDDEEKAAEKLK---AEERKKMAEMQAELDK-QKQLAEAHAKAiaKAEKEAQELKLKMQEEVSK----REIAAVDAEK 2427
Cdd:pfam05557 27 RARIELEKKASALKrqlDRESDRNQELQKRIRLlEKREAEAEEAL--REQAELNRLKKKYLEALNKklneKESQLADARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2428 QKTNIQLELQELKnlseQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKL-RKLA 2506
Cdd:pfam05557 105 VISCLKNELSELR----RQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELeFEIQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2507 Q--DEAEKLRKQVSE-------ETQKKRQAEE-----ELKRKSEAEKEAAKQKQKALEDLEKlrMQAEEAERQVKQAEIE 2572
Cdd:pfam05557 181 SqeQDSEIVKNSKSElaripelEKELERLREHnkhlnENIENKLLLKEEVEDLKRKLEREEK--YREEAATLELEKEKLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2573 KEKQ--IKVAHEA--------AQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAE 2642
Cdd:pfam05557 259 QELQswVKLAQDTglnlrspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2643 KELEKWRQKAnealrLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTA--- 2719
Cdd:pfam05557 339 ALVRRLQRRV-----LLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELggy 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2720 -QQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQlktkaeketMSNTEK 2798
Cdd:pfam05557 414 kQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQG---------DYDPKK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2799 SK--QLLEAEAAKMKD-LAEEASRLRaiseeakhqrqiAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEA 2875
Cdd:pfam05557 485 TKvlHLSMNPAAEAYQqRKNQLEKLQ------------AEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKEL 552
|
570 580
....*....|....*....|
gi 1988774674 2876 ENERLRRQAEDEAYQRKALE 2895
Cdd:pfam05557 553 ESAELKNQRLKEVFQAKIQE 572
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2777-3551 |
5.87e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.16 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2777 EMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAI 2856
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2857 SEATRLKTEAEIALKEKEAENERLRRQaedeayqrkaleDQASQHKQEIEEKIVQlkkssEAEMERQKAIVDDTLKQRRV 2936
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQ------------QLLKQLRARIEELRAQ-----EAVLEETQERINRARKAAPL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2937 VEEEIRILKLNFeKASSGKLDLELELNKLkniADETQQSKIRAEEEAEKLRKLALeeEKRRREAEEKVKKIAAAEEEAAR 3016
Cdd:TIGR00618 296 AAHIKAVTQIEQ-QAQRIHTELQSKMRSR---AKLLMKRAAHVKQQSSIEEQRRL--LQTLHSQEIHIRDAHEVATSIRE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3017 QRKAALEELERLRKKAEEarKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAK 3096
Cdd:TIGR00618 370 ISCQQHTLTQHIHTLQQQ--KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3097 EAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHK 3176
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLT 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3177 KLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELlklknkieeen 3256
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL----------- 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3257 qrlikkdkdstQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKML-KEKMQAIQEASRLKAEAE 3335
Cdd:TIGR00618 597 -----------QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTaLHALQLTLTQERVREHAL 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3336 MLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKrQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQA 3415
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRE-LETHIEEYDREFNEIENASSSLGSDLAAREDALNQS 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3416 DKVATRLHETEIATQEkmtvverLEFERLNTSKEADDLRKA-IADLENEKARLKKEAEELQNKSKEMADAQQKKIEH--- 3491
Cdd:TIGR00618 745 LKELMHQARTVLKART-------EAHFNNNEEVTAALQTGAeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSded 817
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3492 EKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 3551
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4069-4107 |
6.59e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.81 E-value: 6.59e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1988774674 4069 LLEAQAGTGYLVDPVHNQKYTVDEAVKAGVVGPELHEKL 4107
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
1050-1161 |
1.12e-12 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 67.65 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1050 IEDERDrvqKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVL-------SGETLPREKGRMRFHKLQNVQIALD 1122
Cdd:cd21298 2 IEETRE---EKTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVE 76
|
90 100 110
....*....|....*....|....*....|....*....
gi 1988774674 1123 FLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 1161
Cdd:cd21298 77 LGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3166-3697 |
1.44e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.95 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3166 QQADTEMAKHKKLAEQTlkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQmeEL 3245
Cdd:COG4913 265 AAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD--RL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3246 LKLKNKIEEENQRLIKKDKDSTQklLAEEAENMR-KLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAI 3324
Cdd:COG4913 341 EQLEREIERLERELEERERRRAR--LEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3325 QEASRLKAEAEMLQKQK---DLAQEQAQKLLEDK------------QLMQQRLEEEteEYHKSLE-----------VERK 3378
Cdd:COG4913 419 RELRELEAEIASLERRKsniPARLLALRDALAEAlgldeaelpfvgELIEVRPEEE--RWRGAIErvlggfaltllVPPE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3379 RQLEIMA--EAERLRLQVSQLSEAQARAEEEAKKFKKQ--ADKVATRLH------ETEIATQEKMTVVERLE-FERLN-- 3445
Cdd:COG4913 497 HYAAALRwvNRLHLRGRLVYERVRTGLPDPERPRLDPDslAGKLDFKPHpfrawlEAELGRRFDYVCVDSPEeLRRHPra 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3446 -----------TSKEADDL-------------RKAIADLENEKARLKKEAEELQNKSKEMADAQQ--KKIEHEKTVLQQT 3499
Cdd:COG4913 577 itragqvkgngTRHEKDDRrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEY 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3500 FMTEKEMLLKKEKL--IEDEKKRLES------QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEM 3571
Cdd:COG4913 657 SWDEIDVASAEREIaeLEAELERLDAssddlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3572 LRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKVlhkdiihlTTIETTKTVYNGQNVGDVVDGI 3651
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAE--------EELERAMRAFNREWPAETADLD 808
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1988774674 3652 DKKPDPLAFDGIRDKVPASRLHELgvlpKKEFDKLKNgETTVQELG 3697
Cdd:COG4913 809 ADLESLPEYLALLDRLEEDGLPEY----EERFKELLN-ENSIEFVA 849
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2836-3473 |
1.87e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 74.37 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2836 EEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAL--EDQASQHKQEI--EEKIVQ 2911
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikENNATRHLCNLlkETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2912 LKKSSEAEMERQKAI-----VDDTLKQRRVVEEEIRI------LKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAE 2980
Cdd:pfam05483 168 AEKTKKYEYEREETRqvymdLNNNIEKMILAFEELRVqaenarLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2981 EEAEKLRKLaleeekrrreaeekvkKIAAAEEEAARQRKAALEELERLR-KKAEEARKQKDEADKEAEKQIVVAQQAAQK 3059
Cdd:pfam05483 248 QITEKENKM----------------KDLTFLLEESRDKANQLEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3060 CSAAEQQVQ---SVLAQQIEDSITQkkLKEEYEKAKKLAKEAEAAKEKAEREAALLR---QQAEEAERQKTAAEEEAANQ 3133
Cdd:pfam05483 312 QKALEEDLQiatKTICQLTEEKEAQ--MEELNKAKAAHSFVVTEFEATTCSLEELLRteqQRLEKNEDQLKIITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3134 AKAQEDAERLR--KEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTL---------------------------- 3183
Cdd:pfam05483 390 SSELEEMTKFKnnKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqarekeihdleiqltaiktseehy 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3184 -KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLiKK 3262
Cdd:pfam05483 470 lKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNL-RD 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3263 DKDSTQKLLAEEAENMR----KLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQ 3338
Cdd:pfam05483 549 ELESVREEFIQKGDEVKckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3339 KQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEE----------- 3407
Cdd:pfam05483 629 KQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiaemval 708
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3408 AKKFKKQADKVA----TRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEE 3473
Cdd:pfam05483 709 MEKHKHQYDKIIeerdSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5321-5359 |
2.37e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 64.27 E-value: 2.37e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1988774674 5321 LLEAQACTGGIIDPTSGEKYSIAEATEKGLVDKIMVDRL 5359
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2708-3589 |
2.70e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 74.31 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2708 LERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRslleDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTK 2787
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIR----DQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2788 AEK--ETMSNTEKSKQLLEAEAAKMKDLAEEAsrLRAISEEAK---HQRQIAEEEAARQRAEAERILKEKLAAISEATRL 2862
Cdd:TIGR00606 264 IMKldNEIKALKSRKKQMEKDNSELELKMEKV--FQGTDEQLNdlyHNHQRTVREKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2863 KTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQAS----QHKQEIEEKIVQLKKSSEAEMERQKAIV---------DD 2929
Cdd:TIGR00606 342 KTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfERGPFSERQIKNFHTLVIERQEDEAKTAaqlcadlqsKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2930 TLKQRRVVEEEIRILKLNfEKASSGKLDLELELNKLKNIADETQQ---SKIRAEEEAEKLRKLALEEEKRRREAEEKVKK 3006
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLG-RTIELKKEILEKKQEELKFVIKELQQlegSSDRILELDQELRKAERELSKAEKNSLTETLK 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3007 iaaaeeeaARQRKAALEELERLRKKAEEARKQKD-EADKEAEKQIvvaQQAAQKCSAAEQQVQSVLAQQIEDSITQ---- 3081
Cdd:TIGR00606 501 --------KEVKSLQNEKADLDRKLRKLDQEMEQlNHHTTTRTQM---EMLTKDKMDKDEQIRKIKSRHSDELTSLlgyf 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3082 ----------KKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQE---DAERLRKEAE 3148
Cdd:TIGR00606 570 pnkkqledwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDeesDLERLKEEIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3149 FEAAKRAQAEAAALMQKQQAdTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDET-----DKQKSvLDEELQRLKDEVDD 3223
Cdd:TIGR00606 650 KSSKQRAMLAGATAVYSQFI-TQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKlrlapDKLKS-TESELKKKEKRRDE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3224 AVkqrGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKD-STQKLLAEEAENMRKLAEDA-------ARLSVEAQEA 3295
Cdd:TIGR00606 728 ML---GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDiEEQETLLGTIMPEEESAKVCltdvtimERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3296 AR--LRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKqkdlaqeqaqkLLEDKQLMQQRLEEETEEyhksL 3373
Cdd:TIGR00606 805 ERkiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK-----------LIQDQQEQIQHLKSKTNE----L 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3374 EVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEiatQEKMTVVERLEFERLNTSKEADDL 3453
Cdd:TIGR00606 870 KSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ---QEKEELISSKETSNKKAQDKVNDI 946
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3454 RKAI-------ADLENE----KARLKKEAEELQNK---SKEMADAQQKKIEHEKTVLQQTFMTEK--EMLLKKE---KLI 3514
Cdd:TIGR00606 947 KEKVknihgymKDIENKiqdgKDDYLKQKETELNTvnaQLEECEKHQEKINEDMRLMRQDIDTQKiqERWLQDNltlRKR 1026
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774674 3515 EDEKKRLE---SQFEEEVKKAKALKDEQERQKqqMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQE 3589
Cdd:TIGR00606 1027 ENELKEVEeelKQHLKEMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2357-2882 |
2.84e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2357 RLDDEEKAAEKLKaEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqEEVSKREIAAVDAEKQKTNIQLEL 2436
Cdd:PRK03918 156 GLDDYENAYKNLG-EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVL----REINEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2437 QELKNLSEQqIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKqkytaesELKQLRDRAAEAEKLRKLAqDEAEKLRKQ 2516
Cdd:PRK03918 231 KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKK-------EIEELEEKVKELKELKEKA-EEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2517 VSEETQKKRQAEEELKRKSEAEKEAakqkQKALEDLEKLRMQAEEAERQVKqaEIEKEKqikvaheaaqksaaAELQSKH 2596
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGI----EERIKELEEKEERLEELKKKLK--ELEKRL--------------EELEERH 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2597 MSFAEKTSKLE--ESLKQEHGAvlqlqQEAERLKKQQEDAENSREEAEKELEKWRQK----ANEALRLRLQAE------- 2663
Cdd:PRK03918 362 ELYEEAKAKKEelERLKKRLTG-----LTPEKLEKELEELEKAKEEIEEEISKITARigelKKEIKELKKAIEelkkakg 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2664 ---------DEAHKKTLAQ---------EEAEKQKEEAEREAKKRAKAEESAL-------KQKEMAE------------- 2705
Cdd:PRK03918 437 kcpvcgrelTEEHRKELLEeytaelkriEKELKEIEEKERKLRKELRELEKVLkkeseliKLKELAEqlkeleeklkkyn 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2706 -EELERQRKIAESTAQQKLTAEQELIRLRADF-----------------DNAEQQRSLLEDELY---------------- 2751
Cdd:PRK03918 517 lEELEKKAEEYEKLKEKLIKLKGEIKSLKKELekleelkkklaelekklDELEEELAELLKELEelgfesveeleerlke 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2752 ---------RLKN---EVAAAQQQRKQLEDELAKVRSEMDiliQLKTKAEKETMSNTEKSKQLLEAEAAKMKD----LAE 2815
Cdd:PRK03918 597 lepfyneylELKDaekELEREEKELKKLEEELDKAFEELA---ETEKRLEELRKELEELEKKYSEEEYEELREeyleLSR 673
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774674 2816 EASRLRAISEEAKHQRQIAEEEAarqraeaeRILKEKLAAISEATRLKTEAEIALKEKEAENERLRR 2882
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTL--------EKLKEELEEREKAKKELEKLEKALERVEELREKVKK 732
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2390-2644 |
3.08e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.10 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2390 AEAHAKAIAKAEKEAQELKLKMQEEVSKREiaavDAEKQKTNIQLELQELknlsEQQIKDKSQQVDEalhsrtkIEEEIR 2469
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAAL----ERRIAALARRIRA-------LEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2470 LIRIQLETTEKQKYTAESELKQLRDRAAE-AEKLRKLAQDEAEKLRKQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKA 2548
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2549 LEDLEKLRmqaeeaerqvkqAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLK 2628
Cdd:COG4942 159 LAELAALR------------AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*.
gi 1988774674 2629 KQQEDAENSREEAEKE 2644
Cdd:COG4942 227 ALIARLEAEAAAAAER 242
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
1175-1274 |
4.22e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 65.44 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1175 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN---LENLEQAFSVAEK-DLGVTRLL 1250
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1988774674 1251 DPEDVdVPHPDEKSIITYVSSLYD 1274
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3742-3779 |
5.03e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 5.03e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1988774674 3742 LLEAQAATGYMLDPIKNQKLSVNAAVKEGLIGPELHNK 3779
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2495-2709 |
6.16e-12 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 71.38 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2495 RAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKaledleklrmQAEEAERQVKQAEIEKE 2574
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK----------QAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2575 KQIKVAHEAAQKSAAAElqskHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDA-ENSREEAEKELEKWRQKan 2653
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAE----AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAaAKAAAEAKKKAEAEAKK-- 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774674 2654 ealrlrlQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELE 2709
Cdd:PRK09510 210 -------KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2600-3045 |
9.44e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.99 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2600 AEKTSK-LEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLR-----LQ---AEDEAHKKT 2670
Cdd:PRK02224 197 EEKEEKdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEaeiedLRetiAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2671 LAQEEAEKQKEEAEREAKKRAKAEESAL----------------KQKEMAEEELERQR-----------------KIAES 2717
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLddadaeavearreeleDRDEELRDRLEECRvaaqahneeaeslredaDDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2718 TAQQKL----TAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQ--LKTKAEKE 2791
Cdd:PRK02224 357 RAEELReeaaELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREreAELEATLR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2792 TMSNT-EKSKQLLEA--------------EAAKMKDLAEEASRLRAISEEAKHQRQIAEE--EAARQRAEAERILKEKLA 2854
Cdd:PRK02224 437 TARERvEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEErlERAEDLVEAEDRIERLEE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2855 AISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLkksseAEMERQKAIVDDTLKQR 2934
Cdd:PRK02224 517 RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV-----AELNSKLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2935 RVVEEEirilklnFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLAleeekrrreaeekvKKIAAAEEEA 3014
Cdd:PRK02224 592 ERIRTL-------LAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELE--------------AEFDEARIEE 650
|
490 500 510
....*....|....*....|....*....|..
gi 1988774674 3015 ARQRKAALEE-LERLRKKAEEARKQKDEADKE 3045
Cdd:PRK02224 651 AREDKERAEEyLEQVEEKLDELREERDDLQAE 682
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2761-3611 |
1.03e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 72.17 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2761 QQQRKQLEDELAKVRSEMDiliQLKTKAEKETMSNTEKSKQ-------LLEAEAAKMK-------DLAEEASR-LRAISE 2825
Cdd:NF041483 7 QESHRADDDHLSRFEAEMD---RLKTEREKAVQHAEDLGYQvevlrakLHEARRSLASrpaydgaDIGYQAEQlLRNAQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2826 EAKHQRQIAEEEAARQRAEAERILKEKlaaISEATRLKTEAeialkEKEAeNERLRRQAEDEAYQRKALEDQ-------A 2898
Cdd:NF041483 84 QADQLRADAERELRDARAQTQRILQEH---AEHQARLQAEL-----HTEA-VQRRQQLDQELAERRQTVESHvnenvawA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2899 SQHKQEIEEKIVQLKKSSEAEMErqKAIVDDTLKQRRVVEEEIRILKLNFEKASSgkldlelelnklkniadETQQSKIR 2978
Cdd:NF041483 155 EQLRARTESQARRLLDESRAEAE--QALAAARAEAERLAEEARQRLGSEAESARA-----------------EAEAILRR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2979 AEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAAL---------EELERLRKKAEEARKQKDEADKEAEKQ 3049
Cdd:NF041483 216 ARKDAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELsraaeqrmqEAEEALREARAEAEKVVAEAKEAAAKQ 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3050 IVVAQQA-AQKCSAAEQQVQSVLAQQIEDSITQKKLKEEY-------EKAKKLAKEAEAAKEKAEREAALLRQQAEEAER 3121
Cdd:NF041483 296 LASAESAnEQRTRTAKEEIARLVGEATKEAEALKAEAEQAladaraeAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3122 QKTAAEE-EAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQA---DTE--MAKHKKLAEQTLKQKFQVEQeltk 3195
Cdd:NF041483 376 VLTKASEdAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAakdDTKeyRAKTVELQEEARRLRGEAEQ---- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3196 vkLKLDETDKQKSVLDEELQRLKDEVDDAVKqrgQVEEELFKVKVQMEElLKLKNKIEEENQRLIKKDKDSTQKLLAEEA 3275
Cdd:NF041483 452 --LRAEAVAEGERIRGEARREAVQQIEEAAR---TAEELLTKAKADADE-LRSTATAESERVRTEAIERATTLRRQAEET 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3276 enMRKLAEDAARLSVEAQE-AARLRQIAEDDLNQQRALAEK-MLKEKMQAIQEASRLKAEAEmlqkQKDLAQEQAqklLE 3353
Cdd:NF041483 526 --LERTRAEAERLRAEAEEqAEEVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAE----ERLTAAEEA---LA 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3354 DKQLMQQRLEEETEEYHKSLEV---ERKRQLEIMAEAERLRLQVSQLSEAQARaeeeakkfKKQADKVATRLHETEIATQ 3430
Cdd:NF041483 597 DARAEAERIRREAAEETERLRTeaaERIRTLQAQAEQEAERLRTEAAADASAA--------RAEGENVAVRLRSEAAAEA 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3431 EKMTVVERLEFERLNTSKEADDLR------KAIADLENEKARLKKEAEELQNKSKEMADAQQKKI-EHEKTVLQQTFMTE 3503
Cdd:NF041483 669 ERLKSEAQESADRVRAEAAAAAERvgteaaEALAAAQEEAARRRREAEETLGSARAEADQERERArEQSEELLASARKRV 748
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3504 KEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMD-AALSKQKEAEEEMLRKQKEMQElE 3582
Cdd:NF041483 749 EEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEhAAERTRTEAQEEADRVRSDAYA-E 827
|
890 900
....*....|....*....|....*....
gi 1988774674 3583 RQRleqeriLAEENQKLREKLQQLEDAQK 3611
Cdd:NF041483 828 RER------ASEDANRLRREAQEETEAAK 850
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3199-3612 |
1.06e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.99 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3199 KLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEE--------ENQRLIKKDKDSTQKL 3270
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDlretiaetEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3271 LAEEAENMRKLAEDAARLSVEAQEAARLRQiaeDDLNQQRALAEKMLKEKMQAIQEAsrlKAEAEMLQKQKDLAQEQAQK 3350
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEAVEARR---EELEDRDEELRDRLEECRVAAQAH---NEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3351 LLEDKQlmqqRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQ 3430
Cdd:PRK02224 361 LREEAA----ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3431 EKMTVVERLEfERLNTSK---------------EADDLRKAIADLENEKARLKKEAEELQNKSKEMADAqqKKIEHEKTV 3495
Cdd:PRK02224 437 TARERVEEAE-ALLEAGKcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL--VEAEDRIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3496 LQQTFMTEKEMLLKKEKLIEDEKKRLESQFEE--------EVKKAKALKDEQERQKQQ-----MEQEKKTLQATMDA--- 3559
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERaaeleaeaEEKREAAAEAEEEAEEAReevaeLNSKLAELKERIESler 593
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 3560 ---ALSKQKEAEEEMLR---KQKEMQELERQRLEQ-----ERI--LAEEN-----QKLREKLQQLEDAQKD 3612
Cdd:PRK02224 594 irtLLAAIADAEDEIERlreKREALAELNDERRERlaekrERKreLEAEFdeariEEAREDKERAEEYLEQ 664
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2507-2766 |
1.06e-11 |
|
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: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2507 QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKA-LEDLEKL--RMQAEEAERQVKQAEIEKEKQIKVAHEA 2583
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAeQARQKELeqRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2584 AQKSAaaelqskhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRlRLQAE 2663
Cdd:TIGR02794 125 KAKQA-----------AEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEA-KAKAE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2664 DEAHKKtlaqeeaekqkeeaeREAKKRAKAEESALKQKE-MAEEELERQRKIAESTAQQKLTAEQELirlradfdNAEQQ 2742
Cdd:TIGR02794 193 EAKAKA---------------EAAKAKAAAEAAAKAEAEaAAAAAAEAERKADEAELGDIFGLASGS--------NAEKQ 249
|
250 260
....*....|....*....|....
gi 1988774674 2743 RSLLEDELYRLKNEVAAAQQQRKQ 2766
Cdd:TIGR02794 250 GGARGAAAGSEVDKYAAIIQQAIQ 273
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3818-3855 |
1.43e-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: 1.43e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1988774674 3818 VLEAQLATGGIIDPINSHRVPTETAYKQGHYDAEMNKI 3855
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4810-4847 |
1.53e-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: 1.53e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1988774674 4810 LEAQTATGGIIDPEFQFHLPTDVAMQRGYINKETNEKL 4847
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
1053-1152 |
1.66e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 64.37 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1053 ERDRvQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLE-VLSGE-------TLPREKGRMRFHKLQNVQIALDFL 1124
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1988774674 1125 RHRQVKLVNIRNDDIADGNPKLTLGLIW 1152
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2533-2946 |
1.66e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2533 RKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQ 2612
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2613 EHGAVLQLQQEAERLKKQQEDaensREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAK 2692
Cdd:COG4717 144 LPERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2693 AE----ESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQR---------SLLEDELYRLKNEVAA 2759
Cdd:COG4717 220 EEleelEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2760 AQQQRKQLEDELAKVRSEMDILIQLKtkaeKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAE---- 2835
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELL----AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaal 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2836 --------EEAARQRAEAERI---LKEKLAAISEATRLKTEAEIALKEKEAEnERLRRQAEDEAYQRKALEDQASQHKQE 2904
Cdd:COG4717 376 laeagvedEEELRAALEQAEEyqeLKEELEELEEQLEELLGELEELLEALDE-EELEEELEELEEELEELEEELEELREE 454
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1988774674 2905 IEEKIVQLKK-SSEAEMERQKAIVDDTLKQRRVVEEEIRILKL 2946
Cdd:COG4717 455 LAELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3211-3585 |
1.89e-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: 71.25 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3211 DEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKiEEENQRLIKKDKDSTQKLLAEEAENMRKLAE--DAARL 3288
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKEKREYEGYELLKEKEALERQKEaiERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3289 SVEAQEAARLRQIaeDDLNQQRALAEKMLKEKMQAIQEasrlKAEAEMLQKQKDLA-----QEQAQKLLEDKQLMQQRLE 3363
Cdd:TIGR02169 248 SLEEELEKLTEEI--SELEKRLEEIEQLLEELNKKIKD----LGEEEQLRVKEKIGeleaeIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3364 EETEEYhkslEVERKRQLEimaEAERLRLQVSQLseaqaraeeeakkfKKQADKVATRLHETEiatQEKMTVVERLEFEr 3443
Cdd:TIGR02169 322 ERLAKL----EAEIDKLLA---EIEELEREIEEE--------------RKRRDKLTEEYAELK---EELEDLRAELEEV- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3444 lntSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEhektvlqqtfmtEKEMLLKKEKLIEDEKKRLES 3523
Cdd:TIGR02169 377 ---DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE------------ELADLNAAIAGIEAKINELEE 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 3524 QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMdaalSKQKEAEEEMLRKQKEMQELERQR 3585
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK----EEYDRVEKELSKLQRELAEAEAQA 499
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
1175-1275 |
2.23e-11 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 63.53 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1175 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPED 1254
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1988774674 1255 VdVPHPDEKSIITYVSSLYDA 1275
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2525-2928 |
2.64e-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: 70.75 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2525 RQAEEE---LKRKSEAEKE-AAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAeLQSKHMSFA 2600
Cdd:COG3096 275 RHANERrelSERALELRRElFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2601 EKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWrQKANEALRLR-------LQAEDEAhkKTLAQ 2673
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADY-QQALDVQQTRaiqyqqaVQALEKA--RALCG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2674 EEAEKQKEEAEREAKKRAKAEES-----ALKQK----EMA----EEELERQRKIA-ESTAQQKLTAEQELIRLRADFDNA 2739
Cdd:COG3096 431 LPDLTPENAEDYLAAFRAKEQQAteevlELEQKlsvaDAArrqfEKAYELVCKIAgEVERSQAWQTARELLRRYRSQQAL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2740 EQQRSLLEDELYRLKNEVAAAQQQRKQLEdELAKvrsemdiliqlktKAEKETMSNTEKSKQLLEAEAaKMKDLAEEASR 2819
Cdd:COG3096 511 AQRLQQLRAQLAELEQRLRQQQNAERLLE-EFCQ-------------RIGQQLDAAEELEELLAELEA-QLEELEEQAAE 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2820 LRAISEEAKHQRqiaeEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAyQRKALEDQAS 2899
Cdd:COG3096 576 AVEQRSELRQQL----EQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERER-EATVERDELA 650
|
410 420
....*....|....*....|....*....
gi 1988774674 2900 QHKQEIEEKIVQLKKSSEAEMERQKAIVD 2928
Cdd:COG3096 651 ARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
3186-3611 |
3.41e-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: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3186 KFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEE-LFKVKVQMEELLKLKNKIEEENQR---LIK 3261
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERlkaLTG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3262 KDKDSTQKLLAEEA----ENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQ-RALAEKMLKEKMQAIQEASRLKAEAEM 3336
Cdd:pfam12128 369 KHQDVTAKYNRRRSkikeQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeSELREQLEAGKLEFNEEEYRLKSRLGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3337 LQKQKDLAQeqaqklLEDKQLMQQRLEEEteeyhkslEVERKRQLEIMAEAERLRLQvsqlseaqaraeEEAKKFKKQAD 3416
Cdd:pfam12128 449 LKLRLNQAT------ATPELLLQLENFDE--------RIERAREEQEAANAEVERLQ------------SELRQARKRRD 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3417 KVATRLHETEIATQEKMTVVERLE---FERLNTSKEAddLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHE- 3492
Cdd:pfam12128 503 QASEALRQASRRLEERQSALDELElqlFPQAGTLLHF--LRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNl 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3493 ---KTVLQQTFMTEKEMLlkkekliEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEE 3569
Cdd:pfam12128 581 ygvKLDLKRIDVPEWAAS-------EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL 653
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1988774674 3570 EMLRKQKEMQELERQRleqERILAEENQKLREKLQQLEDAQK 3611
Cdd:pfam12128 654 DLRRLFDEKQSEKDKK---NKALAERKDSANERLNSLEAQLK 692
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2137-2630 |
3.58e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2137 KEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQREL 2216
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2217 EQLGRQLGYYRESY-DWLIRWIADAKQRQEKIQAvpitdsktLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKD 2295
Cdd:COG1196 361 AEAEEALLEAEAELaEAEEELEELAEELLEALRA--------AAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2296 YELQLVAYKAQVEplvsplkktKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKK 2375
Cdd:COG1196 433 LEEEEEEEEEALE---------EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2376 MAEMQAELDKQKQLA---------------EAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQ--KTNIQLELQE 2438
Cdd:COG1196 504 EGFLEGVKAALLLAGlrglagavavligveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgrATFLPLDKIR 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2439 LKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEK-----QKYTAESELKQLRDRAAEAEKLRKLAQDEAEKL 2513
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRtlvaaRLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2514 RKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQ 2593
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
490 500 510
....*....|....*....|....*....|....*..
gi 1988774674 2594 SKHMSFAEKTSKLEESLKQEhgavlQLQQEAERLKKQ 2630
Cdd:COG1196 744 EEELLEEEALEELPEPPDLE-----ELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3456-3620 |
3.71e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3456 AIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLEsQFEEEVKKAKAL 3535
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEE-LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3536 KDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHT 3615
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
....*
gi 1988774674 3616 RETDK 3620
Cdd:COG1196 391 ALRAA 395
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1536-1725 |
4.13e-11 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 65.93 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1536 LRYVQDLLAWVEENQRRIDNAEWGSDLPSMESQLGSHRGLHQTVEDFKSKIERAKADETQL---SPVSKGTYREYLGKLD 1612
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1613 LQYGKLLNSSKSRLRNLE---SLHAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDI 1689
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1988774674 1690 QALGDRLVRDGHPGK-KTVESFTAALQTQWSWILQLC 1725
Cdd:cd00176 166 NELAEELLEEGHPDAdEEIEEKLEELNERWEELLELA 202
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2375-2716 |
5.19e-11 |
|
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: 68.02 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2375 KMAEMQAELDKQKqlaeAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLEL--QELKNLSEQQIKDKSQ 2452
Cdd:pfam13868 16 LAAKCNKERDAQI----AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyrQELEEQIEEREQKRQE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2453 QVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELK 2532
Cdd:pfam13868 92 EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2533 RKSEAEKEAAKQKqkaledlEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsfAEKTSKLEESLKQ 2612
Cdd:pfam13868 172 EAEREEIEEEKER-------EIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREE-----AEKKARQRQELQQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2613 EHgavlQLQQEAERLKKQQEdaensREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAK 2692
Cdd:pfam13868 240 AR----EEQIELKERRLAEE-----AEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAER 310
|
330 340 350
....*....|....*....|....*....|.
gi 1988774674 2693 AEESALKQKEMAEEEL-------ERQRKIAE 2716
Cdd:pfam13868 311 EEELEEGERLREEEAErrerieeERQKKLKE 341
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4145-4183 |
5.56e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.03 E-value: 5.56e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1988774674 4145 LLDAQMTTGGIIDPVKSHRIPHDVACKRNYFDDEMKQAL 4183
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
1050-1158 |
5.77e-11 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 62.99 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1050 IEDERDRVQ--KKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLP----REKGRMRFHKLQNVQIALDF 1123
Cdd:cd21222 7 FDEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALEL 86
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774674 1124 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1158
Cdd:cd21222 87 MEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4476-4514 |
5.78e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.03 E-value: 5.78e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1988774674 4476 LLEAQIVSGGIIDPVKSHRVPTDVAYQKNILSRDIAKTL 4514
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2485-2722 |
5.93e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 68.25 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2485 AESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVseetqkkRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAER 2564
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2565 QVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsfAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKE 2644
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2645 LEKWRQ--KANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 2722
Cdd:COG4942 173 RAELEAllAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3214-3612 |
6.34e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3214 LQRLKDEVDDAVKQRGQ-----------VEEELFKVKVQMEELLKLKNKIEEENQRL---------IKKDKDSTQKLLA- 3272
Cdd:COG4717 48 LERLEKEADELFKPQGRkpelnlkelkeLEEELKEAEEKEEEYAELQEELEELEEELeeleaeleeLREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3273 -----EEAENMRKLAEDAARL-SVEAQEAARLRQIAE-DDLNQ-----QRALAEKMLKEKMQAIQEASRLKAEAEMLQKQ 3340
Cdd:COG4717 128 lplyqELEALEAELAELPERLeELEERLEELRELEEElEELEAelaelQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3341 KDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEE-------------- 3406
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvlglla 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3407 --------EAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKS 3478
Cdd:COG4717 288 llflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3479 KEmadaqqkkiEHEKTVLQQTFMTEKEMLLKKEKL------IEDEKKRLESQFEEEVKKAKALKDEQErqKQQMEQEKKT 3552
Cdd:COG4717 368 LE---------QEIAALLAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEELLEALD--EEELEEELEE 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 3553 LQAtmdaalsKQKEAEEEMLRKQKEMQELERQ--RLEQERILAEENQKLREKLQQLEDAQKD 3612
Cdd:COG4717 437 LEE-------ELEELEEELEELREELAELEAEleQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2775-3496 |
7.72e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.48 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2775 RSEMDILIQLKTKAEKETMSNTEKSKQLL---EAEAAKMKDLAEEAS-------RLRAISEEAK-HQRQIAEEEAARQRA 2843
Cdd:pfam12128 205 ILEDDGVVPPKSRLNRQQVEHWIRDIQAIagiMKIRPEFTKLQQEFNtlesaelRLSHLHFGYKsDETLIASRQEERQET 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2844 EAEriLKEKLAA--------ISEATRLKTEAEIALKEKEAENERLRRQA----EDEAYQRKALEDQASQHKQEIEEKIVQ 2911
Cdd:pfam12128 285 SAE--LNQLLRTlddqwkekRDELNGELSAADAAVAKDRSELEALEDQHgaflDADIETAAADQEQLPSWQSELENLEER 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2912 LK------KSSEAEMERQKAIVDDTLKqrRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEK 2985
Cdd:pfam12128 363 LKaltgkhQDVTAKYNRRRSKIKEQNN--RDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEY 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2986 LRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKqivvAQQAAQKCSAAEQ 3065
Cdd:pfam12128 441 RLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ----ASEALRQASRRLE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3066 QVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEaakekaereaalLRQQAEEAERQKTAAEEEAANQAKAQE------- 3138
Cdd:pfam12128 517 ERQSALDELELQLFPQAGTLLHFLRKEAPDWEQS------------IGKVISPELLHRTDLDPEVWDGSVGGElnlygvk 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3139 -DAERLRKEAEFEAAKRAQAEAAALmqKQQADTEMAKHKKLAEQTLKQKFQVEQ---ELTKVKLKLDETDKQKSVLDEEL 3214
Cdd:pfam12128 585 lDLKRIDVPEWAASEEELRERLDKA--EEALQSAREKQAAAEEQLVQANGELEKasrEETFARTALKNARLDLRRLFDEK 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3215 QRLKDEVDDAVKQR-GQVEEELFKVKVQMEELL-KLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAE-DAARLSVE 3291
Cdd:pfam12128 663 QSEKDKKNKALAERkDSANERLNSLEAQLKQLDkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALlKAAIAARR 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3292 AQEAARLRQIAEDdlnQQRALAEKMLKEkmqaiQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHK 3371
Cdd:pfam12128 743 SGAKAELKALETW---YKRDLASLGVDP-----DVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLAT 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3372 SLEverkrqlEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLheteiatQEKMTVVeRLEFERLNTSKEAD 3451
Cdd:pfam12128 815 QLS-------NIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRL-------SENLRGL-RCEMSKLATLKEDA 879
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1988774674 3452 DlrkaIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVL 3496
Cdd:pfam12128 880 N----SEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVI 920
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2704-2925 |
9.01e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 67.55 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2704 AEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQ 2783
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2784 lktkAEKETMSNTEKSKQLLEAEaakmkDLAEEASRLRAISEEAKHQRQI------AEEEAARQRAEAERILKEKLAAIS 2857
Cdd:COG3883 94 ----ALYRSGGSVSYLDVLLGSE-----SFSDFLDRLSALSKIADADADLleelkaDKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774674 2858 EATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKA 2925
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3346-3636 |
9.40e-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: 68.93 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3346 EQAQKLLEDKQLMQQRLE---EETEEYHKSLEVERK---RQLEIMAEAERLRLQVSQLSEAQARAEEeaKKFKKQADKVA 3419
Cdd:TIGR02168 175 KETERKLERTRENLDRLEdilNELERQLKSLERQAEkaeRYKELKAELRELELALLVLRLEELREEL--EELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3420 TRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKA-------IADLENEKARLKKEAEELQNKSKEMADAQQKKIEHe 3492
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESK- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3493 ktvlqqtfmteKEMLLKKEKLIEDEKKRLESQFEEEVKKAKalkdEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEML 3572
Cdd:TIGR02168 332 -----------LDELAEELAELEEKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774674 3573 RKQKEMQELERQ--RLEQER-ILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDIIHLTTIETTK 3636
Cdd:TIGR02168 397 SLNNEIERLEARleRLEDRReRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2525-3038 |
9.50e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2525 RQAEEELKRKSEAEKEA--AKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKqikVAHEAAQKsAAAELQskhmsfaek 2602
Cdd:COG4913 228 DALVEHFDDLERAHEALedAREQIELLEPIRELAERYAAARERLAELEYLRAA---LRLWFAQR-RLELLE--------- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2603 tsKLEESLKQEHGavlQLQQEAERLKKQQEDAENSREEAEkelEKWRQKANEALRlRLQAEDEAHKKTLaqeeaekqkee 2682
Cdd:COG4913 295 --AELEELRAELA---RLEAELERLEARLDALREELDELE---AQIRGNGGDRLE-QLEREIERLEREL----------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2683 aeREAKKRAKAEESALKQKEMA----EEELERQRKIAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVA 2758
Cdd:COG4913 355 --EERERRRARLEALLAALGLPlpasAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2759 AAQQQ-----------RKQLEDELAKVRSEMDI---LIQLKTKAEKETMS--------------------------NTEK 2798
Cdd:COG4913 430 SLERRksniparllalRDALAEALGLDEAELPFvgeLIEVRPEEERWRGAiervlggfaltllvppehyaaalrwvNRLH 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2799 SKQLLEAEAAKMKDLAEEASRL-------------------------------------------RAISEE--AKH---- 2829
Cdd:COG4913 510 LRGRLVYERVRTGLPDPERPRLdpdslagkldfkphpfrawleaelgrrfdyvcvdspeelrrhpRAITRAgqVKGngtr 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2830 -----QRQIAEE-----EAARQRAEAERILKEKLAAISEATRLKTEaeiaLKEKEAENERLRRQAEDEAYQRKALEDQAS 2899
Cdd:COG4913 590 hekddRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2900 QHKQ--EIEEKIVQLKKSS------EAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEkassgklDLELELNKLKNIADE 2971
Cdd:COG4913 666 AEREiaELEAELERLDASSddlaalEEQLEELEAELEELEEELDELKGEIGRLEKELE-------QAEEELDELQDRLEA 738
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774674 2972 tqqskirAEEEAEKLRKLALEEEKRRREAEEKVKKIaaaEEEAARQRKAALEELERLRKKAEEARKQ 3038
Cdd:COG4913 739 -------AEDLARLELRALLEERFAAALGDAVEREL---RENLEERIDALRARLNRAEEELERAMRA 795
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4971-5009 |
1.06e-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: 1.06e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1988774674 4971 LLESQAATGYVIDPIKNLKLTVNEAVKMGIVGPEFKDKL 5009
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5319-5356 |
1.12e-10 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 59.42 E-value: 1.12e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1988774674 5319 QRLLEAQACTGGIIDPTSGEKYSIAEATEKGLVDKIMV 5356
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1175-1270 |
1.24e-10 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 61.63 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1175 KEKLLLWSQRMtdgYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLI-NMGKVYQQTNLENLEQAFSVAEKDLGVTRLLDPE 1253
Cdd:cd21229 5 KKLMLAWLQAV---LPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1988774674 1254 DVDVPHPDEKSIITYVS 1270
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2489-2908 |
1.55e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.87 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2489 LKQLRDRAAEAEKLR----KLAQDEAEKLRKQVSEETQKK---RQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEE 2561
Cdd:COG4717 48 LERLEKEADELFKPQgrkpELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2562 AERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEEsLKQEHGAVLQL-----QQEAERLKKQQEDAEN 2636
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE-LQEELEELLEQlslatEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2637 SREEAEKELEKWRQKANEALR----LRLQAEDEAHKKTLAQEEAEKQ--------------------------------- 2679
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEeleqLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgll 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2680 KEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLED-ELYRLKNEVA 2758
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2759 AAQQQRKQLEDElAKVRSEMDILIQLKTKAEKEtmsntEKSKQLLEAEAAkMKDLAEEASRLRAISEEAKHQRQIAEEEA 2838
Cdd:COG4717 367 ELEQEIAALLAE-AGVEDEEELRAALEQAEEYQ-----ELKEELEELEEQ-LEELLGELEELLEALDEEELEEELEELEE 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 2839 ARQRAEAERI-LKEKLAAISEATR-LKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQA-SQHKQEIEEK 2908
Cdd:COG4717 440 ELEELEEELEeLREELAELEAELEqLEEDGELAELLQELEELKAELRELAEEWAALKLALELlEEAREEYREE 512
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2526-2929 |
2.02e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.06 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2526 QAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVkQAEIEKEKQIKVAHEAA----QKSAAAELQSKHM---- 2597
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMAREL-AELNEAESDLEQDYQAAsdhlNLVQTALRQQEKIeryq 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2598 -SFAEKTSKLEESLkqehgAVLQLQQEaerlkkQQEDAENSREEAEKELEKWR------QKANEALRLR-------LQAE 2663
Cdd:PRK04863 355 aDLEELEERLEEQN-----EVVEEADE------QQEENEARAEAAEEEVDELKsqladyQQALDVQQTRaiqyqqaVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2664 DEAhkKTLAQEEAEKQKEEAEREAKKRAKAEESALkqkemAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQ- 2742
Cdd:PRK04863 424 ERA--KQLCGLPDLTADNAEDWLEEFQAKEQEATE-----ELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWd 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2743 --RSLLED--ELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKeTMSNTEKSKQLLEAEAAKMKDLAEEAS 2818
Cdd:PRK04863 497 vaRELLRRlrEQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGK-NLDDEDELEQLQEELEARLESLSESVS 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2819 RLRAISEEAKHQRqiaeEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAlEDQA 2898
Cdd:PRK04863 576 EARERRMALRQQL----EQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVE-RDEL 650
|
410 420 430
....*....|....*....|....*....|.
gi 1988774674 2899 SQHKQEIEEKIVQLKKSSEAEMERQKAIVDD 2929
Cdd:PRK04863 651 AARKQALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2846-3613 |
2.22e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.84 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2846 ERILKEKLAAISEATRLKTEAEiALKEKEAENER-----LRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEaEM 2920
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLNESN-ELHEKQKFYLRqsvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH-EL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2921 ERQKAIVDDTLKQ--------RRV------VEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAE-- 2984
Cdd:pfam15921 155 EAAKCLKEDMLEDsntqieqlRKMmlshegVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEis 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2985 --KLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALE---ELERLRKKAEEARKQKDEADKEAEkqiVVAQQAAQK 3059
Cdd:pfam15921 235 ylKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEhevEITGLTEKASSARSQANSIQSQLE---IIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3060 CSAAEQQVQsvlaqQIEDSITQkkLKEEYEKAKKlakeaeaakekaereaaLLRQQAEEAERQKTAAeeeaanqakaqeD 3139
Cdd:pfam15921 312 NSMYMRQLS-----DLESTVSQ--LRSELREAKR-----------------MYEDKIEELEKQLVLA------------N 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3140 AERLRKEAEFEAAKRAQAEAAALMQKQQADTemakHKKLAEQTLkqkfqvEQELTKvklKLDETDKQKSVLDEELQRlkd 3219
Cdd:pfam15921 356 SELTEARTERDQFSQESGNLDDQLQKLLADL----HKREKELSL------EKEQNK---RLWDRDTGNSITIDHLRR--- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3220 EVDDAVKQRGQVEEELFKVKV----QMEELLKlknKIEEENQRLIKKDKDSTQklLAEEAENMRKLAED--AARLSVEAQ 3293
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSecqgQMERQMA---AIQGKNESLEKVSSLTAQ--LESTKEMLRKVVEEltAKKMTLESS 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3294 EaarlRQIAedDLNQQralaekmLKEKMQAIQEASrlkAEAEMLQKQKDLAQEQAQKL------LEDKQLMQQRLEEETE 3367
Cdd:pfam15921 495 E----RTVS--DLTAS-------LQEKERAIEATN---AEITKLRSRVDLKLQELQHLknegdhLRNVQTECEALKLQMA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3368 EYHKSLEVERKrQLEIMAE--------AERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQ----EKMTV 3435
Cdd:pfam15921 559 EKDKVIEILRQ-QIENMTQlvgqhgrtAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSdlelEKVKL 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3436 V----ERLEFERlNTSKEADDLRKAIADLENEKARLKKEAEELQ----NKSKEMADAQQK---KIEHEKTVLQQTFMTEK 3504
Cdd:pfam15921 638 VnagsERLRAVK-DIKQERDQLLNEVKTSRNELNSLSEDYEVLKrnfrNKSEEMETTTNKlkmQLKSAQSELEQTRNTLK 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3505 EM----------LLKKEKLIEDEKKRLES-----QFEEEV-----KKAKALKDEQERQKQQME---QEKKTLQATMDAAL 3561
Cdd:pfam15921 717 SMegsdghamkvAMGMQKQITAKRGQIDAlqskiQFLEEAmtnanKEKHFLKEEKNKLSQELStvaTEKNKMAGELEVLR 796
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 3562 SKQKEAEEEMLRKQKEMQELERQRLE-QERILAEENQKLREKLQQLEDAQKDQ 3613
Cdd:pfam15921 797 SQERRLKEKVANMEVALDKASLQFAEcQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2361-2594 |
3.47e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.60 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2361 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEahakaiakaekeAQELKlkmqeevskreiaavdaekqktniQLELQELK 2440
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAE------------QERLK------------------------QLEKERLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2441 nlSEQQIKDKSQQVDEALHSRTKIEEEirliriQLETTEKQKYTAESELKQLRDRAAEAE-KLRKLAQDEAEklrKQVSE 2519
Cdd:PRK09510 113 --AQEQKKQAEEAAKQAALKQKQAEEA------AAKAAAAAKAKAEAEAKRAAAAAKKAAaEAKKKAEAEAA---KKAAA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2520 ETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQS 2594
Cdd:PRK09510 182 EAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2355-2576 |
3.83e-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: 66.69 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2355 QRRLDDEEKAAEKLKAEERKK------MAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL----KLKMQEEVSKREIAAVD 2424
Cdd:pfam17380 340 ERMAMERERELERIRQEERKRelerirQEEIAMEISRMRELERLQMERQQKNERVRQELeaarKVKILEEERQRKIQQQK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2425 AEKQKTNIQLE---LQELKNLSEQQIKDKSQQVDEALHSRTKIE------EEIRLIRIQLETTEKQKYTAESELKQLRDR 2495
Cdd:pfam17380 420 VEMEQIRAEQEearQREVRRLEEERAREMERVRLEEQERQQQVErlrqqeEERKRKKLELEKEKRDRKRAEEQRRKILEK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2496 AAEAeklRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQ------------KALEdlEKLRMQAEEAE 2563
Cdd:pfam17380 500 ELEE---RKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEmeerrriqeqmrKATE--ERSRLEAMERE 574
|
250
....*....|...
gi 1988774674 2564 RQVKQAEIEKEKQ 2576
Cdd:pfam17380 575 REMMRQIVESEKA 587
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2127-2654 |
3.96e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2127 REVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKasavSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVF 2206
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE----LEERIEELKKEIEELEEKVKELKELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2207 TQIDLRQRELEQLGR---QLGYYRESYDWLIRWIADAKQRQEKIqavpitdsktlkeqlaqeKKLLEEIEQNKDKVDECQ 2283
Cdd:PRK03918 297 KLSEFYEEYLDELREiekRLSRLEEEINGIEERIKELEEKEERL------------------EELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2284 KYAKAYiDTIKDYELQLVAYKAQ-----VEPLVSPLK-----KTKLDSASDNIIQEYVTLRTRYSELMTLTSQY--IKFI 2351
Cdd:PRK03918 359 ERHELY-EEAKAKKEELERLKKRltgltPEKLEKELEelekaKEEIEEEISKITARIGELKKEIKELKKAIEELkkAKGK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2352 TDTQRRLDDEEKAAEkLKAEERKKMAEMQAELdkqKQLAEAHAKaiAKAEKEAQELKLKMQEEVSK-REIAavdaeKQKT 2430
Cdd:PRK03918 438 CPVCGRELTEEHRKE-LLEEYTAELKRIEKEL---KEIEEKERK--LRKELRELEKVLKKESELIKlKELA-----EQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2431 NIQlelQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKqkytAESELKQLRDRAAEAEKLRKLAQDEA 2510
Cdd:PRK03918 507 ELE---EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKEL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2511 EKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAER--QVKQAEIEK-EKQIKVAHEAAQKS 2587
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEelAETEKRLEElRKELEELEKKYSEE 659
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774674 2588 AAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKeLEKWRQKANE 2654
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEE 725
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2365-2825 |
4.41e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 66.77 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2365 AEKLKAEERKKMAEMQAEldKQKQLAEAHAKA---IAKAEKEAQE-------LKLKMQEEVSK-REIAAVDAEKQKTNIQ 2433
Cdd:NF041483 737 SEELLASARKRVEEAQAE--AQRLVEEADRRAtelVSAAEQTAQQvrdsvagLQEQAEEEIAGlRSAAEHAAERTRTEAQ 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2434 LELQELKNlseqqikDKSQQVDEALHSRTKIEEEIRliriqlETTEKQKYTAEselKQLRDRAAEAEKLRKLAQDEAEKL 2513
Cdd:NF041483 815 EEADRVRS-------DAYAERERASEDANRLRREAQ------EETEAAKALAE---RTVSEAIAEAERLRSDASEYAQRV 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2514 RKQVSEetqkkrqaeeelkRKSEAEKEAAKQKQKALEDLEKLRMQA------------EEAERQVKQAEIEKEKQIKVAH 2581
Cdd:NF041483 879 RTEASD-------------TLASAEQDAARTRADAREDANRIRSDAaaqadrligeatSEAERLTAEARAEAERLRDEAR 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2582 EAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKqqeDAENSREEAEKELEKWRQKA-NEALRLRL 2660
Cdd:NF041483 946 AEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRT---EAERVKAEAAAEAERLRTEArEEADRTLD 1022
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2661 QAEDEAHKK-TLAQEEAEKQKEEAEREAKK-RAKAEESALKQKEMAEEEL---------ERQRKIAESTAQ--------- 2720
Cdd:NF041483 1023 EARKDANKRrSEAAEQADTLITEAAAEADQlTAKAQEEALRTTTEAEAQAdtmvgaarkEAERIVAEATVEgnslvekar 1102
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2721 -------------------------QKLTAEQELIRLRADFDNAEQQRSLLEdelyRLKNEVAAAQQQRKQLE------- 2768
Cdd:NF041483 1103 tdadellvgarrdataireraeelrDRITGEIEELHERARRESAEQMKSAGE----RCDALVKAAEEQLAEAEakakelv 1178
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2769 ----DELAKVR----SEMDILI---------------QLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISE 2825
Cdd:NF041483 1179 sdanSEASKVRiaavKKAEGLLkeaeqkkaelvreaeKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAEISRVQDVLE 1258
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3262-3601 |
5.65e-10 |
|
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: 64.55 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3262 KDKDSTQKLLAEEAENMRKLAEdAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQK 3341
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMME-EERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3342 DLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQvsqlseaqaraeeeakKFKKQADKVATR 3421
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE----------------YLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3422 LHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADL---ENEKARLKKEAEELQNKSKEMADAQQkkiehektVLQQ 3498
Cdd:pfam13868 172 EAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLyqeEQERKERQKEREEAEKKARQRQELQQ--------AREE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3499 TFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKAlkdEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEM 3578
Cdd:pfam13868 244 QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE---EAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
|
330 340
....*....|....*....|...
gi 1988774674 3579 QELERQRleQERILAEENQKLRE 3601
Cdd:pfam13868 321 REEEAER--RERIEEERQKKLKE 341
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2008-2582 |
5.85e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2008 LRIEDCE--AGTVARIRKPV--EKEPLKEYIQKTTEQKKVQGELdglKKDLDKVSVKTQEVlaspqpSASAPVLRSELDl 2083
Cdd:PRK03918 155 LGLDDYEnaYKNLGEVIKEIkrRIERLEKFIKRTENIEELIKEK---EKELEEVLREINEI------SSELPELREELE- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2084 tvqkmdhahMLSSVYLEKLKTVEMVirntqgaEGVLKQYEDCLREVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSL 2163
Cdd:PRK03918 225 ---------KLEKEVKELEELKEEI-------EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2164 EEELKKASAVS---DKMVRVHSERDVELDHFRQQLSSLQDRWKavftqidlrqrELEQLGRQLGYYRESYDWLIRWIADA 2240
Cdd:PRK03918 289 KEKAEEYIKLSefyEEYLDELREIEKRLSRLEEEINGIEERIK-----------ELEEKEERLEELKKKLKELEKRLEEL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2241 KQRQEKIQavpitDSKTLKEQLAQEKKLLEEIEqnKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKKT--K 2318
Cdd:PRK03918 358 EERHELYE-----EAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2319 LDSASDNII--------QEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEER-----KKMAEMQAELdk 2385
Cdd:PRK03918 431 LKKAKGKCPvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklKELAEQLKEL-- 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2386 QKQLAEAHAKAIAKAEKEAQELK-----LKMQEEVSKREIAAVDA-EKQKTNIQLELQELKN-LSE--QQIKDKSQQVDE 2456
Cdd:PRK03918 509 EEKLKKYNLEELEKKAEEYEKLKeklikLKGEIKSLKKELEKLEElKKKLAELEKKLDELEEeLAEllKELEELGFESVE 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2457 ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEetQKKRQAEEELKRKSE 2536
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE--LEKKYSEEEYEELRE 666
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1988774674 2537 AEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHE 2582
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2327-2783 |
7.88e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.13 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2327 IQEYVTLRTRYSELMTLTSQYIKF----ITDTQRRLDDEEKAAEKLKAEERKKMA-------EMQAELDKQK-------- 2387
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYVAAdymrHANERRVHLEEALELRRELYTSRRQLAaeqyrlvEMARELAELNeaesdleq 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2388 ------------QLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAvdaekqktNIQLELQELKNLSEQQIKD-KSQQV 2454
Cdd:PRK04863 329 dyqaasdhlnlvQTALRQQEKIERYQADLEELEERLEEQNEVVEEAD--------EQQEENEARAEAAEEEVDElKSQLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2455 D--EALhsrtkIEEEIRLIRIQlettekQKYTAESELKQLRDRAA-EAEKlrklAQDEAEKLRKQVSEETQKKRQAEEEL 2531
Cdd:PRK04863 401 DyqQAL-----DVQQTRAIQYQ------QAVQALERAKQLCGLPDlTADN----AEDWLEEFQAKEQEATEELLSLEQKL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2532 krkSEAEkEAAKQKQKALEDLEKL--RMQAEEAERQVKQAEIEKEKQikvAHEAAQKSAaaeLQSKHmsfaektSKLEES 2609
Cdd:PRK04863 466 ---SVAQ-AAHSQFEQAYQLVRKIagEVSRSEAWDVARELLRRLREQ---RHLAEQLQQ---LRMRL-------SELEQR 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2610 LKQehgavlqlQQEAERLKKQQEDAENSREEAEKELekwrqkanEALRLRLQAEDEAHKktlaqeeaekqkeeaerEAKK 2689
Cdd:PRK04863 529 LRQ--------QQRAERLLAEFCKRLGKNLDDEDEL--------EQLQEELEARLESLS-----------------ESVS 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2690 RAKAEESALKQKemaEEELERQRKIAESTAQQKLTAEQELIRLR----ADFDNAEQQRSLLEDELYRLKnevaAAQQQRK 2765
Cdd:PRK04863 576 EARERRMALRQQ---LEQLQARIQRLAARAPAWLAAQDALARLReqsgEEFEDSQDVTEYMQQLLERER----ELTVERD 648
|
490
....*....|....*...
gi 1988774674 2766 QLEDELAKVRSEMDILIQ 2783
Cdd:PRK04863 649 ELAARKQALDEEIERLSQ 666
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2136-2631 |
7.91e-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: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2136 VKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVrvhSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRE 2215
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL---TEARTERDQFSQESGNLDDQLQKLLADLHKREKE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2216 --LEQLGRQLGYYRE-----SYDWLIRWIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKA 2288
Cdd:pfam15921 393 lsLEKEQNKRLWDRDtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLES 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2289 YIDTIKDYELQLVAYKAQVEP---LVSPLKKT--KLDSASDNIIQEYVTLRTRYsELMTLTSQYIKFITDTQRRLDDEEK 2363
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLESserTVSDLTASlqEKERAIEATNAEITKLRSRV-DLKLQELQHLKNEGDHLRNVQTECE 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2364 AAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAI-------AKAEKEAQELKLKMQE---EVSKREIAAVDAEKQKTNIQ 2433
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAgamqvekAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARVSDLE 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2434 LELQELKNLSEQQ---IKDKSQQVDEALH----SRTKIE---EEIRLIRI-------QLETT----EKQKYTAESELKQL 2492
Cdd:pfam15921 632 LEKVKLVNAGSERlraVKDIKQERDQLLNevktSRNELNslsEDYEVLKRnfrnkseEMETTtnklKMQLKSAQSELEQT 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2493 RDRAAEAEKLRKLAQDEAEKLRKQVS------EETQKKRQAEEELKRKSEAEKEAAKQKQKALEdlEKLRMQAEEAERQV 2566
Cdd:pfam15921 712 RNTLKSMEGSDGHAMKVAMGMQKQITakrgqiDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS--QELSTVATEKNKMA 789
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2567 KQAEIEKEKQIKVAHEAAQKSAAaeLQSKHMSFAEKTSKLEeslKQEhgavlqlqQEAERLKKQQ 2631
Cdd:pfam15921 790 GELEVLRSQERRLKEKVANMEVA--LDKASLQFAECQDIIQ---RQE--------QESVRLKLQH 841
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2444-2643 |
8.61e-10 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 64.10 E-value: 8.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2444 EQQIKDKSQQVDEAlhsRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKlaqdeAEKLRKQVSEetqk 2523
Cdd:TIGR02794 49 AQQANRIQQQKKPA---AKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEE---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2524 KRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAElqskhmsfAEKT 2603
Cdd:TIGR02794 117 KQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAE--------AEAK 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1988774674 2604 SKLEESLKQEHGAVLQLQQEAERlKKQQEDAENSREEAEK 2643
Cdd:TIGR02794 189 AKAEEAKAKAEAAKAKAAAEAAA-KAEAEAAAAAAAEAER 227
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3448-3618 |
1.01e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3448 KEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEE 3527
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3528 EVKKAKALKdEQERQKQQMEQEKKTLQATMDAAL-SKQKEAEEEMLRKQKEMQELERQRLEQERILA---EENQKLREKL 3603
Cdd:COG4717 151 LEERLEELR-ELEEELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQRLAELEEELEeaqEELEELEEEL 229
|
170
....*....|....*
gi 1988774674 3604 QQLEDAQKDQHTRET 3618
Cdd:COG4717 230 EQLENELEAAALEER 244
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2120-2647 |
1.02e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 65.38 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2120 KQYEDCLREVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQ 2199
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2200 -------------DRWKAVFTQIDLRQRELEQLGRQLGYYRESYDWLIRWIAD--AKQRQEKIQAVPITD---SKTLKEQ 2261
Cdd:TIGR00618 380 hihtlqqqkttltQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQqeLQQRYAELCAAAITCtaqCEKLEKI 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2262 LAQE--KKLLEEIEQNKDKVDECQKYAKayIDTIKDYELQLVA-------------YKAQVEPLVSPLKKTKLDSASDNI 2326
Cdd:TIGR00618 460 HLQEsaQSLKEREQQLQTKEQIHLQETR--KKAVVLARLLELQeepcplcgscihpNPARQDIDNPGPLTRRMQRGEQTY 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2327 IQEYVTLRTRYSELMTLTSQyIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQE 2406
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2407 LKLKMQEEVSKREIAAVDAEKQKTNIQLEL---QELKNLSEQQIKDKSqqvdealhSRTKIEEEIRLIRIQLETTEkqky 2483
Cdd:TIGR00618 617 LLRKLQPEQDLQDVRLHLQQCSQELALKLTalhALQLTLTQERVREHA--------LSIRVLPKELLASRQLALQK---- 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2484 tAESELKQLRDRAAEAEKLRKLAQDEAEKLrKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAE 2563
Cdd:TIGR00618 685 -MQSEKEQLTYWKEMLAQCQTLLRELETHI-EEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2564 RQVKQAEI-------EKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAEN 2636
Cdd:TIGR00618 763 HFNNNEEVtaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSA 842
|
570
....*....|.
gi 1988774674 2637 SREEAEKELEK 2647
Cdd:TIGR00618 843 TLGEITHQLLK 853
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2803-3613 |
1.05e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2803 LEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEaaRQRAEAERILKEKLAAIsEATRLKTEAEIALKEK---EAENER 2879
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREY-EGYELLKEKEALERQKeaiERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2880 LRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLE 2959
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2960 LELNKLKniaDETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRkaalEELERLRKKAEEARKQK 3039
Cdd:TIGR02169 329 AEIDKLL---AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR----DELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3040 DEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEyekakklakeaeaakekaereaalLRQQAEEA 3119
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE------------------------IKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3120 ERQKTAAEEEAANQAKAQEDAERLRKEaefeaakraqaeaaaLMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLK 3199
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKE---------------LSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3200 LDETDKQKSVLDEELQ---------RLKDEV--DDAVKQRGQveEELFKVKVQMEELLKLkNKIEEENQRLIKKDKDSTQ 3268
Cdd:TIGR02169 523 VHGTVAQLGSVGERYAtaievaagnRLNNVVveDDAVAKEAI--ELLKRRKAGRATFLPL-NKMRDERRDLSILSEDGVI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3269 KLLAEEAENMRKLAEDAA-----RLSVEAQEAA-------RLRQIAEDDLNQQRALAEKMLKEKmQAIQEASRLKAEAEM 3336
Cdd:TIGR02169 600 GFAVDLVEFDPKYEPAFKyvfgdTLVVEDIEAArrlmgkyRMVTLEGELFEKSGAMTGGSRAPR-GGILFSRSEPAELQR 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3337 LQKQKdlaqEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLrlqvsqlseaqaraeeeakkfKKQAD 3416
Cdd:TIGR02169 679 LRERL----EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL---------------------EQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3417 KVATRLheteiatQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQnksKEMADAQQKKIEHEKTVL 3496
Cdd:TIGR02169 734 KLKERL-------EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEIQAELSKL 803
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3497 qqtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVkkAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQK 3576
Cdd:TIGR02169 804 ------EEEVSRIEARLREIEQKLNRLTLEKEY--LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
810 820 830
....*....|....*....|....*....|....*..
gi 1988774674 3577 EMQELERQRLEqeriLAEENQKLREKLQQLEDAQKDQ 3613
Cdd:TIGR02169 876 ALRDLESRLGD----LKKERDELEAQLRELERKIEEL 908
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2422-2617 |
1.20e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.06 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2422 AVDAEKQKTNIQL----ELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRiqlettEKQKYTAESELKQLRDRAA 2497
Cdd:PRK09510 74 AKRAEEQRKKKEQqqaeELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAA------LKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2498 EAEKLRKLAQDEAeklrKQVSEETQKKRQAEEELKRKSEAEKEA-AKQKQKALEDLEKlrmqAEEAERQVKQAEIEKEKQ 2576
Cdd:PRK09510 148 KAEAEAKRAAAAA----KKAAAEAKKKAEAEAAKKAAAEAKKKAeAEAAAKAAAEAKK----KAEAEAKKKAAAEAKKKA 219
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1988774674 2577 IKVAHEAAQKsAAAELQSKHMSFAEKTSKLEESLKQEHGAV 2617
Cdd:PRK09510 220 AAEAKAAAAK-AAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3177-3396 |
1.26e-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: 64.01 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3177 KLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELfkvKVQMEELLKLKNKIEEEN 3256
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3257 QRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAAR----LRQIAEDDLNQQRALAEKmLKEKMQAIQEASRLKA 3332
Cdd:COG4942 97 AEL-EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRrlqyLKYLAPARREQAEELRAD-LAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 3333 EAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQ 3396
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2522-2728 |
1.27e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.06 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2522 QKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEE---AERQVKQAE----IEKEKQiKVAHEAAQKSAAAelqs 2594
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKErlaAQEQKKQAEeaakQAALKQ-KQAEEAAAKAAAA---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2595 khmsfaektSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTlaqe 2674
Cdd:PRK09510 145 ---------AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKA---- 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 2675 eaekqkeeaEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQE 2728
Cdd:PRK09510 212 ---------AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
3113-3393 |
1.92e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 64.37 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3113 RQQAEEAERQKTAAEEEAANQAKaqEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKL----AEQTLKQKFQ 3188
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKA--REVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELerirQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3189 VEQELTKVKL-KLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRlikkdkdST 3267
Cdd:pfam17380 365 IRQEEIAMEIsRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR-------EV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3268 QKLLAEEAENMRKLAEDAARlsvEAQEAARLRQIAEDdlNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQ-KQKDLAQE 3346
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQE---RQQQVERLRQQEEE--RKRKKLELEKEKRDRKRAEEQRRKILEKELEErKQAMIEEE 512
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1988774674 3347 QAQKLLEDKQLMQQRLEEETEEYHKSlEVERKRQLEImaeAERLRLQ 3393
Cdd:pfam17380 513 RKRKLLEKEMEERQKAIYEEERRREA-EEERRKQQEM---EERRRIQ 555
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2444-2646 |
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 1988774674 2444 EQQIKDKSQQVDEALHSRTKIEEEIRLIriqlettEKQKYTAESELKQlrdrAAEAEKLRKLAQDEAEKLRKQVSEETQK 2523
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQL-------EKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2524 KrqAEEELKRKSEAEKEAAKQKQKaLEDLEKLRMQAEEAerqvkQAEIEKEKQIKVAHEAAQKsAAAELQSKHMSFAEKT 2603
Cdd:PRK09510 148 K--AEAEAKRAAAAAKKAAAEAKK-KAEAEAAKKAAAEA-----KKKAEAEAAAKAAAEAKKK-AEAEAKKKAAAEAKKK 218
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1988774674 2604 SKLEESLKQEHGAVlQLQQEAERLKKQQEDAENSREEAEKELE 2646
Cdd:PRK09510 219 AAAEAKAAAAKAAA-EAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
1059-1155 |
2.07e-09 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 58.35 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1059 KKTFTKWVN---------KHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDFL 1124
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1988774674 1125 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1155
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2757-3083 |
2.24e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 64.37 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2757 VAAAQQQRKQLEDELAKVRSEmdiliqlktkaEKETMSNTEKSKQLLEAEAAKMKDLAEEAS----RLRAISEEAKHQRQ 2832
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQE-----------KEEKAREVERRRKLEEAEKARQAEMDRQAAiyaeQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2833 IAEEEAARqraEAERILKEKLAAisEATRLKtEAEIALKEKEAENERLRRQAEdEAYQRKALEDQASQHKQEIEEKIVQL 2912
Cdd:pfam17380 353 IRQEERKR---ELERIRQEEIAM--EISRMR-ELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2913 KKSSEAEMERQkaivddtlkQRRVVEEEIRilklnfekassgkldlELELNKLKNIADETQQSKIRAEEEAEKLRKLALE 2992
Cdd:pfam17380 426 RAEQEEARQRE---------VRRLEEERAR----------------EMERVRLEEQERQQQVERLRQQEEERKRKKLELE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2993 EEKRRREAEEKV-KKIAAAEEEAARQ------------------RKAALEELERLRKKAEEARKQKD-EADKEAEKQIVV 3052
Cdd:pfam17380 481 KEKRDRKRAEEQrRKILEKELEERKQamieeerkrkllekemeeRQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRK 560
|
330 340 350
....*....|....*....|....*....|.
gi 1988774674 3053 AQQAAQKCSAAEQQVQsvLAQQIEDSITQKK 3083
Cdd:pfam17380 561 ATEERSRLEAMERERE--MMRQIVESEKARA 589
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3114-3570 |
2.45e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3114 QQAEEAERQKTAAEEEAANQAKAQEDAERLRKE-AEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQE 3192
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEElEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3193 LTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRG-QVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLl 3271
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3272 aEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQ--EQAQ 3349
Cdd:COG4717 230 -EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKeaEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3350 KLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSeaqaraeeeakKFKKQADKVATRLHETEIAT 3429
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE-----------ELEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3430 QEKMTVVERLEfERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEmaDAQQKKIEHEKTVLQQTfMTEKEMLLK 3509
Cdd:COG4717 378 EAGVEDEEELR-AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEEL-EEELEELRE 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 3510 KEKLIEDEKKRLESqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEE 3570
Cdd:COG4717 454 ELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2434-2835 |
2.64e-09 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 63.82 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2434 LELQELKNLSEQQIKDKSQQVDealhSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAqDEAEKL 2513
Cdd:COG5185 184 LTLGLLKGISELKKAEPSGTVN----SIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTS-DKLEKL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2514 RKQVSE-ETQKKRQAEEELKRKSEAEKEAAKQ----KQKALEDLEKLRMQA--EEAERQVKQAEIEKEKQIKVAH-EAAQ 2585
Cdd:COG5185 259 VEQNTDlRLEKLGENAESSKRLNENANNLIKQfentKEKIAEYTKSIDIKKatESLEEQLAAAEAEQELEESKREtETGI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2586 KSAAAELQSKHMSFAEKTSKLEESLKQEHGAVL--QLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAE 2663
Cdd:COG5185 339 QNLTAEIEQGQESLTENLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2664 DEAHKKtlaqeeaekqkeeAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELI--RLRADFDNAEQ 2741
Cdd:COG5185 419 DRQIEE-------------LQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEInrSVRSKKEDLNE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2742 QRSLLEDELYRLKNEVaaaQQQRKQLEDELAKVRSEMDILIQLKTKAEKETmsNTEKSKQLLEAEAAKMKDLAEEASRLR 2821
Cdd:COG5185 486 ELTQIESRVSTLKATL---EKLRAKLERQLEGVRSKLDQVAESLKDFMRAR--GYAHILALENLIPASELIQASNAKTDG 560
|
410
....*....|....
gi 1988774674 2822 AISEEAKHQRQIAE 2835
Cdd:COG5185 561 QAANLRTAVIDELT 574
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2619-3073 |
3.30e-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: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2619 QLQQEAERLKKQQEDAENSREEAEKElekwRQKAnEALRlRLQAEDEAHKKTlaqeeaeKQKEEAEREAKKRAKAEESAL 2698
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDA----REQI-ELLE-PIRELAERYAAA-------RERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2699 KQkEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLE-DELYRLKNEVAAAQQQRKQLEDELAKVRSE 2777
Cdd:COG4913 289 RL-ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2778 MDILiQLKTKAEKETMSNT-EKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERI---LKEKL 2853
Cdd:COG4913 368 LAAL-GLPLPASAEEFAALrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2854 AAISEATRLKTEA--------EIALKEKEAEN--ER-LRRQA-----EDEAYQR-----------------KALEDQASQ 2900
Cdd:COG4913 447 DALAEALGLDEAElpfvgeliEVRPEEERWRGaiERvLGGFAltllvPPEHYAAalrwvnrlhlrgrlvyeRVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2901 HKQEIEEK----IVQLKKSS-----EAEMERQKAIV----DDTLKQ--RRVVEEeiRILKLN---FEKASSGKL------ 2956
Cdd:COG4913 527 ERPRLDPDslagKLDFKPHPfrawlEAELGRRFDYVcvdsPEELRRhpRAITRA--GQVKGNgtrHEKDDRRRIrsryvl 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2957 ---------DLELELNKLKNIADETQQSKIRAEEEAEKL--RKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALE-- 3023
Cdd:COG4913 605 gfdnraklaALEAELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDAss 684
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 3024 -ELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQ 3073
Cdd:COG4913 685 dDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3385-3598 |
3.83e-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: 62.47 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3385 AEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIAtqekmtvVERLEFERLNTSKEADDLRKAIADLENEK 3464
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR-------IAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3465 ARLKKEAEELQNKSKEMADAQQKKIEHEKTVL----------------QQTFMTEKEMLLKKEKLIEDEKKRLESQFEEE 3528
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3529 VKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQK 3598
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2356-2723 |
4.23e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2356 RRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQ---------ELKLKMQEEVSK-REIAAVDA 2425
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaelperleELEERLEELRELeEELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2426 EKQKTNIQLE--LQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQ--KYTAESELKQLRDRAAEAE- 2500
Cdd:COG4717 171 ELAELQEELEelLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLKEARl 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2501 --------------------------------------------KLRKLAQDEAEKLRKQVSEETQKKRQAEEELKR--- 2533
Cdd:COG4717 251 llliaaallallglggsllsliltiagvlflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELLAAlgl 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2534 KSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQK----SAAAELQSKHMSFAEKTSKLEES 2609
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDeeelRAALEQAEEYQELKEELEELEEQ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2610 LKQEHGAVLQL--QQEAERLKKQQEDAENSREEAEKELEKWRQKanealrlrlQAEDEAHKKTLAQEEAEKQKEEAEREA 2687
Cdd:COG4717 411 LEELLGELEELleALDEEELEEELEELEEELEELEEELEELREE---------LAELEAELEQLEEDGELAELLQELEEL 481
|
410 420 430
....*....|....*....|....*....|....*.
gi 1988774674 2688 KKRAKAEESALKQKEMAEEELERQRKIAESTAQQKL 2723
Cdd:COG4717 482 KAELRELAEEWAALKLALELLEEAREEYREERLPPV 517
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2526-2783 |
4.29e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 62.17 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2526 QAEEELKRKSEAEKEAAKQKQKALEDLEKlrmQAEEAERQvKQAEIEKEKQIKVAHEAAQKSAAAELQSKHmsfAEKTSK 2605
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQ---QAEEAEKQ-RAAEQARQKELEQRAAAEKAAKQAEQAAKQ---AEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2606 LEESLKQEHGAVLQLQQEAERLKKQQEDAENsreeaekelekwrqkanealrlrlQAEDEAHKKTLAQEEAEKQKEEAER 2685
Cdd:TIGR02794 120 QAEEAKAKQAAEAKAKAEAEAERKAKEEAAK------------------------QAEEEAKAKAAAEAKKKAEEAKKKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2686 EAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRK 2765
Cdd:TIGR02794 176 EAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGA 255
|
250
....*....|....*...
gi 1988774674 2766 QLEDELAKVRSEMDILIQ 2783
Cdd:TIGR02794 256 AAGSEVDKYAAIIQQAIQ 273
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3258-3624 |
4.34e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3258 RLIKKDKDSTQKLLAEEAENMRKLAEDAARLsveaqeAARLRQIAE--DDLNQQRALAEKMLKEKmqaiQEASRLKAEAE 3335
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKEL------EEVLREINEisSELPELREELEKLEKEV----KELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3336 MLQKQKDLAQEQAQKLLEDKQLMQQRLEEeTEEYHKSLEVERKRQLEIMAEAERLRlqvsqlseaqaraeeEAKKFKKQA 3415
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEE-LKKEIEELEEKVKELKELKEKAEEYI---------------KLSEFYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3416 DKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAE----------ELQNKSKEMADAQ 3485
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyeeakakkeELERLKKRLTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3486 QKKIEHEKTVLQqtfmTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQER----QKQQMEQEKKTLQATMDAAL 3561
Cdd:PRK03918 386 PEKLEKELEELE----KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEYTAEL 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 3562 SK----QKEAEEEMLRKQKEMQELERQRLEQERI-----LAEENQKLREKLQQLEDAQKDQHTRETDKVLHK 3624
Cdd:PRK03918 462 KRiekeLKEIEEKERKLRKELRELEKVLKKESELiklkeLAEQLKELEEKLKKYNLEELEKKAEEYEKLKEK 533
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3352-3613 |
4.54e-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: 61.86 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3352 LEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLheteiatqe 3431
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ--------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3432 kmtvvERLEFERLNTSKEADDLRKAIADLENEKARLK--KEAEELQNKSKEMaDAQQKKIEHEKTVLQQTFMTEKEMLLK 3509
Cdd:pfam13868 99 -----EREQMDEIVERIQEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKEL-EKEEEREEDERILEYLKEKAEREEERE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3510 KEKL-IEDEKKRLESQFEEEVKKAKALKDEQE---------------RQKQQMEQEKK-TLQATMDAALSKQKEAEEEML 3572
Cdd:pfam13868 173 AEREeIEEEKEREIARLRAQQEKAQDEKAERDelraklyqeeqerkeRQKEREEAEKKaRQRQELQQAREEQIELKERRL 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1988774674 3573 RKQKEMQELERQRL-----EQERILAEENQKLREKLQQLEDAQKDQ 3613
Cdd:pfam13868 253 AEEAEREEEEFERMlrkqaEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2465-2934 |
4.81e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 63.43 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2465 EEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAeklrKLAQDEAEKLRKQVS---EET--QKKRQAEEELKRKSEAEK 2539
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQL----KEQLQLLNKLLPQANllaDETlaDRLEELREELDAAQEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2540 EAAkQKQKALEDLEK----LR---MQAEEAERQVKQAEiEKEKQIKvaheaAQKSAAAEL--QSKHMSFAEKTSKLEESl 2610
Cdd:COG3096 911 FIQ-QHGKALAQLEPlvavLQsdpEQFEQLQADYLQAK-EQQRRLK-----QQIFALSEVvqRRPHFSYEDAVGLLGEN- 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2611 kqehgavlqlQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRlRLQAEDEAHkktlaqeeaekqkeeaereakkR 2690
Cdd:COG3096 983 ----------SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ-VLASLKSSR----------------------D 1029
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2691 AKAEESALKQKEMAEeelerqrkiaestaqqkltaeqelIRLRADfDNAEQQRSLLEDELYrlkNEVAAAQQQRKQLEDE 2770
Cdd:COG3096 1030 AKQQTLQELEQELEE------------------------LGVQAD-AEAEERARIRRDELH---EELSQNRSRRSQLEKQ 1081
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2771 LAKVRSEMDILIQLKTKAEKETMSNTEkskqllEAEAAKmkdlaEEASRLRAISEEAKHQRQIAEEEAARQRAeaerilk 2850
Cdd:COG3096 1082 LTRCEAEMDSLQKRLRKAERDYKQERE------QVVQAK-----AGWCAVLRLARDNDVERRLHRRELAYLSA------- 1143
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2851 EKLAAISEatrlktEAEIALKEKEAENERLR---RQAEDEAY-QRK-ALEDQASQHKQE-IEEKIVQLKKSSEA--EMER 2922
Cdd:COG3096 1144 DELRSMSD------KALGALRLAVADNEHLRdalRLSEDPRRpERKvQFYIAVYQHLRErIRQDIIRTDDPVEAieQMEI 1217
|
490
....*....|..
gi 1988774674 2923 QKAIVDDTLKQR 2934
Cdd:COG3096 1218 ELARLTEELTSR 1229
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5397-5435 |
4.89e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 54.64 E-value: 4.89e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1988774674 5397 FLEVQYLTGGLIEPDVEGRVSIDESIRKGTIDARTAQKL 5435
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2022-2924 |
5.94e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 63.14 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2022 RKPVEKEPLKEYIQKTTEQKKVQGELDGLKKDLDKVSVKTQEvlaspqpsasapvLRSELDLTVQKMDHAHMlssvylEK 2101
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEK-------------DNSELELKMEKVFQGTD------EQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2102 LKTVEmvirNTQGAEGVLKQYE--DCLREVHTVPSDVKEvetyrakLKKMRTEAEDEQPVFdSLEEELKKASAVSDKMVR 2179
Cdd:TIGR00606 303 LNDLY----HNHQRTVREKERElvDCQRELEKLNKERRL-------LNQEKTELLVEQGRL-QLQADRHQEHIRARDSLI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2180 VHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLGYYREsydwlirwiadaKQRQEKIQAVPITDSKTLK 2259
Cdd:TIGR00606 371 QSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS------------KERLKQEQADEIRDEKKGL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2260 EQLAQEKK--LLEEIEQNKDKVDECQKYAKAYIDTIK--------DYELQLVAYKAQVEPLVSPLKKTKLDSAsdNIIQE 2329
Cdd:TIGR00606 439 GRTIELKKeiLEKKQEELKFVIKELQQLEGSSDRILEldqelrkaERELSKAEKNSLTETLKKEVKSLQNEKA--DLDRK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2330 YVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKaAEKLKAEERKKMAEMQAELDKQKQLAEAHAKaIAKAEKEAQELKL 2409
Cdd:TIGR00606 517 LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQ-IRKIKSRHSDELTSLLGYFPNKKQLEDWLHS-KSKEINQTRDRLA 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2410 KMQEEVSKREIAAVDAEKQKTniQLELQELKnLSEQQIKDKSQQVDEALHSRTKieEEIRLIRIQLETTEKQKYTAESEL 2489
Cdd:TIGR00606 595 KLNKELASLEQNKNHINNELE--SKEEQLSS-YEDKLFDVCGSQDEESDLERLK--EEIEKSSKQRAMLAGATAVYSQFI 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2490 KQLRDRAAEAEKL-RKLAQDEAEkLRKQVSEETQKKRQAEEELKrksEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQ 2568
Cdd:TIGR00606 670 TQLTDENQSCCPVcQRVFQTEAE-LQEFISDLQSKLRLAPDKLK---STESELKKKEKRRDEMLGLAPGRQSIIDLKEKE 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2569 AEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQ--QEDAENSREEAEKELE 2646
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKiaQQAAKLQGSDLDRTVQ 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2647 KWRQKANEalrlrlqaEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAE 2726
Cdd:TIGR00606 826 QVNQEKQE--------KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV 897
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2727 QELIRLRADFDNAEQ-QRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEA 2805
Cdd:TIGR00606 898 QSLIREIKDAKEQDSpLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKET 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2806 EAAKMK-DLAEEASRLRAISEEAKHQRQIAEEEAARqraeaERILKEKLaaiseaTRLKTEAEIalkekeAENERLRRQA 2884
Cdd:TIGR00606 978 ELNTVNaQLEECEKHQEKINEDMRLMRQDIDTQKIQ-----ERWLQDNL------TLRKRENEL------KEVEEELKQH 1040
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 1988774674 2885 EDEAYQRKALedQASQHKQEIEEKIVQLKKSSEAEMERQK 2924
Cdd:TIGR00606 1041 LKEMGQMQVL--QMKQEHQKLEENIDLIKRNHVLALGRQK 1078
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2522-2791 |
6.50e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.05 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2522 QKKRQAEEELKRKSEAE---KEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEK-EKQIKVAHEAAQKSAaaelqsKHM 2597
Cdd:PRK04863 844 RRRVELERALADHESQEqqqRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEiREQLDEAEEAKRFVQ------QHG 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2598 SFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAEN---------------SREEAEKELEKwRQKANEALRLRL-Q 2661
Cdd:PRK04863 918 NALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafaltevvqrrahfSYEDAAEMLAK-NSDLNEKLRQRLeQ 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2662 AEDEAhkktlaqeeaekqkeeaeREAKKRAKAEESALKQKEMAEEELerqrKIAESTAQQKLT-AEQEL--IRLRADFdN 2738
Cdd:PRK04863 997 AEQER------------------TRAREQLRQAQAQLAQYNQVLASL----KSSYDAKRQMLQeLKQELqdLGVPADS-G 1053
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 2739 AEQQRSLLEDELYrlkNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKE 2791
Cdd:PRK04863 1054 AEERARARRDELH---ARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2606-2929 |
6.57e-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: 62.01 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2606 LEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEahKKTLAQEEAEKQKEEAER 2685
Cdd:pfam19220 25 LKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGE--LEELVARLAKLEAALREA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2686 EAKKRAKAeeSALKQKEMAEEELERQRKIAestAQQKLTAEQELIRLRADFDNAEQQRSLLEDELyrlknevAAAQQQRK 2765
Cdd:pfam19220 103 EAAKEELR--IELRDKTAQAEALERQLAAE---TEQNRALEEENKALREEAQAAEKALQRAEGEL-------ATARERLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2766 QLEDELAKVRSEMDiliqlktKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLraISEEAKHQRQIAEEEAARQRAEA 2845
Cdd:pfam19220 171 LLEQENRRLQALSE-------EQAAELAELTRRLAELETQLDATRARLRALEGQL--AAEQAERERAEAQLEEAVEAHRA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2846 ERI-LKEKLAAIS---EAT-RLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKksseaEM 2920
Cdd:pfam19220 242 ERAsLRMKLEALTaraAATeQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQ-----EM 316
|
....*....
gi 1988774674 2921 ERQKAIVDD 2929
Cdd:pfam19220 317 QRARAELEE 325
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2432-2792 |
7.21e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 62.22 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2432 IQLELQElknlSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETT----EKQKYTAESELKQLRDRAAEAEKLRKLAQ 2507
Cdd:pfam07888 32 LQNRLEE----CLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2508 DEAEKLRKqvsEETQKKRQAEEELKRKSEAEKEAAKQKQKALE---DLEKLRMQAEEAERQVKQAEIEKEK-QIKV-AHE 2582
Cdd:pfam07888 108 ASSEELSE---EKDALLAQRAAHEARIRELEEDIKTLTQRVLEretELERMKERAKKAGAQRKEEEAERKQlQAKLqQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2583 AAQKSAAAELQSKHMSFAEKTSKLEE------SLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAL 2656
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQlqdtitTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2657 RLRLQAEDEAHKKTLAQEEAEKQKEEAE---REAKKRAKAEESALKQKEMAE--------EELERQRKIAESTAQQKLTA 2725
Cdd:pfam07888 265 AQRDRTQAELHQARLQAAQLTLQLADASlalREGRARWAQERETLQQSAEADkdrieklsAELQRLEERLQEERMEREKL 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774674 2726 EQELIRLRadfDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVrseMDILIQLKTKAEKET 2792
Cdd:pfam07888 345 EVELGREK---DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL---LEYIRQLEQRLETVA 405
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2768-3391 |
7.38e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2768 EDELAKVRSEmdilIQLKTKAEKETMSNTEKSKQLLEAeaaKMKDLAEEASRLRAISEEakhqrqiaEEEAARQRAEAER 2847
Cdd:PRK03918 164 YKNLGEVIKE----IKRRIERLEKFIKRTENIEELIKE---KEKELEEVLREINEISSE--------LPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2848 ILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEdqasqhkqEIEEKIVQLK--KSSEAEMERQKA 2925
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE--------ELEEKVKELKelKEKAEEYIKLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2926 IVDDTLKQRRVVE-------EEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRR 2998
Cdd:PRK03918 301 FYEEYLDELREIEkrlsrleEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2999 EAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKdeadKEAEKQIVVAQQAAQKCsaaeqqvqSVLAQQIEDS 3078
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI----KELKKAIEELKKAKGKC--------PVCGRELTEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3079 iTQKKLKEEYEKAKKLAKEAEaakekaereaallrQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAE 3158
Cdd:PRK03918 449 -HRKELLEEYTAELKRIEKEL--------------KEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3159 AAALMQKQQADTEMAKHKKLA----------EQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQR 3228
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLiklkgeikslKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3229 GQVEEELFKvkvqmeELLKLKNkieeenqrlIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQ 3308
Cdd:PRK03918 594 LKELEPFYN------EYLELKD---------AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3309 QRalAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKqlmqqrleEETEEYHKSLEVERKrqleIMAEAE 3388
Cdd:PRK03918 659 EE--YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL--------EEREKAKKELEKLEK----ALERVE 724
|
...
gi 1988774674 3389 RLR 3391
Cdd:PRK03918 725 ELR 727
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2638-3397 |
7.57e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.83 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2638 REEAEKELEKWRQKANEaLRLRLQAEDEAHKK-------TLAQEEAEKQKEEAEREA-----KKRAKAEESALKQKEMAE 2705
Cdd:pfam15921 73 KEHIERVLEEYSHQVKD-LQRRLNESNELHEKqkfylrqSVIDLQTKLQEMQMERDAmadirRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2706 EELERQRKIAESTAQQKLT--------------AEQELIRLRADFDNAEQQRSLLEDELYRL--KNEVAAAQQQRKQLED 2769
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTqieqlrkmmlshegVLQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2770 ELAKVRSEM----DILIQLKTKAEKET----MSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQ 2841
Cdd:pfam15921 232 EISYLKGRIfpveDQLEALKSESQNKIelllQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2842 RAEAERILKEKLAAISEatrLKTEAEIALKEKEAENERLRRQ---AEDEAYQRKALEDQASQHKQEIEEKIvqlkkssea 2918
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQ---LRSELREAKRMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDDQL--------- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2919 emerQKAIVDdtLKQRrvvEEEirilklnfekassgkLDLELELNklKNIADETQQSKIRAEEEAEKLrklaleeekrrr 2998
Cdd:pfam15921 380 ----QKLLAD--LHKR---EKE---------------LSLEKEQN--KRLWDRDTGNSITIDHLRREL------------ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2999 eaeekvkkiaaaeeeaaRQRKAALEELERLRKkaeearKQKDEADKEAEKQIVVAQ---QAAQKCSAAEQQVQSV--LAQ 3073
Cdd:pfam15921 422 -----------------DDRNMEVQRLEALLK------AMKSECQGQMERQMAAIQgknESLEKVSSLTAQLESTkeMLR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3074 QIEDSITQKKLKEEyekakKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRK-EAEFEAA 3152
Cdd:pfam15921 479 KVVEELTAKKMTLE-----SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvQTECEAL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3153 KRAQAEAAALMQ--KQQADTEM---AKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDavkq 3227
Cdd:pfam15921 554 KLQMAEKDKVIEilRQQIENMTqlvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD---- 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3228 rgqVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKL--LAEEAENM-RKLAEDAARLSVEAQEAARLRQIAED 3304
Cdd:pfam15921 630 ---LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLkRNFRNKSEEMETTTNKLKMQLKSAQS 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3305 DLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE---DKQLMQQRLEEETEEYHKSLEVERKRQL 3381
Cdd:pfam15921 707 ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEamtNANKEKHFLKEEKNKLSQELSTVATEKN 786
|
810
....*....|....*.
gi 1988774674 3382 EIMAEAERLRLQVSQL 3397
Cdd:pfam15921 787 KMAGELEVLRSQERRL 802
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
1060-1154 |
8.05e-09 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 56.19 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1060 KTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMrfhkLQNVQIALDFLRHRQVKL 1131
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1988774674 1132 VNIRNDDIADGNPKLTLGLIWTI 1154
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2493-2718 |
8.44e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 61.81 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2493 RDRAAEAEKLRKLAQDEAEKLrKQVSEETQKKRQAEEELKRKSE------AEKEAAKQKQKALEDLEKLRMQAEeAERQV 2566
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERE-TEIAIAQANREAEEAELEQEREietariAEAEAELAKKKAEERREAETARAE-AEAAY 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2567 KQAEIEKEKQIKVAHEAAQKSAAAELQSKhmsfaektsKLEESLKQEHgAVLQLQQEAERLKKQQEdaensrEEAEKEle 2646
Cdd:COG2268 269 EIAEANAEREVQRQLEIAEREREIELQEK---------EAEREEAELE-ADVRKPAEAEKQAAEAE------AEAEAE-- 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 2647 kwrqkaneALRLRLQAEDEAHKKtlaqeeaekqKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAEST 2718
Cdd:COG2268 331 --------AIRAKGLAEAEGKRA----------LAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
1051-1157 |
8.78e-09 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 56.36 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1051 EDERDrvqKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKG-----RMRFHKLQNVQIALDFLR 1125
Cdd:cd21299 1 ETSRE---ERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGK 75
|
90 100 110
....*....|....*....|....*....|..
gi 1988774674 1126 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 1157
Cdd:cd21299 76 QLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2373-2543 |
9.43e-09 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 61.72 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2373 RKKMAEMQAELDKQKQLAEAHAKAIAK-----AEKEAQELKLKMQEEVSKREiaavdaekqktniqLELQELknlsEQQI 2447
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKealleAKEEIHKLRNEFEKELRERR--------------NELQKL----EKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2448 KDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRA-AEAEKLRKLAQDEA-EKLRKQVSEETQKKR 2525
Cdd:PRK12704 92 LQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQlQELERISGLTAEEAkEILLEKVEEEARHEA 171
|
170 180
....*....|....*....|.
gi 1988774674 2526 QA---EEELKRKSEAEKEAAK 2543
Cdd:PRK12704 172 AVlikEIEEEAKEEADKKAKE 192
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2840-3501 |
1.17e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2840 RQRAEAERILKEKLAAISEATRLKT--EAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQH---KQEIEEKIVQLKK 2914
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERlnGLESELAELDEEIERYEEQREQARETRDEADEVLEEHeerREELETLEAEIED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2915 SSE--AEMERQKAIVDDTLKQRRVVEEEIR------ILKLNFEKASSGKL-----DLELELNKLKNIADETQQSKIRAEE 2981
Cdd:PRK02224 263 LREtiAETEREREELAEEVRDLRERLEELEeerddlLAEAGLDDADAEAVearreELEDRDEELRDRLEECRVAAQAHNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2982 EAEKLRklaleeekrrreaeekvkkiaaaeeeaarqrkaalEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCS 3061
Cdd:PRK02224 343 EAESLR-----------------------------------EDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3062 AAEQQVQSvLAQQIEDSITQKKLKEEYekakklakeaeaakekaereAALLRQQAEEAERQKTAAEEEAANQAKAQEDAE 3141
Cdd:PRK02224 388 ELEEEIEE-LRERFGDAPVDLGNAEDF--------------------LEELREERDELREREAELEATLRTARERVEEAE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3142 RLRKEAEFEAAKRaqaeaaalmqkqqaDTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDEtdkqksvLDEELQRLKdev 3221
Cdd:PRK02224 447 ALLEAGKCPECGQ--------------PVEGSPHVETIEEDRERVEELEAELEDLEEEVEE-------VEERLERAE--- 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3222 dDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQklLAEEAENMRKLAEDAARLSVEAQEAArlrqi 3301
Cdd:PRK02224 503 -DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE--LEAEAEEKREAAAEAEEEAEEAREEV----- 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3302 aeDDLNQQRAlaekMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETeeyhkslevERKRQL 3381
Cdd:PRK02224 575 --AELNSKLA----ELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR---------ERKREL 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3382 EIMAEAERLrlqvsqlsEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERlEFERLntskeaDDLRKAIADLE 3461
Cdd:PRK02224 640 EAEFDEARI--------EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN-ELEEL------EELRERREALE 704
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1988774674 3462 NEKARLK---KEAEELQNKSKEM-ADAQQKKIEHEKTVLQQTFM 3501
Cdd:PRK02224 705 NRVEALEalyDEAEELESMYGDLrAELRQRNVETLERMLNETFD 748
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2375-2554 |
1.18e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 59.17 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2375 KMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELklkmQEEVSKREIAAVDAEKQKTNIQLELQELknlsEQQIKDKSQQV 2454
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAAL----EARLEAAKTELEDLEKEIKRLELEIEEV----EARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2455 DEALHSRtkieeEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRK 2534
Cdd:COG1579 83 GNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170 180
....*....|....*....|
gi 1988774674 2535 seaEKEAAKQKQKALEDLEK 2554
Cdd:COG1579 158 ---LEELEAEREELAAKIPP 174
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2519-2966 |
1.21e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 61.99 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2519 EETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEklrmqaeeaERQVKQAEIEKEKQI-----KVAHEAAQKSAAAELQ 2593
Cdd:PRK10929 24 DEKQITQELEQAKAAKTPAQAEIVEALQSALNWLE---------ERKGSLERAKQYQQVidnfpKLSAELRQQLNNERDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2594 SKHMSFAEKTSKLEESLKQEHGAVL----QLQQEAER----------LKKQQEDAENSREEAEKELE---KWRQKANEAL 2656
Cdd:PRK10929 95 PRSVPPNMSTDALEQEILQVSSQLLeksrQAQQEQDRareisdslsqLPQQQTEARRQLNEIERRLQtlgTPNTPLAQAQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2657 RLRLQAEDEAHKKTLaqeeaekqkeeaereakkrakaeesalkqkemaeEELErqrkiaesTAQQKLTAEQELIRLRAdf 2736
Cdd:PRK10929 175 LTALQAESAALKALV----------------------------------DELE--------LAQLSANNRQELARLRS-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2737 dnaeqqrslledELYrlknevaaaQQQRKQLEDELAKVRSemdiliQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEE 2816
Cdd:PRK10929 211 ------------ELA---------KKRSQQLDAYLQALRN------QLNSQRQREAERALESTELLAEQSGDLPKSIVAQ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2817 ASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAaiseatrLKTEAEIA--LKEKEAENERLRRQAEDEAYQRKAl 2894
Cdd:PRK10929 264 FKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQA-------LNTLREQSqwLGVSNALGEALRAQVARLPEMPKP- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2895 edqasqhkQEIEEKIVQLKKSS---EAEMERQ----KAIVDD----TLKQRRVVEEEIRILKLNFEKASSGKLDLELELN 2963
Cdd:PRK10929 336 --------QQLDTEMAQLRVQRlryEDLLNKQpqlrQIRQADgqplTAEQNRILDAQLRTQRELLNSLLSGGDTLILELT 407
|
...
gi 1988774674 2964 KLK 2966
Cdd:PRK10929 408 KLK 410
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2386-2593 |
1.22e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 60.63 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2386 QKQLAEAHAKAIAKAEKEAqelKLKMQEEVSKREIAAVDAEKQKtniQLELQELKNLSEQQIKDKSqqvdealhsrTKIE 2465
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPA---AKKEQERQKKLEQQAEEAEKQR---AAEQARQKELEQRAAAEKA----------AKQA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2466 EEIRLiriqlETTEKQKYTAESELKQLRDRAAEAEKLRKlaQDEAEKLRKQVSEETQKKRQAE-----EELKRKSEAEKE 2540
Cdd:TIGR02794 108 EQAAK-----QAEEKQKQAEEAKAKQAAEAKAKAEAEAE--RKAKEEAAKQAEEEAKAKAAAEakkkaEEAKKKAEAEAK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774674 2541 A---AKQKQKALEDLEKLRMQAEEAERQVKqAEIEKEKQIKVAHEAAQKSAAAELQ 2593
Cdd:TIGR02794 181 AkaeAEAKAKAEEAKAKAEAAKAKAAAEAA-AKAEAEAAAAAAAEAERKADEAELG 235
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
1168-1270 |
1.43e-08 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 55.94 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1168 QSEDMTAKEKLLLWSQ-RMTDgyqgIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLG 1245
Cdd:cd21315 11 DGKGPTPKQRLLGWIQsKVPD----LPITNFTNDWNDGKAIGALVDALAPGLCPDWEDWDPKDaVKNAKEAMDLAEDWLD 86
|
90 100
....*....|....*....|....*
gi 1988774674 1246 VTRLLDPEDVDVPHPDEKSIITYVS 1270
Cdd:cd21315 87 VPQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2394-2657 |
1.61e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2394 AKAIAKAEKEAQELKLKMQEevSKREIAAVDAEKQKTNIQLE-LQELKNLSEQQIKdksqqVDEALHSRTKIEEEIRLIR 2472
Cdd:COG4913 609 RAKLAALEAELAELEEELAE--AEERLEALEAELDALQERREaLQRLAEYSWDEID-----VASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2473 iqlettekqkyTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKAL-ED 2551
Cdd:COG4913 682 -----------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2552 LEKLRmQAEEAERQVKQAEIEKEKQIKVAhEAAQKSAAAELQSKHMSFAEK----TSKLEESLKQEHGAVLQLQQ-EAER 2626
Cdd:COG4913 751 LEERF-AAALGDAVERELRENLEERIDAL-RARLNRAEEELERAMRAFNREwpaeTADLDADLESLPEYLALLDRlEEDG 828
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1988774674 2627 LKKQQEDAENSREEAEKE--------LEKWRQKA-------NEALR 2657
Cdd:COG4913 829 LPEYEERFKELLNENSIEfvadllskLRRAIREIkeridplNDSLK 874
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3164-3538 |
1.61e-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: 61.57 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3164 QKQQADTEMAKHKKLAEQTLKQKF-----QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKV 3238
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQDWNKELkselkNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3239 KVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKlaedaarlsveaqeaarlrqiaedDLNQQRALAEKMLK 3318
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK------------------------DEQIKKLQQEKELL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3319 EKmqaiqEASRLKAEAEMLQKQ-KDLAQEQAQKLLEDKQLMQQR--LEEETEEYHKSLEVER------KRQLEI-MAEAE 3388
Cdd:TIGR04523 425 EK-----EIERLKETIIKNNSEiKDLTNQDSVKELIIKNLDNTResLETQLKVLSRSINKIKqnleqkQKELKSkEKELK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3389 RLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFE--RLNTSKEADDLRKAIADLENEKAR 3466
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKS 579
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 3467 LKKEAEELQNKSKEMADAQQ---KKIEhEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDE 3538
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKdliKEIE-EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
3211-3615 |
2.29e-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: 60.99 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3211 DEELQRLKDEVDDAVKqrgqveeELFKVKVQMEELlklKNKIEEENQRLIKKDkDSTQKLLAeeaenMRKLAEDAARLSV 3290
Cdd:pfam10174 115 EENFRRLQSEHERQAK-------ELFLLRKTLEEM---ELRIETQKQTLGARD-ESIKKLLE-----MLQSKGLPKKSGE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3291 EAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRlkaeaeMLQKQKDLAQEQA-QKLLEDKQLMQQRLEEETEEY 3369
Cdd:pfam10174 179 EDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHR------RNQLQPDPAKTKAlQTVIEMKDTKISSLERNIRDL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3370 HKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLH--ETEIATQEKMTVVERLEFERLNTS 3447
Cdd:pfam10174 253 EDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLalQTKLETLTNQNSDCKQHIEVLKES 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3448 KEADDLRKAIADLENEKARLKKEAEE--LQNKSKEMADAQQkkiehEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQF 3525
Cdd:pfam10174 333 LTAKEQRAAILQTEVDALRLRLEEKEsfLNKKTKQLQDLTE-----EKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3526 EEEVKKAKALKDEQERQK--QQMEQEKKTLQATMDAALSkQKEAEEEMLRKQKEmqELERQRLEQERILAEENQKLREKL 3603
Cdd:pfam10174 408 EQLRDKDKQLAGLKERVKslQTDSSNTDTALTTLEEALS-EKERIIERLKEQRE--REDRERLEELESLKKENKDLKEKV 484
|
410
....*....|..
gi 1988774674 3604 QQLEDAQKDQHT 3615
Cdd:pfam10174 485 SALQPELTEKES 496
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2433-2769 |
2.65e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.92 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2433 QLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKlrklaqdEAEK 2512
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE-------ELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2513 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAEL 2592
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2593 QSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLA 2672
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2673 QEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYR 2752
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330
....*....|....*..
gi 1988774674 2753 LKNEVAAAQQQRKQLED 2769
Cdd:COG4372 325 AKKLELALAILLAELAD 341
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3346-3619 |
3.10e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3346 EQAQKLLEDKQLMQQRLEEETEEYHKSLEVERK----RQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATR 3421
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEkreyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3422 LHETEIATQEKMTVVERL-EFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEKTVLQQTF 3500
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-LEAEIDKLLAEIEELEREI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3501 MTEKemlLKKEKLIE------DEKKRLESQFEEEVKKAKALKDEQERQKQQMEQ----------EKKTLQATMDAALSKQ 3564
Cdd:TIGR02169 346 EEER---KRRDKLTEeyaelkEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkreinelkrELDRLQEELQRLSEEL 422
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 3565 KEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETD 3619
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2434-2592 |
3.90e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 57.63 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2434 LELQEL---KNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQD-- 2508
Cdd:COG1579 10 LDLQELdseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2509 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKL--RMQAEEAERQVKQAEIEKE-KQIKVAHEAAQ 2585
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELeaELEEKKAELDEELAELEAElEELEAEREELA 169
|
....*..
gi 1988774674 2586 KSAAAEL 2592
Cdd:COG1579 170 AKIPPEL 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3250-3487 |
4.19e-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: 59.01 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3250 NKIEEENQRL--IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEA 3327
Cdd:COG4942 20 DAAAEAEAELeqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3328 SRLKAE-AEMLQKQKDLAQEQAQKLL---EDKQLMQQRLEeeteeYHKSLEVERKRQleimaeAERLRLQVSQLSEAQAR 3403
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLlspEDFLDAVRRLQ-----YLKYLAPARREQ------AEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3404 AEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMAD 3483
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....
gi 1988774674 3484 AQQK 3487
Cdd:COG4942 249 AALK 252
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2444-2758 |
4.38e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.15 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2444 EQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQK 2523
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2524 KRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKT 2603
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2604 SKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEA 2683
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2684 EREAKKRAKAEESALKQKEMAEEELERQRKIaesTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVA 2758
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALE---DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDV 355
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2486-2925 |
5.13e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 59.75 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2486 ESELKQLRDRAAEAEKLRKLAQDEAEK----LRKQVSEETQKKRQAEEELK--RKSEAEKEAAKQKQKaleDLEKLRMQA 2559
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKkasaLKRQLDRESDRNQELQKRIRllEKREAEAEEALREQA---ELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2560 EEAERQVKQaeiEKEKQIKVAHE--AAQKSAAAEL----QSKHMSFAEKTSKLEEsLKQEHGAVLQLQQEAERLKKQQED 2633
Cdd:pfam05557 85 LEALNKKLN---EKESQLADAREviSCLKNELSELrrqiQRAELELQSTNSELEE-LQERLDLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2634 AENSREEAE---KELEKWRQKAN-----------EALRL-RLQAEDEAHK------------KTLAQEEAEKQKEEAERE 2686
Cdd:pfam05557 161 QQSSLAEAEqriKELEFEIQSQEqdseivknsksELARIpELEKELERLRehnkhlnenienKLLLKEEVEDLKRKLERE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2687 AKKRAKAEESALKqKEMAEEELERQRKIAESTA-----------------QQKLTAEQELIRLRADFDNAEQQRSLLEDE 2749
Cdd:pfam05557 241 EKYREEAATLELE-KEKLEQELQSWVKLAQDTGlnlrspedlsrrieqlqQREIVLKEENSSLTSSARQLEKARRELEQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2750 LYRLKNEVAAAQQQRKQ-------LEDELAKVRSEMDILIQLKTKAEKEtMSNTEKSKQLLEaeaaKMKDLAEEASRLRA 2822
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRhkalvrrLQRRVLLLTKERDGYRAILESYDKE-LTMSNYSPQLLE----RIEEAEDMTQKMQA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2823 ISEEAKHQRQIAEEEAARQRAEA---ERILK-----EKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQrkaL 2894
Cdd:pfam05557 395 HNEEMEAQLSVAEEELGGYKQQAqtlERELQalrqqESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEME---L 471
|
490 500 510
....*....|....*....|....*....|..
gi 1988774674 2895 EDQASQHKQEIEE-KIVQLKKSSEAEMERQKA 2925
Cdd:pfam05557 472 ERRCLQGDYDPKKtKVLHLSMNPAAEAYQQRK 503
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2695-3327 |
5.46e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2695 ESALKQKEMAEEELERQRKIAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKV 2774
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARERL---AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2775 RSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEE-ASRLRAISEEAKHQRQIAEE---EAARQRAEAERILK 2850
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARlEALLAALGLPLPASAEEFAAlraEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2851 EKLAAISEATRLKTEAEIALKEKEAENERLRRQAE--DEAYQ--RKALEDQASQHKQEI----EEkiVQLKkssEAEMER 2922
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKSniPARLLalRDALAEALGLDEAELpfvgEL--IEVR---PEEERW 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2923 QKAI------------VDDTLKQ--RRVVEEEIRILKLNFEKASSGKLDLELE-------LNKLkniadETQQSKIRAEE 2981
Cdd:COG4913 477 RGAIervlggfaltllVPPEHYAaaLRWVNRLHLRGRLVYERVRTGLPDPERPrldpdslAGKL-----DFKPHPFRAWL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2982 EAEKLRKLALEeekrrreaeekvkkiaaaeeeaarqRKAALEELERLRK--------KAEEARKQKDEADKEAEKQiVVA 3053
Cdd:COG4913 552 EAELGRRFDYV-------------------------CVDSPEELRRHPRaitragqvKGNGTRHEKDDRRRIRSRY-VLG 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3054 QQAAQKCSAAEQQvqsvlAQQIEDSITQkklkeeyekakklakeaeaakekaereaalLRQQAEEAERQKtaaeeeaanq 3133
Cdd:COG4913 606 FDNRAKLAALEAE-----LAELEEELAE------------------------------AEERLEALEAEL---------- 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3134 AKAQEDAERLRKEAEFeaakraqaeaaalmQKQQADTEMAkHKKLAEqtlkqkfqVEQELTKvklkLDETDKQKSVLDEE 3213
Cdd:COG4913 641 DALQERREALQRLAEY--------------SWDEIDVASA-EREIAE--------LEAELER----LDASSDDLAALEEQ 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3214 LQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLknkIEEENQRLIKKDKDSTQKLLAEeaenmrkLAEDAARLSVEAQ 3293
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEE---LDELQDRLEAAEDLARLELRAL-------LEERFAAALGDAV 763
|
650 660 670
....*....|....*....|....*....|....*.
gi 1988774674 3294 EAARLRQIAE--DDLNQQRALAEKMLKEKMQAIQEA 3327
Cdd:COG4913 764 ERELRENLEEriDALRARLNRAEEELERAMRAFNRE 799
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
1173-1275 |
6.23e-08 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 54.31 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1173 TAKEKLLLWSQRMTdgyQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVAEKDLGVTRLLD 1251
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQpVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1988774674 1252 PEDVDVPHPDEKSIITYVSSLYDA 1275
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2464-2773 |
6.43e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.39 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2464 IEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDE-AEKLRKQVsEETQKKRQAEEELKRKseaEKEAA 2542
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyRQELEEQI-EEREQKRQEEYEEKLQ---EREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2543 KQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAV-LQLQ 2621
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIeEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2622 QEAERLKKQQEDAENSREE---------AEKELEKWRQKANEALRLRLQAEDEAhkktlaqeeaekqkeeaeREAKKRAK 2692
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAErdelraklyQEEQERKERQKEREEAEKKARQRQEL------------------QQAREEQI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2693 AEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELA 2772
Cdd:pfam13868 246 ELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEA 325
|
.
gi 1988774674 2773 K 2773
Cdd:pfam13868 326 E 326
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5045-5081 |
7.06e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 51.33 E-value: 7.06e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1988774674 5045 IRLLEAQIATGGIIDPEESHRLPVEVAYNRGFFDEEM 5081
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
3244-3607 |
7.56e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3244 ELLKLKNKIEEENQRLIkkdkdSTQKLLAEEAENMRKLAED----AARLSVeAQEAARLR-QI--AEDDLNqqrALAEKm 3316
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLV-----EMARELAELNEAESDLEQDyqaaSDHLNL-VQTALRQQeKIerYQADLE---ELEER- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3317 LKEKMQAIQEASRlkaEAEMLQKQKDLAQEQAQKLleDKQL--MQQRLEE-ETE--EYHKSLE-VERKRQLeimaeaerl 3390
Cdd:PRK04863 364 LEEQNEVVEEADE---QQEENEARAEAAEEEVDEL--KSQLadYQQALDVqQTRaiQYQQAVQaLERAKQL--------- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3391 rLQVSQLSeaqaraeeeakkfkkqADKVATRLHEteIATQEKMTVVERLEFE-RLNTSKEADD--------LRKAIADLE 3461
Cdd:PRK04863 430 -CGLPDLT----------------ADNAEDWLEE--FQAKEQEATEELLSLEqKLSVAQAAHSqfeqayqlVRKIAGEVS 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3462 NEKA------------RLKKEAEELQNKSKEMADAQQKKIEHEKTV-LQQTFMTEKEMLLKKEKLIEDEKKRLESQFE-- 3526
Cdd:PRK04863 491 RSEAwdvarellrrlrEQRHLAEQLQQLRMRLSELEQRLRQQQRAErLLAEFCKRLGKNLDDEDELEQLQEELEARLEsl 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3527 -EEVKKAKALKDEQERQKQQMEQEKKTLQA------TMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKL 3599
Cdd:PRK04863 571 sESVSEARERRMALRQQLEQLQARIQRLAArapawlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
....*...
gi 1988774674 3600 REKLQQLE 3607
Cdd:PRK04863 651 AARKQALD 658
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2361-2573 |
8.46e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 57.93 E-value: 8.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2361 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAvdAEKQKtniqleLQELK 2440
Cdd:TIGR02794 78 EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAE--AERKA------KEEAA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2441 NLSEQQIKDKSQQvdealhsrtkieeeirliriqlettEKQKYTAESELKQLRDRAAEAEKLRKLAQDE----AEKLRKQ 2516
Cdd:TIGR02794 150 KQAEEEAKAKAAA-------------------------EAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKAK 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774674 2517 VSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDL--EKLRMQAEEAERQVKQAEIEK 2573
Cdd:TIGR02794 205 AAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLasGSNAEKQGGARGAAAGSEVDK 263
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2543-2725 |
8.84e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 58.35 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2543 KQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAhEAAQKSAAAELQSKhmsfaektskleeslkQEHGAVLQLQQ 2622
Cdd:COG2268 180 EDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIA-QANREAEEAELEQE----------------REIETARIAEA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2623 EAERLKKQQE---DAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALK 2699
Cdd:COG2268 243 EAELAKKKAEerrEAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAE 322
|
170 180
....*....|....*....|....*.
gi 1988774674 2700 QKEMAEEELERQRKIAESTAQQKLTA 2725
Cdd:COG2268 323 AEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2001-2563 |
9.23e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2001 SELKDLRLRIEDCEAG-TVARIRKPVEKEPLKEYIQKTTEQKKVQGELDGLKKDL-----------DKVSVKTQEVLAsp 2068
Cdd:PRK02224 213 SELAELDEEIERYEEQrEQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaeterereelaEEVRDLRERLEE-- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2069 qpsasapvLRSELDltvqkmdhaHMLSSVYLEKL--KTVEMVIRNTQGAEgvlKQYEDCLREVHTVPSDV-KEVETYRAK 2145
Cdd:PRK02224 291 --------LEEERD---------DLLAEAGLDDAdaEAVEARREELEDRD---EELRDRLEECRVAAQAHnEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2146 LKKMRTEAEDEQPVFDSLEEELKKASAVSDkmvrvhsERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQLgrqlgy 2225
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVE-------DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL------ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2226 yRESYDwlirwiaDAKQRQEKIQAvpitDSKTLKEQLAQEKKLLEEieqnkDKVDECQKYAK--AYIDTIKDYELQ---L 2300
Cdd:PRK02224 418 -REERD-------ELREREAELEA----TLRTARERVEEAEALLEA-----GKCPECGQPVEgsPHVETIEEDRERveeL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2301 VAYKAQVEPLVSPLKKtKLDSASDniiqeYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLkaeeRKKMAEMQ 2380
Cdd:PRK02224 481 EAELEDLEEEVEEVEE-RLERAED-----LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL----RERAAELE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2381 AEldkqkqlAEAHAKAIAKAEKEAQElklkmqeevsKREIAAvDAEKQKTNIQLELQELKNLSEQQ--IKDKSQQVDEAL 2458
Cdd:PRK02224 551 AE-------AEEKREAAAEAEEEAEE----------AREEVA-ELNSKLAELKERIESLERIRTLLaaIADAEDEIERLR 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2459 HSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKlrklaqDEAEKLRKQVSEETQKKRQAEEELK------ 2532
Cdd:PRK02224 613 EKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDK------ERAEEYLEQVEEKLDELREERDDLQaeigav 686
|
570 580 590
....*....|....*....|....*....|....*
gi 1988774674 2533 RKSEAEKEAAKQKQKALED----LEKLRMQAEEAE 2563
Cdd:PRK02224 687 ENELEELEELRERREALENrveaLEALYDEAEELE 721
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3436-3613 |
1.09e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3436 VERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQ-------QTFMTEKEMLl 3508
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfSDFLDRLSAL- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3509 kkEKLIEDEKKRLESQfeeevkkaKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQ 3588
Cdd:COG3883 125 --SKIADADADLLEEL--------KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
170 180
....*....|....*....|....*
gi 1988774674 3589 ERILAEENQKLREKLQQLEDAQKDQ 3613
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
3281-3623 |
1.11e-07 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 58.19 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3281 LAEDAARLSVEAQEAARLRQIAEDDLNQQRA-------LAEKMLKEKMQAIQEA-----------SRLKAEAEMLQKQKD 3342
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAkfkelylAKEEDLKRQNAVLQEAqveldalqnqlALARAEMENIKAVAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3343 LAQEQAQKLLED------------KQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAER----LRLQVSQlSEAQARAEE 3406
Cdd:pfam03528 86 VSENTKQEAIDEvksqwqeevaslQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEReiadLRRRLSE-GQEEENLED 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3407 EAKKFKKQADKVATRL--HETEIAT--------QEKMTVVERLEFERLNTSKEAD-----DLRKAIADLENEKARLKKEA 3471
Cdd:pfam03528 165 EMKKAQEDAEKLRSVVmpMEKEIAAlkaklteaEDKIKELEASKMKELNHYLEAEkscrtDLEMYVAVLNTQKSVLQEDA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3472 EELQNKSKEMADA-QQKKIEHekTVLQQTFMTEKEMLLKKEKLIEDEKKRLESqfeeevkkakALKDEQERQKQQmeqek 3550
Cdd:pfam03528 245 EKLRKELHEVCHLlEQERQQH--NQLKHTWQKANDQFLESQRLLMRDMQRMES----------VLTSEQLRQVEE----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3551 ktlqatmdaaLSKQKEAEEEMLRKQKEMQELERQRLEQERILA-------EENQKLREKLQQLEDAQKDQHTRETDKVLH 3623
Cdd:pfam03528 308 ----------IKKKDQEEHKRARTHKEKETLKSDREHTVSIHAvfspagvETSAPLSNVEEQINSAHGSVHSLDTDVVLG 377
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2362-2594 |
1.12e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 57.55 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2362 EKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREiaavdAEKQKTNIQLELQELKN 2441
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2442 LSEQQIKDKSQQvDEALHSRTKIEEEIRliriQLETTEKQKYTAESElkqlrdraAEAEKLRKLAQDEAEKlrkqvSEET 2521
Cdd:TIGR02794 124 AKAKQAAEAKAK-AEAEAERKAKEEAAK----QAEEEAKAKAAAEAK--------KKAEEAKKKAEAEAKA-----KAEA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774674 2522 QKKRQAeEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEI------EKEKQIKVAHEAAQKSAAAELQS 2594
Cdd:TIGR02794 186 EAKAKA-EEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELgdifglASGSNAEKQGGARGAAAGSEVDK 263
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2137-2570 |
1.24e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.90 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2137 KEVETYRAKLKKMRTEAEDEQpvfDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQREL 2216
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKL---KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2217 EQLGRQLGyyresydwlirwIADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTI-KD 2295
Cdd:TIGR00606 768 EEQETLLG------------TIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQeKQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2296 YELQLVAYKAQVeplvsplkKTKLDSASDNIIQEYvtlrtrYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKaeerkK 2375
Cdd:TIGR00606 836 HELDTVVSKIEL--------NRKLIQDQQEQIQHL------KSKTNELKSEKLQIGTNLQRRQQFEEQLVELST-----E 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2376 MAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNL----SEQQIKDKS 2451
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgKDDYLKQKE 976
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2452 Q-------QVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKK 2524
Cdd:TIGR00606 977 TelntvnaQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEH 1056
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1988774674 2525 RQAEEELKRKSEAEKEAAKQkQKALEDlEKLRMQAEEAERQVKQAE 2570
Cdd:TIGR00606 1057 QKLEENIDLIKRNHVLALGR-QKGYEK-EIKHFKKELREPQFRDAE 1100
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3184-3605 |
1.32e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3184 KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQM----EELLKLKNKIEEENQRL 3259
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVedrrEEIEELEEEIEELRERF 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3260 --IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAE---------------------DDLNQQRALAEKM 3316
Cdd:PRK02224 401 gdAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpvegsphvETIEEDRERVEEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3317 LKEKMQAIQEASRLKAEAEMLQKQKDLAQEqAQKLLEDKQLMQQRLEEETEEyhksleVERKRQleimaEAERLRLQVSQ 3396
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVEAEDR-IERLEERREDLEELIAERRET------IEEKRE-----RAEELRERAAE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3397 LSEAQARAEEEAKKFKKQADKVATRLHETEiatQEKMTVVERLefERLNTSKEADDlrkAIADLENEKARLKKEAEELQN 3476
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELN---SKLAELKERI--ESLERIRTLLA---AIADAEDEIERLREKREALAE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3477 KSKEmadaqqkkiehektvlqqtfmtekemllKKEKLIE--DEKKRLESQFEEE-VKKAKALKDEQERQKQQME------ 3547
Cdd:PRK02224 621 LNDE----------------------------RRERLAEkrERKRELEAEFDEArIEEAREDKERAEEYLEQVEekldel 672
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 3548 -QEKKTLQATMDAALSKQKEAEEemLRKQKEMQELERQRLEQERILAEENQ----KLREKLQQ 3605
Cdd:PRK02224 673 rEERDDLQAEIGAVENELEELEE--LRERREALENRVEALEALYDEAEELEsmygDLRAELRQ 733
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2448-2867 |
1.57e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2448 KDKSQQVDEALHSR--------TKIEEEIRLIRIQ--LETTEKQKYTAESELKQLRDRAAeaeklrkLAQdeaEKLRKQv 2517
Cdd:PRK04863 279 NERRVHLEEALELRrelytsrrQLAAEQYRLVEMAreLAELNEAESDLEQDYQAASDHLN-------LVQ---TALRQQ- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2518 seetQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVK----------QAEIEKEKQIKVAHEAAQKS 2587
Cdd:PRK04863 348 ----EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDelksqladyqQALDVQQTRAIQYQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2588 AAAELQSKHMSFAEKtsKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAlrLRLQAEDEAh 2667
Cdd:PRK04863 424 ERAKQLCGLPDLTAD--NAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEV--SRSEAWDVA- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2668 kktlaqeeaekqkeeaeREAKKRAKaeesalKQKEMAEEELERQRKIAEstAQQKLTAEQELIRLRADF----------- 2736
Cdd:PRK04863 499 -----------------RELLRRLR------EQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFckrlgknldde 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2737 DNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELakvrSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEE 2816
Cdd:PRK04863 554 DELEQLQEELEARLESLSESVSEARERRMALRQQL----EQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDV 629
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 2817 ASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAE 2867
Cdd:PRK04863 630 TEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2685-3122 |
1.60e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 57.99 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2685 REAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 2764
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2765 KQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAE 2844
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2845 AERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQK 2924
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2925 AIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKV 3004
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3005 KKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKL 3084
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430
....*....|....*....|....*....|....*...
gi 1988774674 3085 KEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQ 3122
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAA 519
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2242-2664 |
1.67e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 57.83 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2242 QRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAY---KAQVEPLVSPLKK-T 2317
Cdd:pfam05557 121 QRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQeqdSEIVKNSKSELARiP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2318 KLDSASDNIIQEYVTLRTRYSELMTLTSQyikfITDTQRRLDDEEKAAEKLKAEERKKmAEMQAELDKQKQLAEAHAKAI 2397
Cdd:pfam05557 201 ELEKELERLREHNKHLNENIENKLLLKEE----VEDLKRKLEREEKYREEAATLELEK-EKLEQELQSWVKLAQDTGLNL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2398 AKAEKEAQELKLKMQEE-VSKREIAAVDAE-KQKTNIQLELQE-----LKNLSEQQIKDKSQqvdEALHSRTK-----IE 2465
Cdd:pfam05557 276 RSPEDLSRRIEQLQQREiVLKEENSSLTSSaRQLEKARRELEQelaqyLKKIEDLNKKLKRH---KALVRRLQrrvllLT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2466 EEIRLIRIQLETTEKQKYTAESELKQLRdRAAEAEKLRKLAQDEAEKLRKQVS----EETQKKRQA-----EEELKRKSE 2536
Cdd:pfam05557 353 KERDGYRAILESYDKELTMSNYSPQLLE-RIEEAEDMTQKMQAHNEEMEAQLSvaeeELGGYKQQAqtlerELQALRQQE 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2537 AEKEAAKQKQKALE---DLEKLRMQAEEAERQVKQAEIEKEKqikvaHEAAQKSAAAELQSKHMSfAEKTSKLEESLKQE 2613
Cdd:pfam05557 432 SLADPSYSKEEVDSlrrKLETLELERQRLREQKNELEMELER-----RCLQGDYDPKKTKVLHLS-MNPAAEAYQQRKNQ 505
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 2614 HGavlQLQQEAERLKKQQEDAENSREEAEKELEKWRQKAN-EALRLRLQAED 2664
Cdd:pfam05557 506 LE---KLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFkEVLDLRKELES 554
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
1168-1275 |
1.69e-07 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 52.79 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1168 QSEDMTAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQ-QTNLENLEQAFSVAEKDLGV 1246
Cdd:cd21313 3 DAKKQTPKQRLLGWIQ---NKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDpQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1988774674 1247 TRLLDPEDVDVPHPDEKSIITYVSSLYDA 1275
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
1028-1160 |
1.73e-07 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 53.47 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1028 ASPEVDWDHSLGEPEEKtwpnfiederdrvqkKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVL---------S 1098
Cdd:cd21331 8 ENQDIDWTLLEGETREE---------------RTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnkvN 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 1099 GETLPREKGRMRfhKLQNVQIALDFLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 1160
Cdd:cd21331 71 KPPYPKLGANMK--KLENCNYAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3211-3415 |
1.85e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3211 DEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSV 3290
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3291 EAQEAARLRQIAE--------DDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRL 3362
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 3363 EEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQA 3415
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2486-2874 |
1.98e-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: 57.60 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2486 ESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQkqkALEDLEKLRMQAEEAERQ 2565
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ---SREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2566 vkQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKtskleeslkqehgaVLQLQQEAERLKKQQEDAENSREEAEKEl 2645
Cdd:pfam07888 110 --SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQR--------------VLERETELERMKERAKKAGAQRKEEEAE- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2646 ekwrqkaNEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEeelerQRKIAESTAqqkltA 2725
Cdd:pfam07888 173 -------RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA-----HRKEAENEA-----L 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2726 EQELIRLRADFDNAEQQRSLLEDELyrlknEVAAAQQQRKQLEDELAKVRS-EMDILIQLKTKAEKETMSNTEKSKQLL- 2803
Cdd:pfam07888 236 LEELRSLQERLNASERKVEGLGEEL-----SSMAAQRDRTQAELHQARLQAaQLTLQLADASLALREGRARWAQERETLq 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 2804 ---EAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEklaAISEATRLKTEAEIALKEKE 2874
Cdd:pfam07888 311 qsaEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSE---SRRELQELKASLRVAQKEKE 381
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2361-2721 |
2.03e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 57.65 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2361 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQL--ELQE 2438
Cdd:pfam15709 172 ERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERNLEVaaELSG 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2439 LKNLSEQQIKDKSQQVDEALHSRT-------KIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAE 2511
Cdd:pfam15709 252 PDVINSKETEDASERGAFSSDSVVedpwlssKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2512 K-LRKQVSEETQKKRQAEEELKRKSEAEKEaaKQKQKALEDLEKLRMQAEEaERQVKQAEIEKEKQiKVAHEAAQKSAAA 2590
Cdd:pfam15709 332 KaSRDRLRAERAEMRRLEVERKRREQEEQR--RLQQEQLERAEKMREELEL-EQQRRFEEIRLRKQ-RLEEERQRQEEEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2591 ELQSKHMSFAEKTSKLEEslKQEHGAVLQLQQeaerlKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEahkkt 2670
Cdd:pfam15709 408 RKQRLQLQAAQERARQQQ--EEFRRKLQELQR-----KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE----- 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 2671 laqeEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQ 2721
Cdd:pfam15709 476 ----RLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2355-2552 |
2.32e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.74 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2355 QRRLDDEEKaaEKLKAEERKKMAEMQA--ELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKreiAAVDAEKQktni 2432
Cdd:PRK09510 100 QERLKQLEK--ERLAAQEQKKQAEEAAkqAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK---AAAEAKKK---- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2433 qlELQELKNLSEQQIKDKsqqvdealhsrtkieeeirliriqLETTEKQKYTAESELKQLRDRAAEAEKLRKlAQDEAEK 2512
Cdd:PRK09510 171 --AEAEAAKKAAAEAKKK------------------------AEAEAAAKAAAEAKKKAEAEAKKKAAAEAK-KKAAAEA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1988774674 2513 LRKQVSEETQKKRQAEEELKRKSeAEKEAAKQKQKALEDL 2552
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKA-AEKAAAAKAAAEVDDL 262
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2233-2933 |
2.42e-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: 58.14 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2233 LIRWIADAKQRQEKIQAVPITDSKTLKEQLAQE---------KKLLEEIEQNKDKVDECQKYAKAY--IDTIKDYELQlv 2301
Cdd:TIGR01612 1031 IEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEigkniellnKEILEEAEINITNFNEIKEKLKHYnfDDFGKEENIK-- 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2302 aYKAQVEPLVSPLKKtkLDSASDNIIQEYVTLRTRySElmtltsqyiKFITDTQRRLDDEEKAAEKLKAEE-----RKKM 2376
Cdd:TIGR01612 1109 -YADEINKIKDDIKN--LDQKIDHHIKALEEIKKK-SE---------NYIDEIKAQINDLEDVADKAISNDdpeeiEKKI 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2377 AEMQAELDKQKQLAEAHAK---AIAKAEK------EAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQE--LKNLSEq 2445
Cdd:TIGR01612 1176 ENIVTKIDKKKNIYDEIKKllnEIAEIEKdktsleEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEayIEDLDE- 1254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2446 qIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRaaeAEKLRKLAQDEAEK---------LRKQ 2516
Cdd:TIGR01612 1255 -IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDI---REKSLKIIEDFSEEsdindikkeLQKN 1330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2517 VSEETQKKRQAEEELKRKSEAEKEAAKQK-QKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEaaqksaaaelqsk 2595
Cdd:TIGR01612 1331 LLDAQKHNSDINLYLNEIANIYNILKLNKiKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD------------- 1397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2596 HMSFAEKTSKLEESL--KQEHGAVLQLQQEAERLKKQQEDA----ENSREEAE------KELEKWRQKANEALRLRLQAE 2663
Cdd:TIGR01612 1398 DINLEECKSKIESTLddKDIDECIKKIKELKNHILSEESNIdtyfKNADENNEnvlllfKNIEMADNKSQHILKIKKDNA 1477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2664 DEAHKKTLAQEEAEKQKEEAER-EAKKRAKAEEsalKQKEMAEeelerQRKIAESTAQQKLTAeqelIRLRADFDNAEQQ 2742
Cdd:TIGR01612 1478 TNDHDFNINELKEHIDKSKGCKdEADKNAKAIE---KNKELFE-----QYKKDVTELLNKYSA----LAIKNKFAKTKKD 1545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2743 RSLLEDELYRLKN----EVAAAQQQRKQLEDElaKVRSEMDIliqLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEAS 2818
Cdd:TIGR01612 1546 SEIIIKEIKDAHKkfilEAEKSEQKIKEIKKE--KFRIEDDA---AKNDKSNKAAIDIQLSLENFENKFLKISDIKKKIN 1620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2819 rlRAISEEAKHQRQIAEEEAARQRAEaeriLKEKLAAISEatrLKTEAEiALKEKEAENERLRRQAEDEAYQRKALEDQA 2898
Cdd:TIGR01612 1621 --DCLKETESIEKKISSFSIDSQDTE----LKENGDNLNS---LQEFLE-SLKDQKKNIEDKKKELDELDSEIEKIEIDV 1690
|
730 740 750
....*....|....*....|....*....|....*....
gi 1988774674 2899 SQHKQEIE----EKIVQLKKSSEAEMERQKAIVDDTLKQ 2933
Cdd:TIGR01612 1691 DQHKKNYEigiiEKIKEIAIANKEEIESIKELIEPTIEN 1729
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2604-2928 |
2.43e-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: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2604 SKLEESLkQEHGAVLQLQQEAERlkkqqeDAENSREEAEKELEKWRQKANEaLRLRLQAEDEAHKKTLAQEEAEKQKEEA 2683
Cdd:pfam07888 34 NRLEECL-QERAELLQAQEAANR------QREKEKERYKRDREQWERQRRE-LESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2684 EREAKKRAKAEESAL-KQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 2762
Cdd:pfam07888 106 LSASSEELSEEKDALlAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2763 QRKQLEDELAKVRSEMD----ILIQLKTKAEKETMSNTEKSKQLLEAEAAKmKDLAEEASRLrAISEEAKH--QRQIAEE 2836
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALL-EELRSLQERL-NASERKVEglGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2837 EAARQRAEAEriLKEKLAAISEATRLKTEAEIALKEkeaenERLRRQAEDEAYQRKALEDQasQHKQEIEEKIVQLKKS- 2915
Cdd:pfam07888 264 AAQRDRTQAE--LHQARLQAAQLTLQLADASLALRE-----GRARWAQERETLQQSAEADK--DRIEKLSAELQRLEERl 334
|
330
....*....|...
gi 1988774674 2916 SEAEMERQKAIVD 2928
Cdd:pfam07888 335 QEERMEREKLEVE 347
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
3166-3619 |
2.45e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.42 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3166 QQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEE- 3244
Cdd:pfam05483 102 KQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREEt 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3245 ---LLKLKNKIEE------------ENQRL-----IKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAarlrqiaED 3304
Cdd:pfam05483 182 rqvYMDLNNNIEKmilafeelrvqaENARLemhfkLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEK-------EN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3305 DLNQQRALAEKMlKEKMQAIQEASRLKAE--AEMLQKQKDLAQEqaqklLEDKQLMQQR-------LEEETEEYHKS--- 3372
Cdd:pfam05483 255 KMKDLTFLLEES-RDKANQLEEKTKLQDEnlKELIEKKDHLTKE-----LEDIKMSLQRsmstqkaLEEDLQIATKTicq 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3373 LEVERKRQLEIMAEAERLR-LQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEAD 3451
Cdd:pfam05483 329 LTEEKEAQMEELNKAKAAHsFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3452 DLRKAIAD---LENEKARLKKEAEELQNKSKEMADA-QQKKIEHEKTVLQQTFMTEKEMLLKKEklIEDEKKRLESQfee 3527
Cdd:pfam05483 409 ELKKILAEdekLLDEKKQFEKIAEELKGKEQELIFLlQAREKEIHDLEIQLTAIKTSEEHYLKE--VEDLKTELEKE--- 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3528 evkKAKALKDEQERQKQQMEQEKKTLQAT-MDAALSKQKE-------AEEEMLRKQKEMQELERQ-RLEQERILAEENQK 3598
Cdd:pfam05483 484 ---KLKNIELTAHCDKLLLENKELTQEASdMTLELKKHQEdiinckkQEERMLKQIENLEEKEMNlRDELESVREEFIQK 560
|
490 500
....*....|....*....|.
gi 1988774674 3599 LREKLQQLEDAQKDQHTRETD 3619
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYE 581
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
3016-3368 |
2.56e-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: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3016 RQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKcsaAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLA 3095
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQ---SREKHEELEEKYKELSASSEELSEEKDALLAQR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3096 KEAEAAKEKAEREAALLRQQAEEAERQktaaeeeAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKH 3175
Cdd:pfam07888 125 AAHEARIRELEEDIKTLTQRVLERETE-------LERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3176 KKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQR-----------------LKDEVDDAVKQRGQVEEELFKV 3238
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrslqerlnaserkvegLGEELSSMAAQRDRTQAELHQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3239 KVQMEEL--------LKLKnkieeENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQR 3310
Cdd:pfam07888 278 RLQAAQLtlqladasLALR-----EGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREK 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774674 3311 ALAEKMLKEKMQAIQEasrLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEE 3368
Cdd:pfam07888 353 DCNRVQLSESRRELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2352-2643 |
2.60e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 57.18 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2352 TDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHA---KAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQ 2428
Cdd:pfam02029 52 PSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIAdekESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2429 KTNIQlelqeLKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQD 2508
Cdd:pfam02029 132 ETEIR-----EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2509 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQvkqaEIEKEKQikvaheaAQKSA 2588
Cdd:pfam02029 207 VKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESE----EFEKLRQ-------KQQEA 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2589 AAELQSKHMSFAEKTSKLEESLKQEHgavlqlQQEAERLKKQQEDAENSREEAEK 2643
Cdd:pfam02029 276 ELELEELKKKREERRKLLEEEEQRRK------QEEAERKLREEEEKRRMKEEIER 324
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3167-3369 |
2.81e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3167 QADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELL 3246
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3247 K-----------------------------LKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEdaarLSVEAQEAAR 3297
Cdd:COG3883 93 RalyrsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 3298 LRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEY 3369
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2347-2928 |
3.18e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.22 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2347 YIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKqlaeaHAKAIAKAEKEAQELKLKMQEEVSKreiaavdAE 2426
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYN-----NLKSALNELSSLEDMKNRYESEIKT-------AE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2427 KQKTNIQLELQELKNLSEQQIKDKSqqvDEALHSRTKIEEEIRLIRiQLETTEKQKYTAESELKQLRDraaeaeKLRKLA 2506
Cdd:PRK01156 263 SDLSMELEKNNYYKELEERHMKIIN---DPVYKNRNYINDYFKYKN-DIENKKQILSNIDAEINKYHA------IIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2507 QDEAEKlrkqvsEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQ--AEIEKEKQIKVAHEAA 2584
Cdd:PRK01156 333 VLQKDY------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERmsAFISEILKIQEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2585 QKSAAAELQSKHMSFAEKTSKLEESLK---------QEHGAVLQLQ------------QEAERLKKQQEDAENSREEAEK 2643
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRalrenldelSRNMEMLNGQsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2644 ELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEEL-ERQRKIAESTAQQK 2722
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIkNRYKSLKLEDLDSK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2723 ltaeqelirlRADFDNAEQQRSLLE-DELYRLKNEVaaaQQQRKQLEDELAKVRSEMDiliqlktkaekETMSNTEKSKQ 2801
Cdd:PRK01156 567 ----------RTSWLNALAVISLIDiETNRSRSNEI---KKQLNDLESRLQEIEIGFP-----------DDKSYIDKSIR 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2802 LLEAEAAKMKDLAEEASRLRAISEEAKhqrqiaeeeaarqraEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLR 2881
Cdd:PRK01156 623 EIENEANNLNNKYNEIQENKILIEKLR---------------GKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSR 687
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2882 RQAED---EAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVD 2928
Cdd:PRK01156 688 KALDDakaNRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGD 737
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2861-3398 |
3.68e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2861 RLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKivqlkKSSEAEMERQKAIVDDTLKQRRVVEEE 2940
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL-----EELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2941 IRILKLNFEKASsgkldLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKA 3020
Cdd:COG4717 125 LQLLPLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3021 ALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSIT--QKKLKEEYEKAKKLAKEA 3098
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLalLGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3099 EAAKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKL 3178
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3179 AEQTLKQKFQVEQE--LTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELfKVKVQMEELLKLKNKIEEEN 3256
Cdd:COG4717 360 EEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL-EELLEALDEEELEEELEELE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3257 QRlikkdkdstqklLAEEAENMRKLAEDAARLSveaqeaARLRQIAEDDLNQQRALAEKMLKEKMQ-AIQEASRLKAEAE 3335
Cdd:COG4717 439 EE------------LEELEEELEELREELAELE------AELEQLEEDGELAELLQELEELKAELReLAEEWAALKLALE 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 3336 MLQK-QKDLAQEQAQKLLEDkqlMQQRLEEETEEYHKSLEVERKRQLEIMAEAERlRLQVSQLS 3398
Cdd:COG4717 501 LLEEaREEYREERLPPVLER---ASEYFSRLTDGRYRLIRIDEDLSLKVDTEDGR-TRPVEELS 560
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
2361-2658 |
4.05e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 56.40 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2361 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELK 2440
Cdd:pfam06160 87 ALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2441 NLSEQQIKDKSQQVDEALHSRTkIEEEIRLIRI-----QLETT---------------EKQKYT-----AESELKQLRDR 2495
Cdd:pfam06160 167 ELTESGDYLEAREVLEKLEEET-DALEELMEDIpplyeELKTElpdqleelkegyremEEEGYAlehlnVDKEIQQLEEQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2496 AAEAEK-LRKLAQDEAEKLRKQVSEETQK-----------KRQAEEELKRKSEAEKEAAKQKQKALEDLEKL----RMQA 2559
Cdd:pfam06160 246 LEENLAlLENLELDEAEEALEEIEERIDQlydllekevdaKKYVEKNLPEIEDYLEHAEEQNKELKEELERVqqsyTLNE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2560 EEAERqvkQAEIEKE-KQIKVAHEAAQKsaaaELQSKHMSFAEKTSKLEESLKQehgaVLQLQQEAERLKKQQEDAENSR 2638
Cdd:pfam06160 326 NELER---VRGLEKQlEELEKRYDEIVE----RLEEKEVAYSELQEELEEILEQ----LEEIEEEQEEFKESLQSLRKDE 394
|
330 340
....*....|....*....|
gi 1988774674 2639 EEAEKELEKWRQKANEALRL 2658
Cdd:pfam06160 395 LEAREKLDEFKLELREIKRL 414
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2698-2931 |
4.66e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.97 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2698 LKQKEMAEEELERQRKIAESTAQQKLTAEQElirlradfdnAEQQRsLLEDELYRLknevaAAQQQRKQLEDelakvrse 2777
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQA----------AEQER-LKQLEKERL-----AAQEQKKQAEE-------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2778 mdiliQLKTKAEKETMSNTEKSKQlleAEAAKMKdLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILK-EKLAAI 2856
Cdd:PRK09510 123 -----AAKQAALKQKQAEEAAAKA---AAAAKAK-AEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKaEAEAAA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2857 SEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDqasqhKQEIEEKIVQLKKSSEAEMERQKAIVDDTL 2931
Cdd:PRK09510 194 KAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAE-----AKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2355-2583 |
5.06e-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: 55.31 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2355 QRRLDDEEKAAEKLKA--EERKKMAEMQAELDKQ-KQLAEAHAKAIAKAEKEAQELKLKMQEEVSK---REIAAVDAEKQ 2428
Cdd:pfam13868 65 EERKEERKRYRQELEEqiEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKLEKQRQLREeidEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2429 KTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESElkQLRDRAAEAEKLRKLAQD 2508
Cdd:pfam13868 145 LEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERD--ELRAKLYQEEQERKERQK 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2509 EAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEA 2583
Cdd:pfam13868 223 EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK 297
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2446-2727 |
5.07e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.49 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2446 QIKDKSQQVDEAlhsrtKIEEEIRLIRIQlettekqkytaeselkqlRDRAAEAEKLRKLAQDEAEKLRKQVSE--ETQK 2523
Cdd:PRK05035 440 AIEQEKKKAEEA-----KARFEARQARLE------------------REKAAREARHKKAAEARAAKDKDAVAAalARVK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2524 KRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAElqskhmsfAEKT 2603
Cdd:PRK05035 497 AKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQ--------QAAN 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2604 SKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKwRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEA 2683
Cdd:PRK05035 569 AEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDP-KKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA 647
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1988774674 2684 EREAKKRAKAEESALKQKEMAEEELERQRKIAESTA----QQKLTAEQ 2727
Cdd:PRK05035 648 VAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAiaraKAKKAAQQ 695
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2380-2842 |
5.84e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 56.30 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2380 QAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQktniqleLQELKNLSEQQIKDKSQQVDEA-L 2458
Cdd:pfam09731 81 EPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKA-------LEEVLKEAISKAESATAVAKEAkD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2459 HSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAE--AEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKrKSE 2536
Cdd:pfam09731 154 DAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEklKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLD-NVE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2537 AEKEAAKQKQKALEDLEKLrmqaEEAERQVKQAEIEKekqikvaheaaqKSAAAELQSKHMSFAEKtSKLEESLKQEHGA 2616
Cdd:pfam09731 233 EKVEKAQSLAKLVDQYKEL----VASERIVFQQELVS------------IFPDIIPVLKEDNLLSN-DDLNSLIAHAHRE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2617 VLQLQQEAERLKKQ-QEDAENSREEAEKELEKwrqkANEALRLRLQAEDEAHKKTLaqeeaekqkeeaerEAKKRAKAEE 2695
Cdd:pfam09731 296 IDQLSKKLAELKKReEKHIERALEKQKEELDK----LAEELSARLEEVRAADEAQL--------------RLEFEREREE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2696 SALKQKEMAEEELERQRKIAESTAQQKL-TAEQEL-IRLRADFDNA-EQQRSLLE---DELYRLKNEVAAAQQQRKQLED 2769
Cdd:pfam09731 358 IRESYEEKLRTELERQAEAHEEHLKDVLvEQEIELqREFLQDIKEKvEEERAGRLlklNELLANLKGLEKATSSHSEVED 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774674 2770 ELAKVRSemdilIQLKTKAEKETM--SNTEKSKQLLEAEAAKMKDLAEE----ASRLRAISEEAKhQRQIAEEEAARQR 2842
Cdd:pfam09731 438 ENRKAQQ-----LWLAVEALRSTLedGSADSRPRPLVRELKALKELASDdevvKAALASLPEEAY-QRGVYTEAALRER 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2353-2590 |
5.96e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2353 DTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELklkmqeevsKREIAAVDAEKQKTNI 2432
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL---------QAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2433 QLElqelKNLSEQQIKDKSQQVDEALHSRTKIEEEIRliriQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 2512
Cdd:COG3883 87 ELG----ERARALYRSGGSVSYLDVLLGSESFSDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774674 2513 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAA 2590
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2739-2909 |
6.04e-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: 54.16 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2739 AEQQRSLLEdeLYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKEtMSNTEKSKQLLEAEAAKMKDLAEEA- 2817
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLELEIEEVEARIKKYe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2818 SRLRAIS--EEAKH-QRQIaeEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAL 2894
Cdd:COG1579 80 EQLGNVRnnKEYEAlQKEI--ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....*
gi 1988774674 2895 EDQASQHKQEIEEKI 2909
Cdd:COG1579 158 LEELEAEREELAAKI 172
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2299-2830 |
6.44e-07 |
|
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: 56.37 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2299 QLVAYKAQveplvSPLKKTKLDSASDNIIQ---EYVTLRTRyseLMTLTSQYikfiTDTQRRLddeEKAAEKLKAEErKK 2375
Cdd:pfam10174 276 QMEVYKSH-----SKFMKNKIDQLKQELSKkesELLALQTK---LETLTNQN----SDCKQHI---EVLKESLTAKE-QR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2376 MAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL---KLKMQEEVSKREiAAVDAEKQKTNIqleLQE-LKNLSEQqIKDKS 2451
Cdd:pfam10174 340 AAILQTEVDALRLRLEEKESFLNKKTKQLQDLteeKSTLAGEIRDLK-DMLDVKERKINV---LQKkIENLQEQ-LRDKD 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2452 QQVDEalhsrtkieeeirlIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEEL 2531
Cdd:pfam10174 415 KQLAG--------------LKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2532 KRKSEAEKEAAKQKQKALEDLEK----LRMQAEEAERQVKQAEIEKEK----------QIKVAHEAAQKSAAAElqskhm 2597
Cdd:pfam10174 481 KEKVSALQPELTEKESSLIDLKEhassLASSGLKKDSKLKSLEIAVEQkkeecsklenQLKKAHNAEEAVRTNP------ 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2598 SFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKAneALRLRLQAEDEAHKKTLAQEEAE 2677
Cdd:pfam10174 555 EINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLT--LRQMKEQNKKVANIKHGQQEMKK 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2678 KQKEEAErEAKKRAKAEESALKQKEMAE--EELERQRKIAESTAQQKLTAEQELirlradfdnAEQQRSLledelyrlkn 2755
Cdd:pfam10174 633 KGAQLLE-EARRREDNLADNSQQLQLEElmGALEKTRQELDATKARLSSTQQSL---------AEKDGHL---------- 692
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2756 eVAAAQQQRKQLEDELakvrsEMdiliqlKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQ 2830
Cdd:pfam10174 693 -TNLRAERRKQLEEIL-----EM------KQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2128-2736 |
6.45e-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: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2128 EVHTVPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAvsdkmvrvHSERDVELDHFRQQLSSLqDRWKAvFT 2207
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAER--------YAAARERLAELEYLRAAL-RLWFA-QR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2208 QIDLRQRELEQLgrqlgyyRESYDWLIRWIADAKQRQEKIQAvpitDSKTLKEQLAQ-----EKKLLEEIEQNKDKVDEC 2282
Cdd:COG4913 289 RLELLEAELEEL-------RAELARLEAELERLEARLDALRE----ELDELEAQIRGnggdrLEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2283 QKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLK--KTKLDSASDNIIQEYVTLRTRYSELmtltsqyikfiTDTQRRLDD 2360
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDL-----------RRELRELEA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2361 EEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIA-----KAEKEA-----------QELKLKMQEEVSKREIAAVD 2424
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGelievRPEEERwrgaiervlggFALTLLVPPEHYAAALRWVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2425 AEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTK-----IEEEI--RLIRIQLETTEkqkytaesELKQLRdRAA 2497
Cdd:COG4913 507 RLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHpfrawLEAELgrRFDYVCVDSPE--------ELRRHP-RAI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2498 EAEKLRKLAQDEAEK-LRKQVSEE-------TQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQA 2569
Cdd:COG4913 578 TRAGQVKGNGTRHEKdDRRRIRSRyvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2570 eiekEKQIKVAheaaqkSAAAELqskhmsfAEKTSKLEEsLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWR 2649
Cdd:COG4913 658 ----WDEIDVA------SAEREI-------AELEAELER-LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2650 QKANEALRLRLQAEDEAHkktlaqEEAEKQKEEAEREAKKRAKAEESALKQKEMAeEELERQRKIAESTAQQkltAEQEL 2729
Cdd:COG4913 720 KELEQAEEELDELQDRLE------AAEDLARLELRALLEERFAAALGDAVERELR-ENLEERIDALRARLNR---AEEEL 789
|
....*..
gi 1988774674 2730 IRLRADF 2736
Cdd:COG4913 790 ERAMRAF 796
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2425-2607 |
6.85e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 55.24 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2425 AEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETtEKQKYTAESELKQLRDRAAEAEKLRk 2504
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAA-EKAAKQAEQAAKQAEEKQKQAEEAK- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2505 lAQDEAEKLRKqvsEETQKKRQAEEELKRKSEAE---KEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKvah 2581
Cdd:TIGR02794 126 -AKQAAEAKAK---AEAEAERKAKEEAAKQAEEEakaKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKA--- 198
|
170 180
....*....|....*....|....*.
gi 1988774674 2582 EAAQKSAAAELQSKHMSFAEKTSKLE 2607
Cdd:TIGR02794 199 EAAKAKAAAEAAAKAEAEAAAAAAAE 224
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5148-5176 |
6.86e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.48 E-value: 6.86e-07
10 20
....*....|....*....|....*....
gi 1988774674 5148 IVDPETGKEMTVYEAYRKGLIDHQTYLEL 5176
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3489-3687 |
7.26e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 55.99 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3489 IEHEKTVLQqtfmTEKEMLlkkEKLIED-EKKRLESqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEA 3567
Cdd:PRK00409 504 IEEAKKLIG----EDKEKL---NELIASlEELEREL--EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3568 EEEMLRKQKEMQEL---ERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDIIHLTtiETTKTVYNGQNv 3644
Cdd:PRK00409 575 AQQAIKEAKKEADEiikELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVG--DEVKYLSLGQK- 651
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1988774674 3645 GDVVDGIDKKPDPLAFDGIRDKVPASRLHELGVLPKKEFDKLK 3687
Cdd:PRK00409 652 GEVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPK 694
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
3182-3589 |
7.67e-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: 55.67 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3182 TLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIK 3261
Cdd:pfam07888 8 TLEEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3262 KDKDSTQKLlaEEAENMRKLAEDA---------ARLSVEAQEAARLRQIAEDdlnqQRALAEKMLKEKMqaiqEASRLKA 3332
Cdd:pfam07888 88 ELRQSREKH--EELEEKYKELSASseelseekdALLAQRAAHEARIRELEED----IKTLTQRVLERET----ELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3333 EAEMLQKQKdlAQEQAQKllEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLseaqaraeeeakkfK 3412
Cdd:pfam07888 158 RAKKAGAQR--KEEEAER--KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL--------------T 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3413 KQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIE-- 3490
Cdd:pfam07888 220 QKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgr 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3491 ----HEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKE 3566
Cdd:pfam07888 300 arwaQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKE 379
|
410 420
....*....|....*....|....*
gi 1988774674 3567 AEEEMLRKQKEMQELER--QRLEQE 3589
Cdd:pfam07888 380 KEQLQAEKQELLEYIRQleQRLETV 404
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2734-3624 |
8.73e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2734 ADF-DNAEQQRSLLEDELyRLKNEVAAAQQQRKQLEDELAKVRSEMDiliqlktkaeketmsntekskQLLEAEAAKMKD 2812
Cdd:COG3096 271 ADYmRHANERRELSERAL-ELRRELFGARRQLAEEQYRLVEMARELE---------------------ELSARESDLEQD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2813 LAEEASRLRAISEEAKHQRQIAEEEAARqrAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDeaYQRk 2892
Cdd:COG3096 329 YQAASDHLNLVQTALRQQEKIERYQEDL--EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD--YQQ- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2893 ALEDQ---ASQHKQEIE-----EKIVQLKKSSEAEMERQKAIVDDTLKQrrvVEEEIRIL--KLNFEKASSGKLDLELEL 2962
Cdd:COG3096 404 ALDVQqtrAIQYQQAVQalekaRALCGLPDLTPENAEDYLAAFRAKEQQ---ATEEVLELeqKLSVADAARRQFEKAYEL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2963 nkLKNIADETQQSkiRAEEEA-EKLRKLaleeekrrreaeekvkkiaaaeeeaaRQRKAALEELERLRKKAEEARkQKDE 3041
Cdd:COG3096 481 --VCKIAGEVERS--QAWQTArELLRRY--------------------------RSQQALAQRLQQLRAQLAELE-QRLR 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3042 ADKEAEKQIV-VAQQAAQKCSAAEQ--QVQSVLAQQIEDSITQKklkeeyekakklakeaeaakEKAEREAALLRQQAEE 3118
Cdd:COG3096 530 QQQNAERLLEeFCQRIGQQLDAAEEleELLAELEAQLEELEEQA--------------------AEAVEQRSELRQQLEQ 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3119 AERQKTAAEEEAANQAKAQEDAERLRKEAEfeaakraqaeaAALMQKQQADTEMakhkklaEQTLKQKFQVEQELTKVKL 3198
Cdd:COG3096 590 LRARIKELAARAPAWLAAQDALERLREQSG-----------EALADSQEVTAAM-------QQLLEREREATVERDELAA 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3199 KLDETDKQKSVL-------DEELQRLKDE--------------VDDAV--------KQRGQVEEELFKVKVQMEELLKLK 3249
Cdd:COG3096 652 RKQALESQIERLsqpggaeDPRLLALAERlggvllseiyddvtLEDAPyfsalygpARHAIVVPDLSAVKEQLAGLEDCP 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3250 NKI-----------------EEENQRLIKKDKD--------------------STQKLLAEEAEnmrKLAEDAARLSVEA 3292
Cdd:COG3096 732 EDLyliegdpdsfddsvfdaEELEDAVVVKLSDrqwrysrfpevplfgraareKRLEELRAERD---ELAEQYAKASFDV 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3293 QEAARLRQIAEDDLNQQRALA-----EKMLKEKMQAIQEASRLKAEAE----MLQKQKDLAQEQAQ---------KLLED 3354
Cdd:COG3096 809 QKLQRLHQAFSQFVGGHLAVAfapdpEAELAALRQRRSELERELAQHRaqeqQLRQQLDQLKEQLQllnkllpqaNLLAD 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3355 KQLmQQRLEEETEEYHKSLEVERK--------RQLEIMAEAerLR---LQVSQLSEAQARAEEEAKKFKKQADKVATrlh 3423
Cdd:COG3096 889 ETL-ADRLEELREELDAAQEAQAFiqqhgkalAQLEPLVAV--LQsdpEQFEQLQADYLQAKEQQRRLKQQIFALSE--- 962
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3424 eteiatqekmtVVERLEfeRLNTSKEADDLRKAIADLENEKARLKkEAEELQNKSKEMADAQQKKIEHEKTVLQQtfmte 3503
Cdd:COG3096 963 -----------VVQRRP--HFSYEDAVGLLGENSDLNEKLRARLE-QAEEARREAREQLRQAQAQYSQYNQVLAS----- 1023
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3504 kemllkkekliedekkrLESQFEEEVKKAKALKDEqerqkqqMEQEKKTLQATMDA-ALSKQKEAEEEMLRKQKEMQELE 3582
Cdd:COG3096 1024 -----------------LKSSRDAKQQTLQELEQE-------LEELGVQADAEAEErARIRRDELHEELSQNRSRRSQLE 1079
|
970 980 990 1000
....*....|....*....|....*....|....*....|..
gi 1988774674 3583 RQRLEQERILAEENQKLREklqqledAQKDQHTRETDKVLHK 3624
Cdd:COG3096 1080 KQLTRCEAEMDSLQKRLRK-------AERDYKQEREQVVQAK 1114
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3333-3611 |
9.10e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3333 EAEMLQKQKDLAQE---QAQKLLED-KQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRlqvsQLSEAQARAEEEA 3408
Cdd:PTZ00121 1078 DFDFDAKEDNRADEateEAFGKAEEaKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR----KAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3409 KKFKKQADKvATRLHETEIATQEKMTVVER--LEFERLNTSKEADDLRKAIADLENEKARLKKE---------------A 3471
Cdd:PTZ00121 1154 VEIARKAED-ARKAEEARKAEDAKKAEAARkaEEVRKAEELRKAEDARKAEAARKAEEERKAEEarkaedakkaeavkkA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3472 EELQNKSKEMADAQQKKIEHEKTVLQQTFM---TEKEMLLKKE--------KLIEDEKKRLESQFEEEVKKAKALKDEQE 3540
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMahfARRQAAIKAEearkadelKKAEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3541 RQKQQMEQEKKTLQATMDAALSKQK---------------EAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQ 3605
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKaeeakkaaeaakaeaEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
....*.
gi 1988774674 3606 LEDAQK 3611
Cdd:PTZ00121 1393 ADEAKK 1398
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2370-2825 |
9.26e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2370 AEERKKMAEMQAEL-----DKQKQLAEAHAKAIAKAEkeaqELklkmqEEVSKREiAAVDAEKQKTNIQLELqeLKNLSE 2444
Cdd:COG3096 277 ANERRELSERALELrrelfGARRQLAEEQYRLVEMAR----EL-----EELSARE-SDLEQDYQAASDHLNL--VQTALR 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2445 QQIKDKSQQVD-EALHSRTKIEEEIRliriqlettekqkytaeselKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEetqk 2523
Cdd:COG3096 345 QQEKIERYQEDlEELTERLEEQEEVV--------------------EEAAEQLAEAEARLEAAEEEVDSLKSQLAD---- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2524 KRQAEEELKRKseaekeaAKQKQKALEDLEKLRMQAEEAERQVKQAEiekekqikvAHEAAQKSAAAELQSKHMSFAEKT 2603
Cdd:COG3096 401 YQQALDVQQTR-------AIQYQQAVQALEKARALCGLPDLTPENAE---------DYLAAFRAKEQQATEEVLELEQKL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2604 SkLEESLKQEHGAVLQLQQEAerlkkqqeDAENSREEAekelekWrQKANEALR----LRLQAEDEAHKKTlaqeEAEKQ 2679
Cdd:COG3096 465 S-VADAARRQFEKAYELVCKI--------AGEVERSQA------W-QTARELLRryrsQQALAQRLQQLRA----QLAEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2680 KEEAEREAKKRAKAEESALKQK------EMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRL 2753
Cdd:COG3096 525 EQRLRQQQNAERLLEEFCQRIGqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAW 604
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774674 2754 KNEVAAAQQQRKQLEDELAKVRSEMDILIQLktkAEKETMSNTEKS-----KQLLEAEAAKMKDLA-EEASRLRAISE 2825
Cdd:COG3096 605 LAAQDALERLREQSGEALADSQEVTAAMQQL---LEREREATVERDelaarKQALESQIERLSQPGgAEDPRLLALAE 679
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2277-2538 |
9.39e-07 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 55.39 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2277 DKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKKTKLD--------SASDNIIQEYVTLRTRYSELMTLTSQYI 2348
Cdd:pfam05262 79 DHILNLRRILAGYLMAAYGYERSDAETIAKFITIYNAVYRGDLDyfkefykeVVTKSLTKENAGLARRYDQWPGKTQIVI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2349 KF--------ITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREI 2420
Cdd:pfam05262 159 PLkknilsgnVSDVDTDSISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADF 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2421 AAVDAEKQKTNIQLELQELKNlSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTaESELKQLRDRAAEAE 2500
Cdd:pfam05262 239 AQDNADKQRDEVRQKQQEAKN-LPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAK-DHKAFDLKQESKASE 316
|
250 260 270
....*....|....*....|....*....|....*...
gi 1988774674 2501 KLRKLAQDEAEKLRKQVSEETQKKRQAEEElKRKSEAE 2538
Cdd:pfam05262 317 KEAEDKELEAQKKREPVAEDLQKTKPQVEA-QPTSLNE 353
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2391-2748 |
9.98e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 55.26 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2391 EAHAKAIAKA-EKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSeqqikDKSQQVDEALHSRTKIEEEIR 2469
Cdd:pfam02029 1 IEDEEEAARErRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG-----QGGLDEEEAFLDRTAKREERR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2470 LIRIQlETTEKQKytaESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE-----AAKQ 2544
Cdd:pfam02029 76 QKRLQ-EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQEnkwstEVRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2545 KQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKhmSFAEKTSKLEESLKQEHGAVLQLQQEA 2624
Cdd:pfam02029 152 AEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKR--GHPEVKSQNGEEEVTKLKVTTKRRQGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2625 ERLKKQQEDAENSREEAEKELEKWRQKANEALRlrlqAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEEsalkQKEMA 2704
Cdd:pfam02029 230 LSQSQEREEEAEVFLEAEQKLEELRRRRQEKES----EEFEKLRQKQQEAELELEELKKKREERRKLLEEE----EQRRK 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1988774674 2705 EEELERQRKIAESTAQQKltaeQELIRLRAdfDNAEQQRSLLED 2748
Cdd:pfam02029 302 QEEAERKLREEEEKRRMK----EEIERRRA--EAAEKRQKLPED 339
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2351-2836 |
1.02e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 55.58 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2351 ITDTQRRLDDEEKAAEKLKAEErkkMAEMQAELDKQK----QLAEAHAKAIAKAEKEAQelklkMQEEvskreIAAVDAE 2426
Cdd:PRK10246 389 LTHAEQKLNALPAITLTLTADE---VAAALAQHAEQRplrqRLVALHGQIVPQQKRLAQ-----LQVA-----IQNVTQE 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2427 KQKTNIQLELQElknlseQQIKDKSQQVDEAlhsRTKIEEEIRL-----IRIQLE---------TTEK---QKYTAeSEL 2489
Cdd:PRK10246 456 QTQRNAALNEMR------QRYKEKTQQLADV---KTICEQEARIkdleaQRAQLQagqpcplcgSTSHpavEAYQA-LEP 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2490 KQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQA 2569
Cdd:PRK10246 526 GVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQ 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2570 EiEKEKQIKvaheaaQKSAAAELQSKHMSFAEKTSKLEESLKQEHgAVLQLQQEAERLKKQQEDAENS-REEAEKELEKW 2648
Cdd:PRK10246 606 E-EHERQLR------LLSQRHELQGQIAAHNQQIIQYQQQIEQRQ-QQLLTALAGYALTLPQEDEEASwLATRQQEAQSW 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2649 RQKANEALRLRLQ-AEDEAHKKTLAQEEAEKQKEEAE-----REAKKRAKAEESALkQKEMAEEELERQRkIAESTAQ-- 2720
Cdd:PRK10246 678 QQRQNELTALQNRiQQLTPLLETLPQSDDLPHSEETValdnwRQVHEQCLSLHSQL-QTLQQQDVLEAQR-LQKAQAQfd 755
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2721 QKLTA---EQELIRLRADFDNA-----EQQRSLLEDELYRLK-------NEVAAAQQQRKQLEDELAKVRSEMDILIQLK 2785
Cdd:PRK10246 756 TALQAsvfDDQQAFLAALLDEEtltqlEQLKQNLENQRQQAQtlvtqtaQALAQHQQHRPDGLDLTVTVEQIQQELAQLA 835
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 2786 TKAEKETMSNTEKSKQLleaeaakmKDLAEEASRLRAISEEAKHQRQIAEE 2836
Cdd:PRK10246 836 QQLRENTTRQGEIRQQL--------KQDADNRQQQQALMQQIAQATQQVED 878
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2484-2720 |
1.06e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2484 TAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKrkseaekeaakQKQKALEDLEKlrmQAEEAE 2563
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-----------ALQAEIDKLQA---EIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2564 RQVKQAEIEKEKQIKVAHEAAQKSAAAE--LQSKHMS-FAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREE 2640
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYLDvlLGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2641 AEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQ 2720
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2445-2714 |
1.09e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.15 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2445 QQIKDKSQQVDEALHSRTKIEEEIRLIRIQLET--TEKQKYTAE-----SELKQLRDRAAEAEKLRKLAQDEAEKLRKQV 2517
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDElnEELKELAEKrdelnAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2518 SEETQKKRQAEEELKRKSEAEKEAA------KQKQKALEDLEKlRMQAE----EAERQV--KQAEIEKE-KQIKVAHEAA 2584
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNkaggsiDKLRKEIERLEW-RQQTEvlspEEEKELveKIKELEKElEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2585 QK-----SAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRlR 2659
Cdd:COG1340 160 EKlkelrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK-E 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2660 LQAEDEAHKKTLAQEeaekqkeeaerEAKKRAKAEESALKQKEMAEEELERQRKI 2714
Cdd:COG1340 239 LRELRKELKKLRKKQ-----------RALKREKEKEELEEKAEEIFEKLKKGEKL 282
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2849-3621 |
1.09e-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: 55.82 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2849 LKEKLAAISEATRLKTEAEIALKEKEAENERLRrqaedEAYQRKALEDQASQHKQEIEEKIV--QLKKSSEAEMERQKAI 2926
Cdd:TIGR00606 171 LKQKFDEIFSATRYIKALETLRQVRQTQGQKVQ-----EHQMELKYLKQYKEKACEIRDQITskEAQLESSREIVKSYEN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2927 VDDTLKQRRVVEEEIRilklnfekasSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLrklaleeekrRREAEEKVKK 3006
Cdd:TIGR00606 246 ELDPLKNRLKEIEHNL----------SKIMKLDNEIKALKSRKKQMEKDNSELELKMEKV----------FQGTDEQLND 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3007 IAAAEEEAARQRKAAL----EELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQK 3082
Cdd:TIGR00606 306 LYHNHQRTVREKERELvdcqRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3083 KLKEeyekakklakeaeaaKEKAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfEAAKRAQAEAAAL 3162
Cdd:TIGR00606 386 PFSE---------------RQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKK-GLGRTIELKKEIL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3163 MQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSV---LDEE--LQRLKDEVDDAVKQRGQVEEELFK 3237
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTetlKKEVksLQNEKADLDRKLRKLDQEMEQLNH 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3238 VKVQMEELLKLKNKIEEENQRLIKKDKDSTQKL--LAEEAENMRKLAEDAARLSVEAQ-----------EAARLRQIAED 3304
Cdd:TIGR00606 530 HTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELtsLLGYFPNKKQLEDWLHSKSKEINqtrdrlaklnkELASLEQNKNH 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3305 DLNQQRALAEKMLK--EKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYH-------KSLEV 3375
Cdd:TIGR00606 610 INNELESKEEQLSSyeDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqRVFQT 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3376 ERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRK 3455
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3456 AIADLENEKARLKKeAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEML------LKKEKLIEDEKKRLESQFEEEV 3529
Cdd:TIGR00606 770 QETLLGTIMPEEES-AKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLdrtvqqVNQEKQEKQHELDTVVSKIELN 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3530 KKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELER---QRLEQERILAEENQKLREKLQQL 3606
Cdd:TIGR00606 849 RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIReikDAKEQDSPLETFLEKDQQEKEEL 928
|
810
....*....|....*
gi 1988774674 3607 EDAQKDQHTRETDKV 3621
Cdd:TIGR00606 929 ISSKETSNKKAQDKV 943
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2379-2561 |
1.11e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.39 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2379 MQAELDKQKQLAEAHAKaIAKAEKEAQELklkmQEEVSKREIAAVDAEKQKTNIQLELQELknlsEQQIKDKSQQVDEAL 2458
Cdd:COG1579 2 MPEDLRALLDLQELDSE-LDRLEHRLKEL----PAELAELEDELAALEARLEAAKTELEDL----EKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2459 HSRTKIEEEIRLIRiqletTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAE 2538
Cdd:COG1579 73 ARIKKYEEQLGNVR-----NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
170 180
....*....|....*....|...
gi 1988774674 2539 KEAAKQKQKALEDLEKLRMQAEE 2561
Cdd:COG1579 148 DEELAELEAELEELEAEREELAA 170
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2486-2586 |
1.24e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 55.22 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2486 ESELKQLRDRAAEAEKLRKlaqdEAEKLRKQVSEetQKKRQAEEELKRKSEAEKEAAKQ----KQKALEDLEKLR-MQAE 2560
Cdd:PRK00409 526 EELERELEQKAEEAEALLK----EAEKLKEELEE--KKEKLQEEEDKLLEEAEKEAQQAikeaKKEADEIIKELRqLQKG 599
|
90 100
....*....|....*....|....*.
gi 1988774674 2561 EAERQVKQAEIEKEKQIKVAHEAAQK 2586
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEK 625
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2359-2604 |
1.33e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2359 DDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEevSKREIAAVDAEKQKTNIQLElqe 2438
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK--LQAEIAEAEAEIEERREELG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2439 lKNLSEQQIKDKSQQVDEALHSRTKIEEEIRliRIQLettekqkytaeseLKQLRDRAAEAEKLRKLAQDEAEKLRKQVS 2518
Cdd:COG3883 90 -ERARALYRSGGSVSYLDVLLGSESFSDFLD--RLSA-------------LSKIADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2519 EETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMS 2598
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
....*.
gi 1988774674 2599 FAEKTS 2604
Cdd:COG3883 234 AAAAAA 239
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
3462-3607 |
1.45e-06 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 53.83 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3462 NEKARLKKEAEELQNKSKEMADAQQKKIEhEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLEsqfeEEVKKAKALKDEQER 3541
Cdd:pfam02841 155 EERDKLEAKYNQVPRKGVKAEEVLQEFLQ-SKEAVEEAILQTDQALTAKEKAIEAERAKAE----AAEAEQELLREKQKE 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3542 QKQQMEQEKKTLQATMdAALSKQKEAEEEMLRKQKEMQeLERQRLEQERILAE----ENQKLREKLQQLE 3607
Cdd:pfam02841 230 EEQMMEAQERSYQEHV-KQLIEKMEAEREQLLAEQERM-LEHKLQEQEELLKEgfktEAESLQKEIQDLK 297
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3430-3603 |
1.48e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3430 QEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQ---NKSKEMADAQQKKIEHEKTvLQQTFMTEKEM 3506
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEkeiKRLELEIEEVEARIKKYEE-QLGNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3507 L-LKKEklIEDEKKRLeSQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAalsKQKEAEEEMLRKQKEMQELERQR 3585
Cdd:COG1579 92 EaLQKE--IESLKRRI-SDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAER 165
|
170
....*....|....*...
gi 1988774674 3586 LEQERILAEENQKLREKL 3603
Cdd:COG1579 166 EELAAKIPPELLALYERI 183
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2259-2907 |
1.52e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2259 KEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKK-----TKLDSASDNIIQEyvtl 2333
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKnkdkiNKLNSDLSKINSE---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2334 rtryselmtltsqyIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL---KLK 2410
Cdd:TIGR04523 112 --------------IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELeneLNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2411 MQEEVSKREIAAVDAEKQKTNIQLELQELKNLsEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELK 2490
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK-IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2491 QLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAE---EELKRKSEAE-----KEAAKQKQKALEDLEKLRMQAEEA 2562
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKseiSDLNNQKEQDwnkelKSELKNQEKKLEEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2563 ERQVKQaEIEKEKQikvaheaaqksaaaELQSKHMSFAEKTSKLEESlkqehgavlqlQQEAERLKKQQEDAENSREEAE 2642
Cdd:TIGR04523 337 ISQLNE-QISQLKK--------------ELTNSESENSEKQRELEEK-----------QNEIEKLKKENQSYKQEIKNLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2643 KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 2722
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2723 LTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMS-------- 2794
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDledelnkd 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2795 NTEKSKQLLEAEaakMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEklaaISEATRLKTEAEIALKEKE 2874
Cdd:TIGR04523 551 DFELKKENLEKE---IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE----IEEKEKKISSLEKELEKAK 623
|
650 660 670
....*....|....*....|....*....|...
gi 1988774674 2875 AENERLRRQAEDEAYQRKALEDQASQHKQEIEE 2907
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2483-2929 |
1.64e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 54.65 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2483 YTAESELKQLRDRAAEaeklrKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEA----EKEAAKQKQKALEDLEKLRMQ 2558
Cdd:pfam05667 91 YPNEPDIRKILMFLVE-----KLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAApwlpPECKPHQRRQGSRALRPFHTQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2559 A-EEAERQVKQAEIEKEkqikvaheaaqksaAAELQSKHMSFAE----KTSKLEESLKQEHGAVLQLQQEAERLKKQQED 2633
Cdd:pfam05667 166 TlVLPGRKGKTLKNSKE--------------LKEFYSEYLPPVTaqpsSRASVVPSLLERNAAELAAAQEWEEEWNSQGL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2634 AENSREEAEK--ELEKWRQKANEALRLRLQAEDEAHkktlaqeeaekqkeeaeREAKKRAKAEESALKQKEMAEEELERQ 2711
Cdd:pfam05667 232 ASRLTPEEYRkrKRTKLLKRIAEQLRSAALAGTEAT-----------------SGASRSAQDLAELLSSFSGSSTTDTGL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2712 RKIAESTAQQKLTAEQELIRLRADFDNAEQQrslLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILI----QLKTK 2787
Cdd:pfam05667 295 TKGSRFTHTEKLQFTNEAPAATSSPPTKVET---EEELQQQREEELEELQEQLEDLESSIQELEKEIKKLEssikQVEEE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2788 AEKETMSNTEKSKQ----------LLEAEA--AKMKDLAEEAS-RLRAISEE-AKHQRQIAEE------EAARQRAEAER 2847
Cdd:pfam05667 372 LEELKEQNEELEKQykvkkktldlLPDAEEniAKLQALVDASAqRLVELAGQwEKHRVPLIEEyralkeAKSNKEDESQR 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2848 I------LKEKLAAISEATRLKTEaeiALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIE-EKIVQLKKSSEAEM 2920
Cdd:pfam05667 452 KleeikeLREKIKEVAEEAKQKEE---LYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEiTKILSDTKSLQKEI 528
|
490
....*....|....*.
gi 1988774674 2921 -------ERQKAIVDD 2929
Cdd:pfam05667 529 nsltgklDRTFTVTDE 544
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2436-2846 |
1.87e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 54.31 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2436 LQELKNLSEQQIK---DKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEK 2512
Cdd:pfam05622 26 LQEEKNSLQQENKklqERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2513 LRKQVSEETQKK------RQAEEELKrKSEAEKEAAKQKqkaLEDLEKLRMQA---EEAERQVKQAEIEKEKQIKVA--- 2580
Cdd:pfam05622 106 LTSLAEEAQALKdemdilRESSDKVK-KLEATVETYKKK---LEDLGDLRRQVkllEERNAEYMQRTLQLEEELKKAnal 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2581 --HEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQedaENSREeaekelekwrqkANEALRL 2658
Cdd:pfam05622 182 rgQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIER---DTLRE------------TNEELRC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2659 RLQAEDEAHKKTLAQEEAEKQKEEAEREakkrakaeesaLKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDN 2738
Cdd:pfam05622 247 AQLQQAELSQADALLSPSSDPGDNLAAE-----------IMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLED 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2739 AEQQRSLLEDELyRLKNE-VAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEketmsntEKSKQLLEAEAAKMKdlAEEA 2817
Cdd:pfam05622 316 ANRRKNELETQN-RLANQrILELQQQVEELQKALQEQGSKAEDSSLLKQKLE-------EHLEKLHEAQSELQK--KKEQ 385
|
410 420
....*....|....*....|....*....
gi 1988774674 2818 SRLRAISEEAKHQRQIAEEEAARQRAEAE 2846
Cdd:pfam05622 386 IEELEPKQDSNLAQKIDELQEALRKKDED 414
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2707-2851 |
1.88e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.62 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2707 ELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRS---------E 2777
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyealqkE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 2778 MDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKE 2851
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3018-3484 |
1.91e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3018 RKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSvLAQQIEDSITQKKLKEEYEKAKKLAKE 3097
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3098 AEAAKEKAEReaalLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfeaakraqaeaaalmqkqqadtemAKHKK 3177
Cdd:COG4717 127 LLPLYQELEA----LEAELAELPERLEELEERLEELRELEEELEELEAELA------------------------ELQEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3178 LAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELfkvkvqmeELLKLKNKIEEENQ 3257
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL--------EAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3258 RLI------------KKDKDSTQK----------LLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRA---- 3311
Cdd:COG4717 251 LLLiaaallallglgGSLLSLILTiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalgl 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3312 ---LAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKlledKQLMQQRLEEETEEYHKSLEVERKRQlEIMAEAE 3388
Cdd:COG4717 331 ppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI----AALLAEAGVEDEEELRAALEQAEEYQ-ELKEELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3389 RLRLQVSQLSEAQARAEEEAKKfkkqaDKVATRLHETEIAtqekmtvVERLEFERLNTSKEADDLRKAIADLENEK--AR 3466
Cdd:COG4717 406 ELEEQLEELLGELEELLEALDE-----EELEEELEELEEE-------LEELEEELEELREELAELEAELEQLEEDGelAE 473
|
490
....*....|....*...
gi 1988774674 3467 LKKEAEELQNKSKEMADA 3484
Cdd:COG4717 474 LLQELEELKAELRELAEE 491
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2132-2306 |
2.06e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 52.06 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2132 VPSDVKEVETYRAKLKKMRTEAEDEQPVFDSLEEElkkasavSDKMVRVHSERDVELdhfRQQLSSLQDRWKAVFTQIDL 2211
Cdd:cd00176 28 YGDDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHPDAEEI---QERLEELNQRWEELRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2212 RQRELEQLGRQLGYYRESYDwLIRWIADAKQRQEKIQavPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYID 2291
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLE 174
|
170
....*....|....*
gi 1988774674 2292 TIKDYELQLVAYKAQ 2306
Cdd:cd00176 175 EGHPDADEEIEEKLE 189
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3299-3607 |
2.13e-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: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3299 RQIAEDDLNQQRALAEKMLKEKMQAIQEasRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERK 3378
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEE--EEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3379 RQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKvatrlheteiatQEKMTVVERLEFERLNTSKEADdlrkaia 3458
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE------------EEREEDERILEYLKEKAEREEE------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3459 dLENEKARLKKEAEELQNKskemADAQQKKIEHEKTvlqqtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDE 3538
Cdd:pfam13868 171 -REAEREEIEEEKEREIAR----LRAQQEKAQDEKA--------ERDELRAKLYQEEQERKERQKEREEAEKKARQRQEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3539 QERQKQQMEQEKKTLQATMDaalsKQKEAEEEMLRKQKEMQELERQRLEQERI-----------LAEENQKLREKLQQLE 3607
Cdd:pfam13868 238 QQAREEQIELKERRLAEEAE----REEEEFERMLRKQAEDEEIEQEEAEKRRMkrlehrrelekQIEEREEQRAAEREEE 313
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
1177-1272 |
2.21e-06 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 50.38 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1177 KLLL-WSQRMTDGYqGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTNL-----------------------EN 1232
Cdd:cd21224 3 SLLLkWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 1233 LEQAFSVAEK-----------DLG-VTRLLDPEDVDVPHPDEKSIITYVSSL 1272
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3479-3611 |
2.25e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.01 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3479 KEMADAQQKKIEHE-KTVLQQTfmtEKEM-LLKKEKLIE--DEKKRLESQFEEEVKKAKalkDEQERQKQQMEQEKKTLQ 3554
Cdd:PRK12704 26 KKIAEAKIKEAEEEaKRILEEA---KKEAeAIKKEALLEakEEIHKLRNEFEKELRERR---NELQKLEKRLLQKEENLD 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774674 3555 ATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLrEKLQQL--EDAQK 3611
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLtaEEAKE 157
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4932-4968 |
2.27e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 2.27e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1988774674 4932 RYLQGTGCIAGVFLESTKERLSIYQAMKKNMIRPGTA 4968
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2699-2986 |
2.31e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.75 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2699 KQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEM 2778
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2779 DILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKH-QRQIAEEEAARQR---AEAERILKEKLA 2854
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESlQEELAALEQELQAlseAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2855 AISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQR 2934
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 2935 RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKL 2986
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2372-3586 |
2.32e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 54.67 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2372 ERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELK---LKMQEEVSK--REIAAVDAEKQKTN-IQLELQE-LKNLSe 2444
Cdd:TIGR01612 535 KAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENedsIHLEKEIKDlfDKYLEIDDEIIYINkLKLELKEkIKNIS- 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2445 qqikDKSQQVDEALHSRTKIEEEIRLIRiqlETTEKQKYTAESELKQlRDRAAEAEK--LRKLAQDEAEKLRKQVSEETQ 2522
Cdd:TIGR01612 614 ----DKNEYIKKAIDLKKIIENNNAYID---ELAKISPYQVPEHLKN-KDKIYSTIKseLSKIYEDDIDALYNELSSIVK 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2523 KKRQAEEELKRKseaekeaakqkqkaLEDLeklrmqaeeaerqvkQAEIEKE-KQIKVAHEAAQKSAAAELQSKHmsfAE 2601
Cdd:TIGR01612 686 ENAIDNTEDKAK--------------LDDL---------------KSKIDKEyDKIQNMETATVELHLSNIENKK---NE 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2602 KTSKLEESLKQEHGAVL-QLQQEAERLKKQQEDAENSREEAEK---ELEKWRQKANEalrLRLQAEDEAHKKTLAQEEAE 2677
Cdd:TIGR01612 734 LLDIIVEIKKHIHGEINkDLNKILEDFKNKEKELSNKINDYAKekdELNKYKSKISE---IKNHYNDQINIDNIKDEDAK 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2678 KQKEEAEREAKKRAKAEESALK----QKEMAEEELERQRKIA--ESTAQQKLTAEQELI-----RLRADFdnAEQQRSLL 2746
Cdd:TIGR01612 811 QNYDKSKEYIKTISIKEDEIFKiineMKFMKDDFLNKVDKFInfENNCKEKIDSEHEQFaeltnKIKAEI--SDDKLNDY 888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2747 EDEL---YRLKNEVAAAQQQRKQLEDELAKVRSEMDIliqlkTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLrai 2823
Cdd:TIGR01612 889 EKKFndsKSLINEINKSIEEEYQNINTLKKVDEYIKI-----CENTKESIEKFHNKQNILKEILNKNIDTIKESNLI--- 960
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2824 seEAKHQRQIaEEEAARQRAEAERILKEklAAISEATRLKTEAeiaLKEKEAENERLRRQAEDEAYQRKaleDQASQHKQ 2903
Cdd:TIGR01612 961 --EKSYKDKF-DNTLIDKINELDKAFKD--ASLNDYEAKNNEL---IKYFNDLKANLGKNKENMLYHQF---DEKEKATN 1029
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2904 EIEEKIVQLKKS-SEAEMERQKAIVDDTLKQRRVVEEEIRILKLN-FEKASSGKLDLELELNKLK--NIADETQQSKIRA 2979
Cdd:TIGR01612 1030 DIEQKIEDANKNiPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEiLEEAEINITNFNEIKEKLKhyNFDDFGKEENIKY 1109
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2980 EEEaeklrklaleeekrrreaeekVKKIAAAEEEAARQRKAALEELERLRKKAE----EARKQKDEADKEAEKQIvvaqq 3055
Cdd:TIGR01612 1110 ADE---------------------INKIKDDIKNLDQKIDHHIKALEEIKKKSEnyidEIKAQINDLEDVADKAI----- 1163
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3056 AAQKCSAAEQQVQSVLAQ-----QIEDSItQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEA 3130
Cdd:TIGR01612 1164 SNDDPEEIEKKIENIVTKidkkkNIYDEI-KKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMI 1242
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3131 ANQAKAQEDAERLRKEAEfeaaKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQ--ELTKVKLKLDETDKQKS 3208
Cdd:TIGR01612 1243 KAMEAYIEDLDEIKEKSP----EIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENisDIREKSLKIIEDFSEES 1318
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3209 VLDEELQRLKDEVDDAVKQRGQVEE------------ELFKVKVQMEELLKLKNKIEEENQRlIKKDKDSTQKLLAEEAE 3276
Cdd:TIGR01612 1319 DINDIKKELQKNLLDAQKHNSDINLylneianiynilKLNKIKKIIDEVKEYTKEIEENNKN-IKDELDKSEKLIKKIKD 1397
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3277 N----------------------MRKLAEDAAR-LSVEAQEAARLRQIAEDDLNQQRALAE-KMLKEKMQAIQEASR--- 3329
Cdd:TIGR01612 1398 DinleeckskiestlddkdidecIKKIKELKNHiLSEESNIDTYFKNADENNENVLLLFKNiEMADNKSQHILKIKKdna 1477
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3330 ----------LKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLE--------IMAEAERLR 3391
Cdd:TIGR01612 1478 tndhdfnineLKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAktkkdseiIIKEIKDAH 1557
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3392 LQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSkeadDLRKAIADLENEKARLKKEA 3471
Cdd:TIGR01612 1558 KKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKIS----DIKKKINDCLKETESIEKKI 1633
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3472 EELQnkskemADAQQKKIEHEKTVLQ--QTFMtekEMLLKKEKLIEDEKKRLESqfeeevkkakaLKDEQERQKQQMEQE 3549
Cdd:TIGR01612 1634 SSFS------IDSQDTELKENGDNLNslQEFL---ESLKDQKKNIEDKKKELDE-----------LDSEIEKIEIDVDQH 1693
|
1290 1300 1310
....*....|....*....|....*....|....*..
gi 1988774674 3550 KKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRL 3586
Cdd:TIGR01612 1694 KKNYEIGIIEKIKEIAIANKEEIESIKELIEPTIENL 1730
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2686-2942 |
2.57e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 53.31 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2686 EAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRadfdnaeQQRSLLEDELYRLKNEVAAAQQQRK 2765
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQK-------ELEQRAAAEKAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2766 QLEDELAKVRSEMDILIQLKTKAEKETMSNTEKskqllEAEAAKMKDLAEEASRlraiseEAKHQRQIAEEEAaRQRAEA 2845
Cdd:TIGR02794 118 QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK-----QAEEEAKAKAAAEAKK------KAEEAKKKAEAEA-KAKAEA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2846 ERILK-EKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQK 2924
Cdd:TIGR02794 186 EAKAKaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYA 265
|
250
....*....|....*...
gi 1988774674 2925 AIVDDTLKQRRVVEEEIR 2942
Cdd:TIGR02794 266 AIIQQAIQQNLYDDPSFR 283
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2355-2612 |
2.70e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.18 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2355 QRRLDDEekaaeKLKAEERKKMAEmqAELDKQKQLAEAHAKAIAKAEKEAQElklkmqeevskREIAAVDAEKQKTNIQL 2434
Cdd:PRK05035 459 QARLERE-----KAAREARHKKAA--EARAAKDKDAVAAALARVKAKKAAAT-----------QPIVIKAGARPDNSAVI 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2435 ELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRliRIQLETTEKQKYTAESELKQLRDRAAEAEklrKLAQDEAEKLR 2514
Cdd:PRK05035 521 AAREARKAQARARQAEKQAAAAADPKKAAVAAAIA--RAKAKKAAQQAANAEAEEEVDPKKAAVAA---AIARAKAKKAA 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2515 KQVSEETQKKRQAEEELKrKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVK-QAEIEKEKQIKVAHEAAQKSAAAELQ 2593
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPK-KAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAvAAAIARAKARKAAQQQANAEPEEAED 674
|
250
....*....|....*....
gi 1988774674 2594 SKHMSFAEKTSKLEESLKQ 2612
Cdd:PRK05035 675 PKKAAVAAAIARAKAKKAA 693
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2138-3048 |
2.70e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 54.67 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2138 EVETYRAKLKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRW-KAVFTQIDLRQREL 2216
Cdd:TIGR01612 780 ELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFlNKVDKFINFENNCK 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2217 EQLGRQlgyyRESYDWLIRWI-ADAKQRQEKIQAVPITDSKTLkeqLAQEKKLLEEIEQNKD---KVDECQKYAKAYIDT 2292
Cdd:TIGR01612 860 EKIDSE----HEQFAELTNKIkAEISDDKLNDYEKKFNDSKSL---INEINKSIEEEYQNINtlkKVDEYIKICENTKES 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2293 IKDYELQLVAYKAQVEPLVSPLKKTkldsasdNIIQEyvtlrtryselmTLTSQYIKFITDTQRRLDDEEKAAEkLKAEE 2372
Cdd:TIGR01612 933 IEKFHNKQNILKEILNKNIDTIKES-------NLIEK------------SYKDKFDNTLIDKINELDKAFKDAS-LNDYE 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2373 RKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAqelklkmQEEVSKREIAAVDAEKQKTNIQLELQ-ELKNLSEQQIKDKS 2451
Cdd:TIGR01612 993 AKNNELIKYFNDLKANLGKNKENMLYHQFDEK-------EKATNDIEQKIEDANKNIPNIEIAIHtSIYNIIDEIEKEIG 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2452 QQVdEALHSRTKIEEEIRLIRIQlETTEKQKYTAESELKQlRDRAAEAEKLRKLAQDeaeklRKQVSEETQKKRQAEEEL 2531
Cdd:TIGR01612 1066 KNI-ELLNKEILEEAEINITNFN-EIKEKLKHYNFDDFGK-EENIKYADEINKIKDD-----IKNLDQKIDHHIKALEEI 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2532 KRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAE-----IEKEKQI-----KVAHEAAQ----KSAAAELQSKHM 2597
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIEnivtkIDKKKNIydeikKLLNEIAEiekdKTSLEEVKGINL 1217
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2598 SFAEKTSKL------EESLKQEH--GAVLQLQQEAERLKKQQEDAENsreeaEKELEKWRQKANEALRLRlQAEDEAHKK 2669
Cdd:TIGR01612 1218 SYGKNLGKLflekidEEKKKSEHmiKAMEAYIEDLDEIKEKSPEIEN-----EMGIEMDIKAEMETFNIS-HDDDKDHHI 1291
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2670 TLAQEEAEKQKEEAEREAKKRAKAEESALK--QKEMAEEELERQRKIAE-STAQQKLTAEQELIRL---RADFDNAEQQR 2743
Cdd:TIGR01612 1292 ISKKHDENISDIREKSLKIIEDFSEESDINdiKKELQKNLLDAQKHNSDiNLYLNEIANIYNILKLnkiKKIIDEVKEYT 1371
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2744 SLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKM-------KDLAEE 2816
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIdtyfknaDENNEN 1451
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2817 ASRLRAISEEAKHQRQ-IAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEaENERLRRQAEDEA------Y 2889
Cdd:TIGR01612 1452 VLLLFKNIEMADNKSQhILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIE-KNKELFEQYKKDVtellnkY 1530
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2890 QRKALEDQASQHKQEIEEKIVQLKKSS-----EAEMERQKaiVDDTLKQRRVVEEEIRilklNFEKASSGKLDLELEL-- 2962
Cdd:TIGR01612 1531 SALAIKNKFAKTKKDSEIIIKEIKDAHkkfilEAEKSEQK--IKEIKKEKFRIEDDAA----KNDKSNKAAIDIQLSLen 1604
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2963 --NKLKNIAD-ETQQSKIRAEEEA--EKLRKLALEEEKRRreaeekvkkiAAAEEEAARQRKAALEELERLRKKAEEARK 3037
Cdd:TIGR01612 1605 feNKFLKISDiKKKINDCLKETESieKKISSFSIDSQDTE----------LKENGDNLNSLQEFLESLKDQKKNIEDKKK 1674
|
970
....*....|.
gi 1988774674 3038 QKDEADKEAEK 3048
Cdd:TIGR01612 1675 ELDELDSEIEK 1685
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1633-1725 |
2.80e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 48.87 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1633 HAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMTAKKDNYSGLMRELELREKKVNDIQALGDRLVRDGHPGKKTVESFTA 1712
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1988774674 1713 ALQTQWSWILQLC 1725
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2737-2985 |
2.83e-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: 53.31 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2737 DNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLE-AEAAKMKDLAE 2815
Cdd:TIGR02794 29 PEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQrAAAEKAAKQAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2816 EASRL-RAISEEAKHQRQIAEEEAARQR-AEAERILKEKLAAISEATRLKTEAEIALKEKEAEnerlRRQAEDEAyqrKA 2893
Cdd:TIGR02794 109 QAAKQaEEKQKQAEEAKAKQAAEAKAKAeAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEA----KKKAEAEA---KA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2894 ledqasqhKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvvEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQ 2973
Cdd:TIGR02794 182 --------KAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEA--EAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGG 251
|
250
....*....|..
gi 1988774674 2974 QSKIRAEEEAEK 2985
Cdd:TIGR02794 252 ARGAAAGSEVDK 263
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2137-2665 |
2.92e-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: 54.03 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2137 KEVETYRAKLKKMRTEAEDEQPVFDSLEEELKKA--------------SAVSDKM----VRVHSERD---VELDHFRQQL 2195
Cdd:pfam01576 517 RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLqrelealtqqleekAAAYDKLektkNRLQQELDdllVDLDHQRQLV 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2196 SSLQDRWKAvFTQIDLRQRELEqlgrqlGYYRESYDwliRWIADAKQRQEKIQAvpitdsktlkeqLAQEkklLEEIEQN 2275
Cdd:pfam01576 597 SNLEKKQKK-FDQMLAEEKAIS------ARYAEERD---RAEAEAREKETRALS------------LARA---LEEALEA 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2276 KDKVDECQKYAKAYIDtikdyelQLVAYKAQVEPLVSPLKKTKldSASDNIIQEyvtLRTRYSElmtltsqyikfitdtq 2355
Cdd:pfam01576 652 KEELERTNKQLRAEME-------DLVSSKDDVGKNVHELERSK--RALEQQVEE---MKTQLEE---------------- 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2356 rrLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKA-EKEAQELKLKMQEEVSKREIAAvdAEKQKtnIQL 2434
Cdd:pfam01576 704 --LEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQlVKQVRELEAELEDERKQRAQAV--AAKKK--LEL 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2435 ELQELknlsEQQIKDKSQQVDEALHSRTKIE----------EEIRLIR----IQLETTEKQKYTAESELKQLRDRAAEAE 2500
Cdd:pfam01576 778 DLKEL----EAQIDAANKGREEAVKQLKKLQaqmkdlqrelEEARASRdeilAQSKESEKKLKNLEAELLQLQEDLAASE 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2501 KLRKLAQDEAEKLRKQVSEETQKKRQAEEElKRKSEAEkeaAKQKQKALEDLE-KLRMQAEEAERQVKQAE-IEKEKQIK 2578
Cdd:pfam01576 854 RARRQAQQERDELADEIASGASGKSALQDE-KRRLEAR---IAQLEEELEEEQsNTELLNDRLRKSTLQVEqLTTELAAE 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2579 VAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEH-GAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALr 2657
Cdd:pfam01576 930 RSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFkSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVL- 1008
|
....*...
gi 1988774674 2658 lrLQAEDE 2665
Cdd:pfam01576 1009 --LQVEDE 1014
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2461-2989 |
3.08e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.14 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2461 RTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKlAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE 2540
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKS-SNLELENIKKQIADDEKSHSITLKEIERLSIEYNN 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2541 AAKQKQKALEDLEKLRMQAEEAERqvkqaeiekekqikvaHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQL 2620
Cdd:PRK01156 230 AMDDYNNLKSALNELSSLEDMKNR----------------YESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2621 QQEAERLKKQQEDAENSREEAEKelekwrqkaneaLRLRLQAEDEAHKKtLAQEEAEKQKEEAEREAKKRAKAEESALKQ 2700
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSN------------IDAEINKYHAIIKK-LSVLQKDYNDYIKKKSRYDDLNNQILELEG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2701 KEMAEEELER-----QRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLED---ELYRLKNEVAAAQQQRKQLEDELA 2772
Cdd:PRK01156 361 YEMDYNSYLKsieslKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEinvKLQDISSKVSSLNQRIRALRENLD 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2773 KVRSEMDILIQLKTKAEKETMSNTEKSKQLLEaeaakmkDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEK 2852
Cdd:PRK01156 441 ELSRNMEMLNGQSVCPVCGTTLGEEKSNHIIN-------HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2853 LAAISEATRLKTEAE-----IALKEKEAENERLRRQAEDEAYQRKALEDQASQHkqeiEEKIVQLKKSSEAEMERQKAIV 2927
Cdd:PRK01156 514 INKSINEYNKIESARadledIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKR----TSWLNALAVISLIDIETNRSRS 589
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774674 2928 DDTLKQRRVVEEEIRILKLNFEKASS----GKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKL 2989
Cdd:PRK01156 590 NEIKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNY 655
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2623-3056 |
3.12e-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: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2623 EAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQK- 2701
Cdd:NF033838 56 QKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTl 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2702 EMAEEELERQRKIAEstAQQKLTAEQElirlradfdnaEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVrsemdil 2781
Cdd:NF033838 136 EPGKKVAEATKKVEE--AEKKAKDQKE-----------EDRRNYPTNTYKTLELEIAESDVEVKKAELELVKE------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2782 iqlktkaEKETMSNTEKSKQlleaEAAKMKDLAEEASRLraisEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATR 2861
Cdd:NF033838 196 -------EAKEPRDEEKIKQ----AKAKVESKKAEATRL----EKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2862 LKTEAEIALKEKEAENERLRRQAE--DEAYQRKALEDQASQHKQ---EIEEKIVQLKKSSEAEMERQKaivddtlkqRRV 2936
Cdd:NF033838 261 PKRRAKRGVLGEPATPDKKENDAKssDSSVGEETLPSPSLKPEKkvaEAEKKVEEAKKKAKDQKEEDR---------RNY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2937 VEEEIRILKLNFEKASSGKLDLELELNK--LKNIADETQQSKIRAEEEAEKlrklaleeekrrreaeekvkkiaaaeeea 3014
Cdd:NF033838 332 PTNTYKTLELEIAESDVKVKEAELELVKeeAKEPRNEEKIKQAKAKVESKK----------------------------- 382
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1988774674 3015 arQRKAALEELERLRKKAEEARKQK-DEADKEAEKQIVVAQQA 3056
Cdd:NF033838 383 --AEATRLEKIKTDRKKAEEEAKRKaAEEDKVKEKPAEQPQPA 423
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2474-2900 |
3.12e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 53.76 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2474 QLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLE 2553
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2554 KLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQED 2633
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2634 AENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRK 2713
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2714 IAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDElyrlknevAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETM 2793
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAE--------AVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEAL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2794 SNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEK 2873
Cdd:COG5278 423 ELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLA 502
|
410 420
....*....|....*....|....*..
gi 1988774674 2874 EAENERLRRQAEDEAYQRKALEDQASQ 2900
Cdd:COG5278 503 LALAALLLAAAEAALAAALAAALASAE 529
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
3436-3606 |
3.29e-06 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 53.68 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3436 VERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKsKEMADAQQKKIEHEKTVLQQTFMTEKEmllKKEKLIE 3515
Cdd:pfam15066 372 VEELIEDKYNVILEKNDINKTLQNLQEILANTQKHLQESRKE-KETLQLELKKIKVNYVHLQERYITEMQ---QKNKSVS 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3516 D--EKKRLESQFEEEVKKAKALKDEQERqkqqmeqekktlqATMDA--ALSKQKEA-EEEMLRKQKEMQELERQRLeqer 3590
Cdd:pfam15066 448 QclEMDKTLSKKEEEVERLQQLKGELEK-------------ATTSAldLLKREKETrEQEFLSLQEEFQKHEKENL---- 510
|
170
....*....|....*.
gi 1988774674 3591 ilaEENQKLREKLQQL 3606
Cdd:pfam15066 511 ---EERQKLKSRLEKL 523
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3248-3610 |
3.38e-06 |
|
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: 53.82 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3248 LKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEdaARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEA 3327
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLH--GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3328 SRLKAEAEMLQKQKDLAQEQAQKlleDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSeaqaraeee 3407
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKK---QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVT--------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3408 akKFKKQADKVATRLheteiatQEKMTVVERLEFERLNTSKEADDL---RKAIADLENEKARLKKEAEElQNKSKEMADA 3484
Cdd:TIGR00618 304 --QIEQQAQRIHTEL-------QSKMRSRAKLLMKRAAHVKQQSSIeeqRRLLQTLHSQEIHIRDAHEV-ATSIREISCQ 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3485 QQKKIEHEKTVLQQtfmteKEMLLKKEKLIedekKRLESQFEEEVKKAKALKDEQERQKQQMeqekktlqatmdAALSKQ 3564
Cdd:TIGR00618 374 QHTLTQHIHTLQQQ-----KTTLTQKLQSL----CKELDILQREQATIDTRTSAFRDLQGQL------------AHAKKQ 432
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1988774674 3565 KEAEEEMLRKQKEMQELERQRLEQERILAEE-NQKLREKLQQLEDAQ 3610
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIHLQEsAQSLKEREQQLQTKE 479
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3448-3607 |
3.41e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3448 KEADDLRKAIADLENEKARLKKEAEELQNKSKEmADAQQKKIEHEktvlqqtfmtekemLLKKEKLIEDEKKRLESqfee 3527
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELE--------------IEEVEARIKKYEEQLGN---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3528 eVKKAKALK------DEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLRE 3601
Cdd:COG1579 85 -VRNNKEYEalqkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*.
gi 1988774674 3602 KLQQLE 3607
Cdd:COG1579 164 EREELA 169
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2146-2652 |
3.44e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2146 LKKMRTEAEDEQPVFDSLEEELKKASAVSDKMVRVHSERDVELDHFRQQLSSLQDRWKAVFTQIDLRQRELEQlgrqlgy 2225
Cdd:TIGR04523 234 IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2226 yresyDWlirwiadakqrqekiqavpitdSKTLKEQLAQEKKLLEEIEqnkDKVDECQKYAKAYIDTIKDyelqlvayka 2305
Cdd:TIGR04523 307 -----DW----------------------NKELKSELKNQEKKLEEIQ---NQISQNNKIISQLNEQISQ---------- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2306 qveplvspLKKTKLDSASDNiiqeyvtlRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKkmaemqaeLDK 2385
Cdd:TIGR04523 347 --------LKKELTNSESEN--------SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK--------IQN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2386 QKQLAEAHAKAIAKAEKEAQEL-----KLKMQEEVSKREIAavDAEKQKTNIQLELQELKNLSEQQikdkSQQVDEalhs 2460
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLekeieRLKETIIKNNSEIK--DLTNQDSVKELIIKNLDNTRESL----ETQLKV---- 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2461 rtkIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKlrklaqdEAEKLRKQVSEETQKKRQAEEElkrKSEAEKE 2540
Cdd:TIGR04523 473 ---LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE-------KVKDLTKKISSLKEKIEKLESE---KKEKESK 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2541 AAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQehgaVLQL 2620
Cdd:TIGR04523 540 ISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK----ISSL 615
|
490 500 510
....*....|....*....|....*....|..
gi 1988774674 2621 QQEAERLKKQQEDAENSREEAEKELEKWRQKA 2652
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3209-3480 |
3.45e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3209 VLDEelQRLKDEVDDAVKQRGQ---VEEELFKVKVQMEELLKlknkIEEENQRLikkdkdstqkllAEEAENMRKLAEDA 3285
Cdd:COG4913 217 MLEE--PDTFEAADALVEHFDDlerAHEALEDAREQIELLEP----IRELAERY------------AAARERLAELEYLR 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3286 ARLSV-EAQEAARLRQIAEDDLNQQRALAEKmlkEKMQAIQEASRLKAEAEMLQKQKDLAQ----EQAQKLLEDKQLMQQ 3360
Cdd:COG4913 279 AALRLwFAQRRLELLEAELEELRAELARLEA---ELERLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3361 RLEEETEEYHKSLeveRKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLE 3440
Cdd:COG4913 356 ERERRRARLEALL---AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1988774674 3441 FERLNTSKEADDLRKAIAD-LENEKARLKKEAEELQNKSKE 3480
Cdd:COG4913 433 RRKSNIPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4733-4767 |
3.49e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.71 E-value: 3.49e-06
10 20 30
....*....|....*....|....*....|....*
gi 1988774674 4733 LLEAQAATGFIVDPLKNETLTVDEAVRKGVVGPEI 4767
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2871-3309 |
3.57e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.59 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2871 KEKEAENERLRRQAEDEAyqrkaledqasqHKQEIEEKIVQLKKSSEAEMERQKAIVDDtlkQRRVVEEEIRilklnfek 2950
Cdd:pfam17380 292 KFEKMEQERLRQEKEEKA------------REVERRRKLEEAEKARQAEMDRQAAIYAE---QERMAMERER-------- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2951 assgkldlelELNKLKNIADETQQSKIRAEE---EAEKLRKLaleeekrrreaeekvkkiaaAEEEAARQRKAaleelER 3027
Cdd:pfam17380 349 ----------ELERIRQEERKRELERIRQEEiamEISRMREL--------------------ERLQMERQQKN-----ER 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3028 LRKKAEEARKQKDEadkEAEKQIVVAQQAAQKCSAAEQQVQsvlAQQIEdsitQKKLKEEyekakklakeaeaakekaeR 3107
Cdd:pfam17380 394 VRQELEAARKVKIL---EEERQRKIQQQKVEMEQIRAEQEE---ARQRE----VRRLEEE-------------------R 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3108 EAALLRQQAEEAERQKtaaeeeaANQAKAQEDAERLRKEAEfeaakraqaeaaalMQKQQADtemakhKKLAEQtlKQKF 3187
Cdd:pfam17380 445 AREMERVRLEEQERQQ-------QVERLRQQEEERKRKKLE--------------LEKEKRD------RKRAEE--QRRK 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3188 QVEQELTKVKLKLDETDKQKSVLDEElqrlkdevddavkqrgqveeelfkvkvqMEEllkLKNKIEEENQRLIKKDKDST 3267
Cdd:pfam17380 496 ILEKELEERKQAMIEEERKRKLLEKE----------------------------MEE---RQKAIYEEERRREAEEERRK 544
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1988774674 3268 QKLLAEE---AENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQ 3309
Cdd:pfam17380 545 QQEMEERrriQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2486-2725 |
3.63e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 53.06 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2486 ESELKQLRDRAAEAEKlrKLAQDE-AEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQK--QKALEDLEKLRMQAEEA 2562
Cdd:PRK07735 4 EKDLEDLKKEAARRAK--EEARKRlVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRaaAAAKAKAAALAKQKREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2563 ERQVKQAEIEKEKqiKVAHEAAQKSAAAELQSKHMSFAEKTSklEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAE 2642
Cdd:PRK07735 82 TEEVTEEEKAKAK--AKAAAAAKAKAAALAKQKREGTEEVTE--EEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2643 KELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKK-----RAKAEESAL-KQKEM-----AEEELERQ 2711
Cdd:PRK07735 158 EETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKakaaaAAKAKAAALaKQKASqgngdSGDEDAKA 237
|
250
....*....|....
gi 1988774674 2712 RKIAESTAQQKLTA 2725
Cdd:PRK07735 238 KAIAAAKAKAAAAA 251
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2398-2669 |
3.64e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 53.16 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2398 AKAEKEAQELKlKMQEEVSKREIAAVDAEKQKTNIQLELQElknlSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLET 2477
Cdd:PRK11637 40 AHASDNRDQLK-SIQQDIAAKEKSVRQQQQQRASLLAQLKK----QEEAISQASRKLRETQNTLNQLNKQIDELNASIAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2478 TEKQKYTAESELKQLRDRAaeaeklrkLAQDEAEKLRKQVS-EETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLR 2556
Cdd:PRK11637 115 LEQQQAAQERLLAAQLDAA--------FRQGEHTGLQLILSgEESQRGERILAYFGYLNQARQETIAELKQTREELAAQK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2557 MQAEEAERQVKQAEIEKEKQ---IKVAHEAAQKSAAAelqskhmsfaektskLEESLKQEHGAVLQLQQEAERLKKQQED 2633
Cdd:PRK11637 187 AELEEKQSQQKTLLYEQQAQqqkLEQARNERKKTLTG---------------LESSLQKDQQQLSELRANESRLRDSIAR 251
|
250 260 270
....*....|....*....|....*....|....*..
gi 1988774674 2634 AE-NSREEAEKElekwrqkANEALRLRlQAEDEAHKK 2669
Cdd:PRK11637 252 AErEAKARAERE-------AREAARVR-DKQKQAKRK 280
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2690-2865 |
3.86e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2690 RAKAEESALKQKEMAEEELERQRKIAESTAQQKLT-AEQELIRLRADFDNAEQQRsllEDELYRLKNEVaaaQQQRKQLE 2768
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRER---RNELQKLEKRL---LQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2769 DELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDL-------AEEASR--LRAISEEAKHQRQI----AE 2835
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisgltAEEAKEilLEKVEEEARHEAAVlikeIE 179
|
170 180 190
....*....|....*....|....*....|.
gi 1988774674 2836 EEAarqRAEAERILKEKLA-AIseaTRLKTE 2865
Cdd:PRK12704 180 EEA---KEEADKKAKEILAqAI---QRCAAD 204
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
1055-1154 |
3.86e-06 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 49.19 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1055 DRVQKKTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGETLPREKG--RMRFHKLQNVQIALDFLRHRQVK 1130
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 1988774674 1131 LVNIRNDDIADGNPKLTLGLIWTI 1154
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2498-2855 |
4.02e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.42 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2498 EAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQI 2577
Cdd:pfam15709 164 TPASISHAERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERNL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2578 KVAHEAAQK----SAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQ---------EDAENSREEAEKE 2644
Cdd:pfam15709 244 EVAAELSGPdvinSKETEDASERGAFSSDSVVEDPWLSSKYDAEESQVSIDGRSSPTQtfvvtgnmeSEEERSEEDPSKA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2645 LEKWRQKANEAlRLRLQAEdEAHKKTLAQeeaekqkeeaerEAKKRAKAEESALKQkemaeEELERQRKIAESTAQQKLT 2724
Cdd:pfam15709 324 LLEKREQEKAS-RDRLRAE-RAEMRRLEV------------ERKRREQEEQRRLQQ-----EQLERAEKMREELELEQQR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2725 AEQElIRLRADFDNAEQQRSllEDELYRLKNEVAAAQQQRKQLEDELAKVrsemdiLIQLKTKAEKETMSNTEKSKQLLE 2804
Cdd:pfam15709 385 RFEE-IRLRKQRLEEERQRQ--EEEERKQRLQLQAAQERARQQQEEFRRK------LQELQRKKQQEEAERAEAEKQRQK 455
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 2805 AEAAKmkdLAEEASRLRAISEEAK--HQRQIAEEEAARQRAEAERILKEKLAA 2855
Cdd:pfam15709 456 ELEMQ---LAEEQKRLMEMAEEERleYQRQKQEAEEKARLEAEERRQKEEEAA 505
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2616-2855 |
4.13e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2616 AVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEE 2695
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2696 SALKQKEMAEEELERQRKIAESTAQQkltAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVR 2775
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQ---PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2776 SEMDILIQLKT--KAEKETMSNTEKSKQLLEAEAAkmKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKL 2853
Cdd:COG4942 171 AERAELEALLAelEEERAALEALKAERQKLLARLE--KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
..
gi 1988774674 2854 AA 2855
Cdd:COG4942 249 AA 250
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2756-2911 |
4.27e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.95 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2756 EVAAAQQQRKQledELAKVRSEMDILIQLKTKAEKETmsntEKSKQLLEAEAAKMKDLAEEASRLRAIS---------EE 2826
Cdd:COG2268 213 EIAIAQANREA---EEAELEQEREIETARIAEAEAEL----AKKKAEERREAETARAEAEAAYEIAEANaerevqrqlEI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2827 AKHQRQI--AEEEAARQRAEAERILKEKLAAISEATRLKTEAE----IALKEKEAENERLRRQAEdEAYQRKALEDQASQ 2900
Cdd:COG2268 286 AEREREIelQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEaeaiRAKGLAEAEGKRALAEAW-NKLGDAAILLMLIE 364
|
170
....*....|.
gi 1988774674 2901 HKQEIEEKIVQ 2911
Cdd:COG2268 365 KLPEIAEAAAK 375
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2513-2692 |
4.27e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2513 LRKQVSEetQKKRQAEEELKR-KSEAEKEAAKQKQKAL----EDLEKLRmqaEEAERQVKQAEIE---KEKQIKVAHEA- 2583
Cdd:PRK12704 24 VRKKIAE--AKIKEAEEEAKRiLEEAKKEAEAIKKEALleakEEIHKLR---NEFEKELRERRNElqkLEKRLLQKEENl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2584 AQKSAAAELQSKHMsfaektSKLEESLKQEHGAVLQLQQEAERLKKQQED-----AENSREEAEKE-LEKWRQKA-NEAL 2656
Cdd:PRK12704 99 DRKLELLEKREEEL------EKKEKELEQKQQELEKKEEELEELIEEQLQeleriSGLTAEEAKEIlLEKVEEEArHEAA 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 1988774674 2657 RLRLQAEDEAHKktlaqeeaekqkeeaerEAKKRAK 2692
Cdd:PRK12704 173 VLIKEIEEEAKE-----------------EADKKAK 191
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2443-2968 |
4.32e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.37 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2443 SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQdEAEKLRKQVSEETQ 2522
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIK-TAESDLSMELEKNN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2523 KKRQAEEELKRkseAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAeiekEKQIKVAHEAAQKsaAAELQSKHMSFAEK 2602
Cdd:PRK01156 274 YYKELEERHMK---IINDPVYKNRNYINDYFKYKNDIENKKQILSNI----DAEINKYHAIIKK--LSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2603 TSKLEE------SLKQEHGAVLQLQQEAERLKKQqedaensREEAEKELEKWRQKANEALRLRLQAEDE--AHKKTLAQE 2674
Cdd:PRK01156 345 KSRYDDlnnqilELEGYEMDYNSYLKSIESLKKK-------IEEYSKNIERMSAFISEILKIQEIDPDAikKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2675 EAEKQKEEAEREAKKRakaeesALKQKEMaeeELERQRKIAESTAQQKLT----AEQELIRLRADFDNaeqQRSLLEDEL 2750
Cdd:PRK01156 418 LQDISSKVSSLNQRIR------ALRENLD---ELSRNMEMLNGQSVCPVCgttlGEEKSNHIINHYNE---KKSRLEEKI 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2751 YRLKNEVAAAQQQRKQLE--------DELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRA 2822
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKkrkeylesEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2823 ISEE---AKHQRQIAEEEAARQRAEaerilkEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAY----QRKALE 2895
Cdd:PRK01156 566 KRTSwlnALAVISLIDIETNRSRSN------EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANnlnnKYNEIQ 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2896 DQASQhKQEIEEKIVQLKKSSEAEMERQKAI--------------------VDDTLKQRRVVEEEIRILKLNFEKASSGK 2955
Cdd:PRK01156 640 ENKIL-IEKLRGKIDNYKKQIAEIDSIIPDLkeitsrindiednlkksrkaLDDAKANRARLESTIEILRTRINELSDRI 718
|
570
....*....|...
gi 1988774674 2956 LDLELELNKLKNI 2968
Cdd:PRK01156 719 NDINETLESMKKI 731
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2384-2669 |
4.35e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 53.06 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2384 DKQKQLAEAHAKAIAKAEKEAQELKLKMQEEvskrEIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTK 2463
Cdd:PRK07735 2 DPEKDLEDLKKEAARRAKEEARKRLVAKHGA----EISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2464 IEEEIRliriqlETTEKQKYTAESelkqlrdRAAEAEKLRklaqdeAEKLRKQVSEETQkkrQAEEELKRKSEAeKEAAK 2543
Cdd:PRK07735 78 KREGTE------EVTEEEKAKAKA-------KAAAAAKAK------AAALAKQKREGTE---EVTEEEKAAAKA-KAAAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2544 QKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQE 2623
Cdd:PRK07735 135 AKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAK 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1988774674 2624 AERLKKQQEdaenSREEAEKELEKWRQKANEALRLRLQAEDEAHKK 2669
Cdd:PRK07735 215 AAALAKQKA----SQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTK 256
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2386-2578 |
4.77e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2386 QKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREiAAVDAEKQKTNIqLELQELKNLSEQQIKDKSQQVDEALHSRTKIE 2465
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAE-AALEEFRQKNGL-VDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2466 EEIRLIRIQLETTEKQKYT--AESELKQLRDRAAEAE-KLRKLAQD------EAEKLRKQVSEETQKKRQAEEELKRKSE 2536
Cdd:COG3206 240 ARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEaELAELSARytpnhpDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1988774674 2537 AEKEAAKQKQKALED-LEKLRMQAEE-AERQVKQAEIEKEKQIK 2578
Cdd:COG3206 320 AELEALQAREASLQAqLAQLEARLAElPELEAELRRLEREVEVA 363
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2696-2900 |
4.83e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2696 SALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAK-- 2773
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2774 --------VRSEMDILIQLK---------------TKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKH- 2829
Cdd:COG3883 93 ralyrsggSVSYLDVLLGSEsfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAe 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 2830 -QRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQ 2900
Cdd:COG3883 173 lEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3511-3616 |
4.98e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3511 EKLIEDEKKRLESQFEEEVKKAKalkDEQERQKQQMEQEKKTLQATMdAALSKQKEAEEEMLRKQKEMQELERQRLE-QE 3589
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEALLEAK---EEIHKLRNEFEKELRERRNEL-QKLEKRLLQKEENLDRKLELLEKREEELEkKE 116
|
90 100
....*....|....*....|....*..
gi 1988774674 3590 RILAEENQKLREKLQQLEDAQKDQHTR 3616
Cdd:PRK12704 117 KELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2695-2928 |
5.95e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2695 ESALKQKEMAEEELERQRKIAEsTAQQKLTA---EQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDEL 2771
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2772 AKVRSEMDILIQLKTKAEKETmsntekskQLLEAEAakmkDLAEEASRLRaiseeAKHQRQIAeeeAARQRAEAERILKE 2851
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRA--------QLAELEA----ELAELSARYT-----PNHPDVIA---LRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2852 KLAAISEAtrLKTEAEiALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIE--EKIVQ--LKKSSEAEMERQKAIV 2927
Cdd:COG3206 310 EAQRILAS--LEAELE-ALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEvaRELYEslLQRLEEARLAEALTVG 386
|
.
gi 1988774674 2928 D 2928
Cdd:COG3206 387 N 387
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2616-2944 |
6.57e-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: 51.84 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2616 AVLQLQQEAERLKKQQEDAENSREEAEKELEkwRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEE 2695
Cdd:pfam13868 22 KERDAQIAEKKRIKAEEKEEERRLDEMMEEE--RERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2696 SALKQKEMAEEELERQRKIAESTAQQKLTAE--QELIRLRADFDNAEQQRSLLEDElyRLKNEVAAAQQQRKQLEDELAK 2773
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKELEKEEEREEDE--RILEYLKEKAEREEEREAEREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2774 VRSEMDILIQLKTKAEKETMsnteksKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKL 2853
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQ------DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2854 AAIsEATRLKTEAEIALKEKEAENERLRRQAEDeayQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQ 2933
Cdd:pfam13868 252 LAE-EAEREEEEFERMLRKQAEDEEIEQEEAEK---RRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAER 327
|
330
....*....|.
gi 1988774674 2934 RRVVEEEIRIL 2944
Cdd:pfam13868 328 RERIEEERQKK 338
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4933-4971 |
6.87e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.78 E-value: 6.87e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1988774674 4933 YLQGTGCIAGVFLESTKERLSIYQAMKKNMIRPGTAFEL 4971
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2734-3185 |
7.53e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.60 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2734 ADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKE---TMSNTEKSKQLLEAeaakM 2810
Cdd:COG5278 79 EPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEaalALVRSGEGKALMDE----I 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2811 KDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQ 2890
Cdd:COG5278 155 RARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2891 RKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAD 2970
Cdd:COG5278 235 LAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2971 ETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQI 3050
Cdd:COG5278 315 AAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3051 VVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAEREAALLRQQAEEAERQKTAAEEEA 3130
Cdd:COG5278 395 IAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAAL 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 3131 ANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQ 3185
Cdd:COG5278 475 AALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAE 529
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
1043-1165 |
8.82e-06 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 48.89 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1043 EKTWPNFIEDErdrvqKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRM 1109
Cdd:cd21323 15 EGTQHSYSEEE-----KVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLT 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774674 1110 RFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 1165
Cdd:cd21323 90 PFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
3162-3615 |
9.12e-06 |
|
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: 52.44 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3162 LMQKQQADTEMAKHKKLAEQTLKQKFqveqeLTKVKLKLDETDKQKSVLDEELQRLKDEVDD----AVKQRGQVEEELFK 3237
Cdd:pfam05557 59 LLEKREAEAEEALREQAELNRLKKKY-----LEALNKKLNEKESQLADAREVISCLKNELSElrrqIQRAELELQSTNSE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3238 VKVQMEELLKLKNKIEEENQRliKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEA----ARLRQIAEDDLNQQRALA 3313
Cdd:pfam05557 134 LEELQERLDLLKAKASEAEQL--RQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVknskSELARIPELEKELERLRE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3314 E-KMLKEkmqAIQEASRLKAEAEMLQKQKDlAQEQAQKLLEDKQLMQQRLEEETEEYHK----------SLEVERKRQLE 3382
Cdd:pfam05557 212 HnKHLNE---NIENKLLLKEEVEDLKRKLE-REEKYREEAATLELEKEKLEQELQSWVKlaqdtglnlrSPEDLSRRIEQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3383 IMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLEN 3462
Cdd:pfam05557 288 LQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDK 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3463 E---------KARLKKEAEEL----QNKSKEMaDAQQKKIEHEKTVL-QQTFMTEKEMLLKKEKLIEDEKKRLESQFEEE 3528
Cdd:pfam05557 368 EltmsnyspqLLERIEEAEDMtqkmQAHNEEM-EAQLSVAEEELGGYkQQAQTLERELQALRQQESLADPSYSKEEVDSL 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3529 VKKAKALKDEQERQKQQ-----MEQEKKTLQATMDAALSKQkeaeeeMLRKQKEMQELERQRLEQERILAEENQKLREKL 3603
Cdd:pfam05557 447 RRKLETLELERQRLREQkneleMELERRCLQGDYDPKKTKV------LHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLL 520
|
490
....*....|..
gi 1988774674 3604 QQLEDAQKDQHT 3615
Cdd:pfam05557 521 KKLEDDLEQVLR 532
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2416-2588 |
9.14e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2416 SKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDksqqvdEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQlrdr 2495
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKE------EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2496 aaeaeKLRKLaqdeaEKLRKQVSEETQKKRQAEEELKRKseaEKEAAKQKQKALEDLEKL-RMQAEEAERQV-----KQA 2569
Cdd:PRK12704 101 -----KLELL-----EKREEELEKKEKELEQKQQELEKK---EEELEELIEEQLQELERIsGLTAEEAKEILlekveEEA 167
|
170
....*....|....*....
gi 1988774674 2570 EIEKEKQIKVAHEAAQKSA 2588
Cdd:PRK12704 168 RHEAAVLIKEIEEEAKEEA 186
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2355-2569 |
9.58e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 52.52 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2355 QRRLDDEEKAAEKLKAEERKKMAEMQaelDKQKQLAEAHAKAIAKAEKEAQElKLKMqeevSKREIAAVDAEKQktniQL 2434
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELE---EKKEKLQEEEDKLLEEAEKEAQQ-AIKE----AKKEADEIIKELR----QL 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2435 ELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYtaeSELKQlrdraaEAEKLRKLAQDEAeklr 2514
Cdd:PRK00409 597 QKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVKY---LSLGQ------KGEVLSIPDDKEA---- 663
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 2515 kQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEK------LR-MQAEEAERQVKQA 2569
Cdd:PRK00409 664 -IVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTvsleldLRgMRYEEALERLDKY 724
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
2355-2580 |
1.03e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 51.30 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2355 QRRLDDEEKAAEKLK----AEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEevskreiaavdAEKQKT 2430
Cdd:pfam09787 17 ARILQSKEKLIASLKegsgVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE-----------LEAQQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2431 NIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRiqlETTEKQKYTAESELKQLrdraaeaeklrklaQDEA 2510
Cdd:pfam09787 86 EEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLE---EELRRSKATLQSRIKDR--------------EAEI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 2511 EKLRKQVSEETQKKRQaEEELKRKSEAEKEAAKQKQKALEDL--EK--LRMQAEEAERQVKQAEIEKEKQIKVA 2580
Cdd:pfam09787 149 EKLRNQLTSKSQSSSS-QSELENRLHQLTETLIQKQTMLEALstEKnsLVLQLERMEQQIKELQGEGSNGTSIN 221
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2238-2554 |
1.05e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.22 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2238 ADAKQRQEKI--QAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQ-VEPLVSPL 2314
Cdd:PRK11281 39 ADVQAQLDALnkQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDnDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2315 KKT-------KLDSASDNIIQEYVTLRTRYSELMTLTSQYI---KFITDTQRR-------LDDEEKAAEKLKAEERKKMA 2377
Cdd:PRK11281 119 STLslrqlesRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraqAALYANSQRlqqirnlLKGGKVGGKALRPSQRVLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2378 EMQAELDKQ-------------------KQLAEAHAKaIAKAEKEAQEL-------KLKMQEEVSKREIAAVDAEKQKTN 2431
Cdd:PRK11281 199 AEQALLNAQndlqrkslegntqlqdllqKQRDYLTAR-IQRLEHQLQLLqeainskRLTLSEKTVQEAQSQDEAARIQAN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2432 --IQLEL--------------QELKNLSEQQIKDKsQQVDEALHSRTKIEEEIR-------LIRIQLEttEKQKYTAESE 2488
Cdd:PRK11281 278 plVAQELeinlqlsqrllkatEKLNTLTQQNLRVK-NWLDRLTQSERNIKEQISvlkgsllLSRILYQ--QQQALPSADL 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 2489 LKQLRDRAAeaeKLRkLAQDEAEKLRKQVSEETQKKRQAEEELKRK-SEAEKEA----AKQKQKALEDLEK 2554
Cdd:PRK11281 355 IEGLADRIA---DLR-LEQFEINQQRDALFQPDAYIDKLEAGHKSEvTDEVRDAllqlLDERRELLDQLNK 421
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3447-3580 |
1.11e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 52.14 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3447 SKEADDLRKAIADLENEKARLKKEAEELQNKSKEmadAQQKKiehektvlqqtfmteKEMLLKKEKLIEDEKK---RLES 3523
Cdd:PRK00409 512 GEDKEKLNELIASLEELERELEQKAEEAEALLKE---AEKLK---------------EELEEKKEKLQEEEDKlleEAEK 573
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 3524 QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDA-----ALSKQKEAEEEMLRKQKEMQE 3580
Cdd:PRK00409 574 EAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELiearkRLNKANEKKEKKKKKQKEKQE 635
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3511-3619 |
1.11e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.70 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3511 EKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTlqatmdaalskqkEAEEEMLRKQKEMQELERQRLEQER 3590
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRN-------------EFEKELRERRNELQKLEKRLLQKEE 96
|
90 100
....*....|....*....|....*....
gi 1988774674 3591 ILAEENQKLREKLQQLEDAQKDQHTRETD 3619
Cdd:PRK12704 97 NLDRKLELLEKREEELEKKEKELEQKQQE 125
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2523-2856 |
1.12e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.07 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2523 KKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQaeiEKEKQIKVAHEAAQKSAAAELQSKHMsfaek 2602
Cdd:pfam13868 31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQ---ELEEQIEEREQKRQEEYEEKLQEREQ----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2603 tskLEESLKQEHgavLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKaneaLRLRLQAEDEAHKKTLAQEEAekqkee 2682
Cdd:pfam13868 103 ---MDEIVERIQ---EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKEL----EKEEEREEDERILEYLKEKAE------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2683 aeREAKKRAKAEEsalkQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 2762
Cdd:pfam13868 167 --REEEREAEREE----IEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2763 QRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQR 2842
Cdd:pfam13868 241 REEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
|
330
....*....|....
gi 1988774674 2843 AEAERILKEKLAAI 2856
Cdd:pfam13868 321 REEEAERRERIEEE 334
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2536-2903 |
1.18e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 51.79 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2536 EAEKEAAKQK-QKALEDLEKLRmQAEEAERQVKQAEIEKEKQIkVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQeh 2614
Cdd:pfam02029 2 EDEEEAARERrRRAREERRRQK-EEEEPSGQVTESVEPNEHNS-YEEDSELKPSGQGGLDEEEAFLDRTAKREERRQK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2615 gavlQLQQEAERLKKQQED--------AENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTlaqeeaekqkeeaeRE 2686
Cdd:pfam02029 78 ----RLQEALERQKEFDPTiadekesvAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIRE--------------KE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2687 AKKRAKAEESALKQKEMAEEElerqRKIAESTAQQKltaeqelirlraDFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQ 2766
Cdd:pfam02029 140 YQENKWSTEVRQAEEEGEEEE----DKSEEAEEVPT------------ENFAKEEVKDEKIKKEKKVKYESKVFLDQKRG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2767 LEDELAKVRSEMDILIQLKTKAEKETMSNT----EKSKQLLEAEAAKmkdlaEEASRLRAISE----EAKHQRQiaeEEA 2838
Cdd:pfam02029 204 HPEVKSQNGEEEVTKLKVTTKRRQGGLSQSqereEEAEVFLEAEQKL-----EELRRRRQEKEseefEKLRQKQ---QEA 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 2839 ARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERL------RRQAEDEAYQRKALEDQASQHKQ 2903
Cdd:pfam02029 276 ELELEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRmkeeieRRRAEAAEKRQKLPEDSSSEGKK 346
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2355-2670 |
1.18e-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: 51.19 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2355 QRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKqLAEAHAKaiAKAEKEAQELKLKMQEEvskreiaavdaekqktniql 2434
Cdd:pfam15558 78 ERRRADRREKQVIEKESRWREQAEDQENQRQEK-LERARQE--AEQRKQCQEQRLKEKEE-------------------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2435 ELQELKNLSEQQIKDKSQQvdeALHSRTKIEEEIRLIRIQLETTEKQKYTAeseLKQLRDRAAEAEK-LRKL-------- 2505
Cdd:pfam15558 135 ELQALREQNSLQLQERLEE---ACHKRQLKEREEQKKVQENNLSELLNHQA---RKVLVDCQAKAEElLRRLsleqslqr 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2506 AQDEAEKLRKQVSEETQKKRQAEEELKRKSeaeKEAAKQKQKalEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQ 2585
Cdd:pfam15558 209 SQENYEQLVEERHRELREKAQKEEEQFQRA---KWRAEEKEE--ERQEHKEALAELADRKIQQARQVAHKTVQDKAQRAR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2586 KSAAAELQSKHMSfAEKTSKLEESLKQEhgavlqlqqEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDE 2665
Cdd:pfam15558 284 ELNLEREKNHHIL-KLKVEKEEKCHREG---------IKEAIKKKEQRSEQISREKEATLEEARKTARASFHMREKVREE 353
|
....*
gi 1988774674 2666 AHKKT 2670
Cdd:pfam15558 354 TNNRT 358
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2213-2945 |
1.26e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2213 QRELEQLGRQLGYYRESYDWLIRWIADAKQRQEKIQavpitdskTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDT 2292
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQ--------TRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEE 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2293 IKDYELQLVAYKAQVEplvsplkkTKLDSASDniiqeyvtLRTRYSELMTLtsqyIKFITDTQRRLDDEEKAAEKLKAEE 2372
Cdd:PRK04863 447 FQAKEQEATEELLSLE--------QKLSVAQA--------AHSQFEQAYQL----VRKIAGEVSRSEAWDVARELLRRLR 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2373 RKKMaemqaeLDKQKQLAEAHAKAIAKAEKEAQELKlKMQEEVSKREIAAVDAEKqktniqlELQELKNLSEQQIKDKSQ 2452
Cdd:PRK04863 507 EQRH------LAEQLQQLRMRLSELEQRLRQQQRAE-RLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2453 QVDEALHSRTKIEEEIRLIRIQ---LETTEKQKYTAESELKQLRDRAAEA----EKLRKLAQDEAEKLRK---QVSEETQ 2522
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARiqrLAARAPAWLAAQDALARLREQSGEEfedsQDVTEYMQQLLEREREltvERDELAA 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2523 KKRQAEEELKRKSEAEK-------------------------------------------------EAAKQKQKALEDL- 2552
Cdd:PRK04863 653 RKQALDEEIERLSQPGGsedprlnalaerfggvllseiyddvsledapyfsalygparhaivvpdlSDAAEQLAGLEDCp 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2553 EKLRM-------------QAEEAERQV------KQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESlkqe 2613
Cdd:PRK04863 733 EDLYLiegdpdsfddsvfSVEELEKAVvvkiadRQWRYSRFPEVPLFGRAAREKRIEQLRAEREELAERYATLSFD---- 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2614 hgavlqlQQEAERLKKQQEDAENS------REEAEKELEKWRQKANEALRlRLQAEDEAHKKTLAQEEAEKQKEEAEREA 2687
Cdd:PRK04863 809 -------VQKLQRLHQAFSRFIGShlavafEADPEAELRQLNRRRVELER-ALADHESQEQQQRSQLEQAKEGLSALNRL 880
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2688 KKRAK--AEESALKQKEMAEEELERQRKIAESTAQQKLTA---EQELIRLRADFDNAEQqrslledelyrLKNEVAAAQQ 2762
Cdd:PRK04863 881 LPRLNllADETLADRVEEIREQLDEAEEAKRFVQQHGNALaqlEPIVSVLQSDPEQFEQ-----------LKQDYQQAQQ 949
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2763 QRKQLedelakvrsemdiliQLKTKAEKETMSNTEkskQLLEAEAAKMkdLAEEA---SRLRAISEEAKHQRQIAEEEAA 2839
Cdd:PRK04863 950 TQRDA---------------KQQAFALTEVVQRRA---HFSYEDAAEM--LAKNSdlnEKLRQRLEQAEQERTRAREQLR 1009
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2840 RQRAEAERILKEKLAAISEATRLKTEaeiaLKEKEAENERLRRQAEDEAyqrkalEDQASQHKQEIEEKIV--QLKKSS- 2916
Cdd:PRK04863 1010 QAQAQLAQYNQVLASLKSSYDAKRQM----LQELKQELQDLGVPADSGA------EERARARRDELHARLSanRSRRNQl 1079
|
810 820
....*....|....*....|....*....
gi 1988774674 2917 EAEMERQKAIVDDTLKQRRVVEEEIRILK 2945
Cdd:PRK04863 1080 EKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2847-3613 |
1.26e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2847 RILKEKLAAISEATRLKTEAEIALKEKEAENERL---RRQAEDEAYQRKALEDQ-------------ASQHKQEIEEKIV 2910
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDyqaasdhlnlvqtALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2911 QLKKSSEAeMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKiRAEEEAEKLRKLA 2990
Cdd:PRK04863 356 DLEELEER-LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAV-QALERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2991 leeekrrreaeekvkkiaaaeeeaarqrkaALEeLERLRKKAEEARKQKDEADKE---AEKQIVVAQQAAQKCSAAEQQV 3067
Cdd:PRK04863 434 ------------------------------DLT-ADNAEDWLEEFQAKEQEATEEllsLEQKLSVAQAAHSQFEQAYQLV 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3068 QSvLAQQIEDSITQKKLKEeyekakklAKEAEAAKEKAEREAALLRQQAEEAERQktaaeeeaanqAKAQEDAERLRKEA 3147
Cdd:PRK04863 483 RK-IAGEVSRSEAWDVARE--------LLRRLREQRHLAEQLQQLRMRLSELEQR-----------LRQQQRAERLLAEF 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3148 EFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSV---LDEELQRLKDEVDDA 3224
Cdd:PRK04863 543 CKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEE 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3225 VKQRGQVEEelfkvkvQMEELLKLKNKIEEENQRLikkdkdstqkllaeeAENMRKLAEDAARLS-VEAQEAARLRQIAE 3303
Cdd:PRK04863 623 FEDSQDVTE-------YMQQLLERERELTVERDEL---------------AARKQALDEEIERLSqPGGSEDPRLNALAE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3304 -----------DDLNQQRA-LAEKMLKEKMQAIQeASRLKAEAEMLQKQKDlaqeqaqkLLEDKQLMQ---QRLEE---E 3365
Cdd:PRK04863 681 rfggvllseiyDDVSLEDApYFSALYGPARHAIV-VPDLSDAAEQLAGLED--------CPEDLYLIEgdpDSFDDsvfS 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3366 TEEYHKSLEVErkrqleimaEAERlRLQVSQLSEA----QARAEEEAKKFKKQADKVATRLHETEIATQEkmtvVERL-- 3439
Cdd:PRK04863 752 VEELEKAVVVK---------IADR-QWRYSRFPEVplfgRAAREKRIEQLRAEREELAERYATLSFDVQK----LQRLhq 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3440 EFER-----LNTSKEAD------DLRKAIADLENEKARLKKEAEELQN---KSKEMADAQQKKIEHEKTVLQQTFMTEKE 3505
Cdd:PRK04863 818 AFSRfigshLAVAFEADpeaelrQLNRRRVELERALADHESQEQQQRSqleQAKEGLSALNRLLPRLNLLADETLADRVE 897
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3506 MLlkKEKLIEDEK-----KRLESQFEEEVKKAKALKDEQE------RQKQQMEQEKKTLQATMDA---------ALSKQK 3565
Cdd:PRK04863 898 EI--REQLDEAEEakrfvQQHGNALAQLEPIVSVLQSDPEqfeqlkQDYQQAQQTQRDAKQQAFAltevvqrraHFSYED 975
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 1988774674 3566 EAeeEMLRKQKEMQELERQRLEQ-ERILAEENQKLREKLQQLedAQKDQ 3613
Cdd:PRK04863 976 AA--EMLAKNSDLNEKLRQRLEQaEQERTRAREQLRQAQAQL--AQYNQ 1020
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
3322-3610 |
1.32e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3322 QAIQEASRLKAEAEMLqKQKDLAQEQAQKLLEDKQLMQQRLEEET--EEYHKSLEVERKRQLEIM---------AEAERL 3390
Cdd:COG3206 75 SLSASDSPLETQIEIL-KSRPVLERVVDKLNLDEDPLGEEASREAaiERLRKNLTVEPVKGSNVIeisytspdpELAAAV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3391 ------RLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEIATQEkmtvverleFER----LNTSKEADDLRKAIADL 3460
Cdd:COG3206 154 analaeAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE---------FRQknglVDLSEEAKLLLQQLSEL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3461 ENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEkemLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQE 3540
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774674 3541 RQKQQMEQEKKTLQATMDAALSKQKeAEEEMLRKQ--------KEMQELERQRLEQERILAEENQKLREKLQQLEDAQ 3610
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAELEALQ-AREASLQAQlaqlearlAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2360-2658 |
1.33e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 51.76 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2360 DEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQEL 2439
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2440 KNLSEQ----QIKDKSQQVDEALHSRTKIEEEIRLIRIQLETT---------------EKQKY-----TAESELKQLRDR 2495
Cdd:PRK04778 185 VELTESgdyvEAREILDQLEEELAALEQIMEEIPELLKELQTElpdqlqelkagyrelVEEGYhldhlDIEKEIQDLKEQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2496 AAEAEK-LRKLAQDEAEKLRKQVSEETQkkrQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQ----AEEAERqVKQA- 2569
Cdd:PRK04778 265 IDENLAlLEELDLDEAEEKNEEIQERID---QLYDILEREVKARKYVEKNSDTLPDFLEHAKEQnkelKEEIDR-VKQSy 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2570 -----EIEK----EKQIKvAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEhgAVLQLQQE--AERLkKQQEDAENsr 2638
Cdd:PRK04778 341 tlnesELESvrqlEKQLE-SLEKQYDEITERIAEQEIAYSELQEELEEILKQL--EEIEKEQEklSEML-QGLRKDEL-- 414
|
330 340
....*....|....*....|
gi 1988774674 2639 eEAEKELEKWRQKANEALRL 2658
Cdd:PRK04778 415 -EAREKLERYRNKLHEIKRY 433
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
1057-1158 |
1.36e-05 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 47.41 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1057 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRF----HKLQNVQIALDFLRHRQVKLV 1132
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1988774674 1133 NIRNDDIADGNPKLTLGLIWTIILHF 1158
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
3436-3625 |
1.41e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.55 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3436 VERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMAD-------AQQKKIEHEKTVLQQTFMTEKEMLL 3508
Cdd:PHA02562 236 IEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3509 KKEKLIEDEKKRLESQFEEEVKKAKALKDeqerqkqQMEQEKKTLQATMDAALskqkeaeeemlRKQKEMQELERQRLEQ 3588
Cdd:PHA02562 316 EKLDTAIDELEEIMDEFNEQSKKLLELKN-------KISTNKQSLITLVDKAK-----------KVKAAIEELQAEFVDN 377
|
170 180 190
....*....|....*....|....*....|....*..
gi 1988774674 3589 ERILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKD 3625
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3282-3493 |
1.54e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3282 AEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQR 3361
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3362 LEEETEEYhksleVERKRQLEIMAEAERLRLQVSQ------------LSEAQARAEEEAKKFKKQADKVATRLHETEIAT 3429
Cdd:COG4942 99 LEAQKEEL-----AELLRALYRLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 3430 QEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEK 3493
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2463-2613 |
1.58e-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: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2463 KIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKS------- 2535
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyea 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2536 -EAEKEAAKQKQKALEDLEK-LRMQAEEAERQVK--QAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLK 2611
Cdd:COG1579 94 lQKEIESLKRRISDLEDEILeLMERIEELEEELAelEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
..
gi 1988774674 2612 QE 2613
Cdd:COG1579 174 PE 175
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
1053-1161 |
1.59e-05 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 47.29 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1053 ERDRVQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEV---------LSGETLPREKGRMRfhKLQNVQIALDF 1123
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1988774674 1124 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 1161
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
3244-3618 |
1.87e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.34 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3244 ELLKLKNKIEEENQRLIKKDKDSTQ-KLLAEEAENMRKLAEDAARL----------SVEaQEAARLRQIAEDDLNQQRAL 3312
Cdd:PRK10246 455 EQTQRNAALNEMRQRYKEKTQQLADvKTICEQEARIKDLEAQRAQLqagqpcplcgSTS-HPAVEAYQALEPGVNQSRLD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3313 AekMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDkqlmQQRLEEETEEYHKSLEVERKRQLEI---MAEAER 3389
Cdd:PRK10246 534 A--LEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQE----EQALTQQWQAVCASLNITLQPQDDIqpwLDAQEE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3390 LRLQVSQLSeaqaraeeeaKKFKKQADKVATRLHETEIATQekmtvverLEFERLNTSKEADDLRKAIADLENEKARL-- 3467
Cdd:PRK10246 608 HERQLRLLS----------QRHELQGQIAAHNQQIIQYQQQ--------IEQRQQQLLTALAGYALTLPQEDEEASWLat 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3468 -KKEAEELQNKSKEMADAQQKKieHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfeeevkkAKALKDEQERQKQQM 3546
Cdd:PRK10246 670 rQQEAQSWQQRQNELTALQNRI--QQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQ-------CLSLHSQLQTLQQQD 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3547 EQEKKTL---QATMDAALSKQ----KEA-------EEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKD 3612
Cdd:PRK10246 741 VLEAQRLqkaQAQFDTALQASvfddQQAflaalldEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDL 820
|
....*.
gi 1988774674 3613 QHTRET 3618
Cdd:PRK10246 821 TVTVEQ 826
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3190-3627 |
1.90e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3190 EQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIeeeNQRLIKKDKDStqK 3269
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKF---LTEIKKKEKEL--E 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3270 LLAEEAENMRKLAEDaarlsVEAQEAARLRQIAE-----DDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKdla 3344
Cdd:TIGR04523 156 KLNNKYNDLKKQKEE-----LENELNLLEKEKLNiqkniDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQN--- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3345 qeqaQKLLEDKQLMQQRLEEETEEYHKSLEverkrqleimaeaerlrlQVSQLseaqaraeeeakkfKKQADKVATRLhe 3424
Cdd:TIGR04523 228 ----NQLKDNIEKKQQEINEKTTEISNTQT------------------QLNQL--------------KDEQNKIKKQL-- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3425 teiatQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKAR--LKKEAEELQNKSKEMADAQQKKIEHEKTVLQqtfMT 3502
Cdd:TIGR04523 270 -----SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQ---LN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3503 EKEMLLKKEKL-IEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQekktlqatmdaaLSKQKEAEEEMLRKQKEMQEL 3581
Cdd:TIGR04523 342 EQISQLKKELTnSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN------------LESQINDLESKIQNQEKLNQQ 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1988774674 3582 ERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDII 3627
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2706-3228 |
1.91e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2706 EELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQ--QQRKQLEDELAKVRSEmdiliq 2783
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPER------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2784 lktkaeketmsntekskqlLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLK 2863
Cdd:COG4717 148 -------------------LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2864 TEAEIALKEKEAENERLRRQAEDEayqrkaledQASQHKQEIEEKIVQLKKSSEAEmerqKAIVDDTLKQRRVVEEEIRI 2943
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQL---------ENELEAAALEERLKEARLLLLIA----AALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2944 LKLNFekASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALeeekrrreaeekvKKIAAAEEEAARQRKAALE 3023
Cdd:COG4717 276 AGVLF--LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEL-------------EELLAALGLPPDLSPEELL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3024 ELERLRKKAEEARKQKDEADKEAEKQivvaqqaaqkcsAAEQQVQSVLAQQIEDSItqkklkEEYEKAKKLAKEAEAAKE 3103
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLE------------ELEQEIAALLAEAGVEDE------EELRAALEQAEEYQELKE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3104 KAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAakraqaeaaalMQKQQADTEmAKHKKLAEQTL 3183
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE-----------LREELAELE-AELEQLEEDGE 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 3184 KQkfQVEQELTKVKLKLDETDKQ-------KSVLDEELQRLKDEVDDAVKQR 3228
Cdd:COG4717 471 LA--ELLQELEELKAELRELAEEwaalklaLELLEEAREEYREERLPPVLER 520
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2338-2595 |
2.05e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 51.37 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2338 SELMTLTSQYIKFITD---TQRRLDDEEKAaeklkAEERKKMaemqaELDKQKQLAeahakAIAKAEKEAQELKLKMQEE 2414
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERA-----EADRQRL-----EQEKQQQLA-----AISGSQSQLESTDQNALET 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2415 VSKREIAAVDAEKQKTNIQLE--LQELKNLSEQQ-----------------IKDKSQ-QVDEA-LHSRTKIEEeirliri 2473
Cdd:NF012221 1603 NGQAQRDAILEESRAVTKELTtlAQGLDALDSQAtyagesgdqwrnpfaggLLDRVQeQLDDAkKISGKQLAD------- 1675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2474 qlettEKQKYTAesELKQLRDRAAEAEKlrklAQDEAEKLRKQVSEETQKKR-QAEeelKRKSEA---EKEAAKQKQKAL 2549
Cdd:NF012221 1676 -----AKQRHVD--NQQKVKDAVAKSEA----GVAQGEQNQANAEQDIDDAKaDAE---KRKDDAlakQNEAQQAESDAN 1741
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1988774674 2550 EDLEKLRMQaeeAERQVKQAEIEKEKqikvaheaAQKSAAAELQSK 2595
Cdd:NF012221 1742 AAANDAQSR---GEQDASAAENKANQ--------AQADAKGAKQDE 1776
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2587-2846 |
2.17e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2587 SAAAELQSKHMSFAEKTSKLEESLKQehgaVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAlrlrlQAEDEA 2666
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-----EAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2667 HKKTLaqeeaekqkeeaereaKKRAKAE-------------------ESALKQKEMAEEELERQRKIAESTAQQKLTAEQ 2727
Cdd:COG3883 84 RREEL----------------GERARALyrsggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2728 ELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEA 2807
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 1988774674 2808 AKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAE 2846
Cdd:COG3883 228 AAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
3179-3350 |
2.21e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3179 AEQTLkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELL------KLKNKI 3252
Cdd:COG3206 194 AEAAL-EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLqspviqQLRAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3253 EEENQRLIKKDKDST------QKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQE 3326
Cdd:COG3206 273 AELEAELAELSARYTpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
170 180 190
....*....|....*....|....*....|..
gi 1988774674 3327 ASRLKAEAE--------MLQKQKDLAQEQAQK 3350
Cdd:COG3206 353 LRRLEREVEvarelyesLLQRLEEARLAEALT 384
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2625-2869 |
2.33e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2625 ERLKKQQEDAENSREEAEKELEKWRQKANealrlRLQAEDEAHKKtlaqeeaekqkeeaeREAKKRAKAEESALKQKEMA 2704
Cdd:COG2268 192 RKIAEIIRDARIAEAEAERETEIAIAQAN-----REAEEAELEQE---------------REIETARIAEAEAELAKKKA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2705 EEELERQRKIAESTAQQKLtaeqelirlradfdnaeqqrslledelyrlknevaAAQQQRKQLEDELAKVRSEMDILIQL 2784
Cdd:COG2268 252 EERREAETARAEAEAAYEI-----------------------------------AEANAEREVQRQLEIAEREREIELQE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2785 KTKAEKEtmsNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKhqrqiAEEEAARQRAEAERILKEklAAISEAtRLKT 2864
Cdd:COG2268 297 KEAEREE---AELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGL-----AEAEGKRALAEAWNKLGD--AAILLM-LIEK 365
|
....*
gi 1988774674 2865 EAEIA 2869
Cdd:COG2268 366 LPEIA 370
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2461-2554 |
2.37e-05 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 47.05 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2461 RTKIEEEIRLIRIQLETTEKQKYTAESELKQLRdraAEAEKLRKLAQDEAEKLRKQVseetqkKRQAEEELKR-KSEAEK 2539
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEI------LAEAKEEAERiLEQAKA 102
|
90
....*....|....*
gi 1988774674 2540 EAAKQKQKALEDLEK 2554
Cdd:cd06503 103 EIEQEKEKALAELRK 117
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
3508-3612 |
2.51e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.07 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3508 LKKEKLIEDEKKRLESQFEEevkkAKALKDEQERQKQQMEQEKKTLQAtmdaALSKQKEAEEEMLRKQKEMQELERQRLE 3587
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQ----TLALLDKIDRQKEETEQLKQQLAQ----APAKLRQAQAELEALKDDNDEETRETLS 119
|
90 100
....*....|....*....|....*
gi 1988774674 3588 QERiLAEENQKLREKLQQLEDAQKD 3612
Cdd:PRK11281 120 TLS-LRQLESRLAQTLDQLQNAQND 143
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
3290-3597 |
2.57e-05 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 51.10 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3290 VEAQEAARLRQIAEDDLNQQRAlaekmlkekmQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLE--DKQLMQQR--LEEE 3365
Cdd:pfam15818 10 LEALEELRMRREAETQYEEQIG----------KIIVETQELKWQKETLQNQKETLAKQHKEAMAvfKKQLQMKMcaLEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3366 TEEYHKSLEVERKrqlEIMAEAERLR-LQVSQLSEAQARAEEEAKKfkkQADKVATRLHETEIATQEK--MTVVERLEFE 3442
Cdd:pfam15818 80 KGKYQLATEIKEK---EIEGLKETLKaLQVSKYSLQKKVSEMEQKL---QLHLLAKEDHHKQLNEIEKyyATITGQFGLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3443 RLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEhEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLE 3522
Cdd:pfam15818 154 KENHGKLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIK-SKVTCQYKMGEENINLTIKEQKFQELQERLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3523 SQFEEEVKKAKALKDEQERQK---------QQMEQEKKTLQATMDAALSKQKEaEEEMLRKQKEMQElERQRLEQERILA 3593
Cdd:pfam15818 233 MELELNKKINEEITHIQEEKQdiiisfqhmQQLLQQQTQANTEMEAELKALKE-NNQTLERDNELQR-EKVKENEEKFLN 310
|
....
gi 1988774674 3594 EENQ 3597
Cdd:pfam15818 311 LQNE 314
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2465-2655 |
2.72e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2465 EEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQ 2544
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2545 KQKALEDLEKL--------------RMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsFAEKTSKLEESL 2610
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1988774674 2611 KQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEA 2655
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1937-2536 |
2.72e-05 |
|
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: 51.13 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1937 RLIMRNLELHYQDFMRDSQDSQLFGPDDRMQVEDDYTKSTQHFDNLLRSmeKGQQNETLCKNYISELKDLRLRIEDCEAG 2016
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ--KLEERSQKESKARSGLKVLLALIKDGVGG 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2017 TVARIRKPVEKEPLKEYIQKTTEQKKVQGELDGLKKDLDKVSVKTQEVLASPQPSASAPVLRSELDLTVQKMDHAHMLSS 2096
Cdd:pfam02463 523 RIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPI 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2097 VYLEKLKTVEMVIRNTQGAEGVLKQYEDCLREVHTVPSDVKEVETYRAK-------LKKMRTEAEDEQPVFDSLEEELKK 2169
Cdd:pfam02463 603 LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGvsleeglAEKSEVKASLSELTKELLEIQELQ 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2170 ASAVSDKMVRVHSERDVELDhFRQQLSSLQDRWKAVFTQIDLRQRELEQLGRQLGYYREsydwLIRWIADAKQRQEKIQA 2249
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIK-KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL----LKQKIDEEEEEEEKSRL 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2250 VPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKayidtIKDYELQLVAYKAQVEPLVSPLKKTKLDSASDNIIQE 2329
Cdd:pfam02463 758 KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEK-----LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2330 YVTLRTRYSELMTLTSQYiKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQlaeahakaiaKAEKEAQELKL 2409
Cdd:pfam02463 833 EELEELALELKEEQKLEK-LAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES----------KEEKEKEEKKE 901
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2410 KMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKqkytaesEL 2489
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL-------GK 974
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1988774674 2490 KQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSE 2536
Cdd:pfam02463 975 VNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2360-2612 |
2.95e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.34 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2360 DEEKAAEKLKAEERKKMAEMQAELDKQKQLAEahakaiAKAEKEAQELKLKMQEEvskreiaavdaekqktniqLELqel 2439
Cdd:pfam15709 329 EQEKASRDRLRAERAEMRRLEVERKRREQEEQ------RRLQQEQLERAEKMREE-------------------LEL--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2440 knlsEQQikdksqqvdealhsrtKIEEEIRLIRIQLEttEKQKYTAESELKQLRDRAAEAEKLRKlaqdEAEKLRKQVSE 2519
Cdd:pfam15709 381 ----EQQ----------------RRFEEIRLRKQRLE--EERQRQEEEERKQRLQLQAAQERARQ----QQEEFRRKLQE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2520 ETQKKRQAEEElkrKSEAEKEAAKQKQKALEDLEKLRMQAEEAER----QVKQAEIEKEKQikvahEAAQKSAAAELQSK 2595
Cdd:pfam15709 435 LQRKKQQEEAE---RAEAEKQRQKELEMQLAEEQKRLMEMAEEERleyqRQKQEAEEKARL-----EAEERRQKEEEAAR 506
|
250
....*....|....*..
gi 1988774674 2596 hMSFAEKTSKLEESLKQ 2612
Cdd:pfam15709 507 -LALEEAMKQAQEQARQ 522
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
3303-3577 |
2.97e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3303 EDDLNQQRALAEKMLKE----KMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEEteeyhksleveRK 3378
Cdd:COG1340 10 LEELEEKIEELREEIEElkekRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL-----------KE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3379 RQLEIMAEAERLRLQVSQLSEAQARAEEEA---KKFKKQADKVATRLHETEIATQEKMTVVERLE--FERLNTSKEADDL 3453
Cdd:COG1340 79 ERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKelEKELEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3454 RKAIADLENEKARLKKEAEELQNKSKEMADAQQKKieHEKtvlqqtfMTEkemLLKKEKLIEDEKKRLESQFEEEVKKAK 3533
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQEL--HEE-------MIE---LYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1988774674 3534 ALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKE 3577
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5141-5169 |
3.08e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 3.08e-05
10 20
....*....|....*....|....*....
gi 1988774674 5141 VRKRRVVIVDPETGKEMTVYEAYRKGLID 5169
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2559-3033 |
3.26e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2559 AEEAERQVKQA-EIEKEKQIKVAHEAAQKSAAAELQSKhmsfAEKTSKLEESLKQEHGAV---LQLQQEAERLKKQQEDA 2634
Cdd:PRK04863 278 ANERRVHLEEAlELRRELYTSRRQLAAEQYRLVEMARE----LAELNEAESDLEQDYQAAsdhLNLVQTALRQQEKIERY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2635 ENSREEAEKELEkwrqkanEALRLRLQAEDEAhkktlaqeeaekqkeeAEREAKKRAkAEESALK-QKEMA--EEELERQ 2711
Cdd:PRK04863 354 QADLEELEERLE-------EQNEVVEEADEQQ----------------EENEARAEA-AEEEVDElKSQLAdyQQALDVQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2712 --RKIAESTAQQKLTAEQELIRLrADFDnAEQqrslLEDELYRLKNEVAAAQQQRKQLEDELA---KVRSEMDILIQLKT 2786
Cdd:PRK04863 410 qtRAIQYQQAVQALERAKQLCGL-PDLT-ADN----AEDWLEEFQAKEQEATEELLSLEQKLSvaqAAHSQFEQAYQLVR 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2787 KAEKETMSNT--EKSKQLLEaEAAKMKDLAEEASRLRAISEEAKhQRQIAEEEAARQRAEAERILKEKLAAISEATRLkt 2864
Cdd:PRK04863 484 KIAGEVSRSEawDVARELLR-RLREQRHLAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL-- 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2865 eaeiaLKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEE--KIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIR 2942
Cdd:PRK04863 560 -----QEELEARLESLSESVSEARERRMALRQQLEQLQARIQRlaARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQ 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2943 ILKLNfEKassgkldlELELNKlkniaDETQQSKIRAEEEAEKLRklaleeekrrreaeekvkkiaaaeeeaarQRKAAl 3022
Cdd:PRK04863 635 QLLER-ER--------ELTVER-----DELAARKQALDEEIERLS-----------------------------QPGGS- 670
|
490
....*....|.
gi 1988774674 3023 eELERLRKKAE 3033
Cdd:PRK04863 671 -EDPRLNALAE 680
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2351-2548 |
3.28e-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: 49.76 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2351 ITDTQRRLDDEEKAAEKLKAEER---KKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEvsKREIAAVDAEK 2427
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAaleRRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ--KEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2428 QKTNIQLELQELKNLSE-QQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDR---------AA 2497
Cdd:COG4942 114 YRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEleeeraaleAL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 2498 EAEKLRKLAQDEAEKlrKQVSEETQKKRQAEEELKRK-SEAEKEAAKQKQKA 2548
Cdd:COG4942 194 KAERQKLLARLEKEL--AELAAELAELQQEAEELEALiARLEAEAAAAAERT 243
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
3297-3624 |
3.47e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 50.40 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3297 RLRQIAEDDLNQQRALAEKMLKEKMQAIQE---ASRLKAEAEMLQKQKDLAqEQAQKLLEDKQLMQQRLEEETEEY---- 3369
Cdd:NF033838 92 KLSDIKTEYLYELNVLKEKSEAELTSKTKKeldAAFEQFKKDTLEPGKKVA-EATKKVEEAEKKAKDQKEEDRRNYptnt 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3370 HKSLEVERKRQLEIMAEAERlrlqvsQLSEAQARAEEEAKKFKKQADKVATRlheteiatQEKMTVVERLEFERlntsKE 3449
Cdd:NF033838 171 YKTLELEIAESDVEVKKAEL------ELVKEEAKEPRDEEKIKQAKAKVESK--------KAEATRLEKIKTDR----EK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3450 ADDLRKAIADLENEKARLKKEAEELQNKSKEMA--------DAQQKKIEHEKT----VLQQTFMTEKemlLKKEKLI-ED 3516
Cdd:NF033838 233 AEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAkrgvlgepATPDKKENDAKSsdssVGEETLPSPS---LKPEKKVaEA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3517 EKKRLESQfeeevKKAKALKDEQERQKQQMEQekKTLQATMDAALSKQKEAEEEMLRKQ-KEMQELERQRLEQERILAEE 3595
Cdd:NF033838 310 EKKVEEAK-----KKAKDQKEEDRRNYPTNTY--KTLELEIAESDVKVKEAELELVKEEaKEPRNEEKIKQAKAKVESKK 382
|
330 340 350
....*....|....*....|....*....|...
gi 1988774674 3596 NQKLR-EKLQQLEDAQKDQHTR---ETDKVLHK 3624
Cdd:NF033838 383 AEATRlEKIKTDRKKAEEEAKRkaaEEDKVKEK 415
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2617-2941 |
3.70e-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: 49.65 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2617 VLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRL-------QAEDEAHKKTLAQEEAEKQKEEAEREAKK 2689
Cdd:pfam15558 13 MLARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLqqsqeqwQAEKEQRKARLGREERRRADRREKQVIEK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2690 RAKAEESALKQKEMAEEELERQRKIAESTAQ---QKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVaaAQQQRKQ 2766
Cdd:pfam15558 93 ESRWREQAEDQENQRQEKLERARQEAEQRKQcqeQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKER--EEQKKVQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2767 LEDELAKVRSE-MDILIQLKTKAEKETMSNT---------EKSKQLLEAEAAKMKDLA----EEASRLRAISEEAKHQRQ 2832
Cdd:pfam15558 171 ENNLSELLNHQaRKVLVDCQAKAEELLRRLSleqslqrsqENYEQLVEERHRELREKAqkeeEQFQRAKWRAEEKEEERQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2833 ------IAEEEAARQRAE--AERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKaledqasqhkqe 2904
Cdd:pfam15558 251 ehkealAELADRKIQQARqvAHKTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKK------------ 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 1988774674 2905 iEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEI 2941
Cdd:pfam15558 319 -EQRSEQISREKEATLEEARKTARASFHMREKVREET 354
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
3464-3636 |
3.74e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.34 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3464 KARLKKEAEELQNKSKEMADAQQKKIEhektvLQQTFMTEkEMLLKKEKLiEDEKKRLEsqfEEEVKKAKALKDEQERQK 3543
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELE-----LEQQRRFE-EIRLRKQRL-EEERQRQE---EEERKQRLQLQAAQERAR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3544 QQMEQEKKTLQatmDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAE--ENQKLREKLQQLEDAQKDQHTRETDKV 3621
Cdd:pfam15709 423 QQQEEFRRKLQ---ELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEmaEEERLEYQRQKQEAEEKARLEAEERRQ 499
|
170
....*....|....*
gi 1988774674 3622 LHKDIIHLTTIETTK 3636
Cdd:pfam15709 500 KEEEAARLALEEAMK 514
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
1058-1166 |
3.82e-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: 46.97 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1058 QKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 1124
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1988774674 1125 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 1166
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2775-3570 |
4.12e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2775 RSEMDILIQLKTKAEKETMSNT---EKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEeAARQR--------- 2842
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRrqlAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQT-ALRQQekieryqad 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2843 -AEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDeaYQRkALEDQ---ASQHKQEIE--EKIVQLKKSS 2916
Cdd:PRK04863 357 lEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD--YQQ-ALDVQqtrAIQYQQAVQalERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2917 EAEMERQKAIVDDTLKQRRVVEEEIRIL--KLNFEKASSGKLDLELELnkLKNIADET-----QQSKIRAEEEAEKLRKL 2989
Cdd:PRK04863 434 DLTADNAEDWLEEFQAKEQEATEELLSLeqKLSVAQAAHSQFEQAYQL--VRKIAGEVsrseaWDVARELLRRLREQRHL 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2990 AleeekrrreaeekvkkiaaaeeEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAaqkcsaaeQQVQS 3069
Cdd:PRK04863 512 A----------------------EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDEL--------EQLQE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3070 VLAQQIEDsitqkkLKEEYEKAKKLAKEaeaakekaereaalLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRkeAEF 3149
Cdd:PRK04863 562 ELEARLES------LSESVSEARERRMA--------------LRQQLEQLQARIQRLAARAPAWLAAQDALARLR--EQS 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3150 EAAKRAQAEAAALMQKQQadtemakhKKLAEQTLkQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKD---------- 3219
Cdd:PRK04863 620 GEEFEDSQDVTEYMQQLL--------ERERELTV-ERDELAARKQALDEEIERLSQPGGSEDPRLNALAErfggvllsei 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3220 ----EVDDA---------------VKQRGQVEEEL-------------------FKVKVQMEELLKlKNKIEEENQRLIK 3261
Cdd:PRK04863 691 yddvSLEDApyfsalygparhaivVPDLSDAAEQLagledcpedlyliegdpdsFDDSVFSVEELE-KAVVVKIADRQWR 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3262 KDKDSTQKLLAEEAENMR---------KLAEDAARLSVEAQEAARLRQIAEDDLNQQRALA-----EKMLKEKMQAIQEA 3327
Cdd:PRK04863 770 YSRFPEVPLFGRAAREKRieqlraereELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVEL 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3328 SRLKAEAE----MLQKQKDLAQEQAQ---------KLLEDKQLmQQRLEEETEEYHKSLEVERK--------RQLEIMAE 3386
Cdd:PRK04863 850 ERALADHEsqeqQQRSQLEQAKEGLSalnrllprlNLLADETL-ADRVEEIREQLDEAEEAKRFvqqhgnalAQLEPIVS 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3387 A--------ERLRLQVSQLseaqaraEEEAKKFKKQADKVAtrlheteiatqekmTVVERLefERLNTSKEADDLRKAIA 3458
Cdd:PRK04863 929 VlqsdpeqfEQLKQDYQQA-------QQTQRDAKQQAFALT--------------EVVQRR--AHFSYEDAAEMLAKNSD 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3459 DLENEKARLkKEAEELQNKSKEMADAQQKKIEHEKTV---LQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEevkKAKAL 3535
Cdd:PRK04863 986 LNEKLRQRL-EQAEQERTRAREQLRQAQAQLAQYNQVlasLKSSYDAKRQMLQELKQELQDLGVPADSGAEE---RARAR 1061
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1988774674 3536 KDE-QER------QKQQMEQEKKTLQATMDAALSKQKEAEEE 3570
Cdd:PRK04863 1062 RDElHARlsanrsRRNQLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2377-2775 |
4.47e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 49.97 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2377 AEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDE 2456
Cdd:COG4995 76 LLLALALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2457 ALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSE 2536
Cdd:COG4995 156 AAAAAAAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2537 AEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSkhmsfAEKTSKLEESLKQEHGA 2616
Cdd:COG4995 236 LLLALLALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALAL-----AAAALALALLLAAAAAA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2617 VLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 2696
Cdd:COG4995 311 ALAALALLLLAALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALL 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2697 ALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQ-QRSLLEDELYRLkneVAAAQQQRKQLEDELAKVR 2775
Cdd:COG4995 391 AALLLLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALiEYIILPDRLYAF---VQLYQLLIAPIEAELPGIK 467
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
1059-1124 |
4.70e-05 |
|
first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409070 Cd Length: 106 Bit Score: 45.73 E-value: 4.70e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1059 KKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREK----GRMRFHKLQNVQIALDFL 1124
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5008-5039 |
4.79e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.79e-05
10 20 30
....*....|....*....|....*....|..
gi 1988774674 5008 KLLSAERAVTGYRDPYTGKTISLFQAMKKGLI 5039
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
3514-3648 |
5.04e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.86 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3514 IEDEKKRLeSQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATmdaaLSKQKEAEEEMLRKQKEMQELER--QRLEQERI 3591
Cdd:COG2433 408 LTEEEEEI-RRLEEQVERLEAEVEELEAELEEKDERIERLERE----LSEARSEERREIRKDREISRLDReiERLERELE 482
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774674 3592 -LAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDIIHLTTIETTKTVYnGQNVGDVV 3648
Cdd:COG2433 483 eERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEY-GLKEGDVV 539
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4106-4142 |
5.08e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 5.08e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1988774674 4106 KLLSAERAVTGYRDPYTGKTVSLFQAMKKDLIPKEQG 4142
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
3181-3605 |
5.14e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 49.64 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3181 QTLKQKFQVEQELTKVKlkldetdkqksvldEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEEL-LKLKNKIEEENQRl 3259
Cdd:pfam05701 32 QTVERRKLVELELEKVQ--------------EEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELkLNLERAQTEEAQA- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3260 iKKDKDstqklLAE-EAENMRKLAEDAARLSVEAQ-EAARLRQIAeddlnqqrALAE-KMLKEKMQAIQEasrlkaEAEM 3336
Cdd:pfam05701 97 -KQDSE-----LAKlRVEEMEQGIADEASVAAKAQlEVAKARHAA--------AVAElKSVKEELESLRK------EYAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3337 LQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEY---HKSLEVERKRQLEimAEAERLRLQVSqlseaqaraeeeakkfkK 3413
Cdd:pfam05701 157 LVSERDIAIKRAEEAVSASKEIEKTVEELTIELiatKESLESAHAAHLE--AEEHRIGAALA-----------------R 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3414 QADKVAtrlHETEIATQEKmtvverlEFERLNtskeaDDLRKAiadlENEKARLKKEAEELQNKSKEMADAQQKKIEHEK 3493
Cdd:pfam05701 218 EQDKLN---WEKELKQAEE-------ELQRLN-----QQLLSA----KDLKSKLETASALLLDLKAELAAYMESKLKEEA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3494 TVLQQTFMTE---KEMLLKKEKLIEDEKKRLESQfEEEVK----KAKALKDEQERQK------QQ-----------MEQE 3549
Cdd:pfam05701 279 DGEGNEKKTStsiQAALASAKKELEEVKANIEKA-KDEVNclrvAAASLRSELEKEKaelaslRQregmasiavssLEAE 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3550 KKTLQATMDAALSKQKEAEEEMLRKQKEMQElERQRLEQERILA----EENQKLREKLQQ 3605
Cdd:pfam05701 358 LNRTKSEIALVQAKEKEAREKMVELPKQLQQ-AAQEAEEAKSLAqaarEELRKAKEEAEQ 416
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2353-3214 |
5.14e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2353 DTQRRLDDEEKAAEKLkAEERKKMAEMQAELDKQKQLAEAH----AKAIAKAEK--------EAQELKLKMQEEVSK-RE 2419
Cdd:COG3096 296 GARRQLAEEQYRLVEM-ARELEELSARESDLEQDYQAASDHlnlvQTALRQQEKieryqedlEELTERLEEQEEVVEeAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2420 IAAVDAEKQKTNIQLELQELKNlseqQIKDKSQQVDEaLHSRTkieeeirlirIQLETTEKQKYTAEsELKQLRDRAAEA 2499
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKS----QLADYQQALDV-QQTRA----------IQYQQAVQALEKAR-ALCGLPDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2500 eklrklAQDEAEKLRKQVSEETQKKRQAEEELkrkSEAEkEAAKQKQKALEDLEKL-----RMQAEEAERQVkqaeieke 2574
Cdd:COG3096 439 ------AEDYLAAFRAKEQQATEEVLELEQKL---SVAD-AARRQFEKAYELVCKIageveRSQAWQTAREL-------- 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2575 kqikVAHEAAQKSAAAELQSKHMSFAEktskLEESLKQEHGAVLQLQQEAERLKKQQEDA---ENSREEAEKELEKWRQK 2651
Cdd:COG3096 501 ----LRRYRSQQALAQRLQQLRAQLAE----LEQRLRQQQNAERLLEEFCQRIGQQLDAAeelEELLAELEAQLEELEEQ 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2652 ANEAL--RLRLQAEDEAHKktlaqeeaekqkeEAEREAKKRA----KAEESALKQKEMAEEELERQRKIAEsTAQQKLTA 2725
Cdd:COG3096 573 AAEAVeqRSELRQQLEQLR-------------ARIKELAARApawlAAQDALERLREQSGEALADSQEVTA-AMQQLLER 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2726 EQELIRLRadfDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVR-SEM--DILIqlktkaeketmsntekskql 2802
Cdd:COG3096 639 EREATVER---DELAARKQALESQIERLSQPGGAEDPRLLALAERLGGVLlSEIydDVTL-------------------- 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2803 leaeaakmkdlaEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAIS-------EATRLKTEAEIALKEKEA 2875
Cdd:COG3096 696 ------------EDAPYFSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLYLIEgdpdsfdDSVFDAEELEDAVVVKLS 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2876 ENE-RLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSS--EAEMERQKAIVDDTLKQRRVV------EEEIRILKl 2946
Cdd:COG3096 764 DRQwRYSRFPEVPLFGRAAREKRLEELRAERDELAEQYAKASfdVQKLQRLHQAFSQFVGGHLAVafapdpEAELAALR- 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2947 nfekASSGKLDLELElnklkNIADETQQSKIRAEEEAEKLRKLAleeekrrreaeekvKKIAAAEEEAARQRKAALEELE 3026
Cdd:COG3096 843 ----QRRSELERELA-----QHRAQEQQLRQQLDQLKEQLQLLN--------------KLLPQANLLADETLADRLEELR 899
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3027 RLRKKAEEAR---KQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQieDSITQKKLKEEYEKAKKLAKEAEAAKE 3103
Cdd:COG3096 900 EELDAAQEAQafiQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQ--RRLKQQIFALSEVVQRRPHFSYEDAVG 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3104 KAEREAAL---LRQQAEEAERQKTAAEEEAANQAKAQEDA-------------------ERLRKEAEFEAAKRAQAEAAA 3161
Cdd:COG3096 978 LLGENSDLnekLRARLEQAEEARREAREQLRQAQAQYSQYnqvlaslkssrdakqqtlqELEQELEELGVQADAEAEERA 1057
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 3162 LMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEEL 3214
Cdd:COG3096 1058 RIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
2459-2630 |
5.34e-05 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 50.04 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2459 HSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAE-AEKLRKlAQDEAEKLRKQVSEETQKKRQAEEELkrkSEA 2537
Cdd:pfam10168 554 LAREEIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKlAEKYEE-IKDKQEKLMRRCKKVLQRLNSQLPVL---SDA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2538 EKEAAKQkqkaledLEKLRMQAEEAERQVKQAEIEKEKQIKvaHEAAQKSAAaelQSKHMSFAEKTSK-LEESLKQEHGA 2616
Cdd:pfam10168 630 EREMKKE-------LETINEQLKHLANAIKQAKKKMNYQRY--QIAKSQSIR---KKSSLSLSEKQRKtIKEILKQLGSE 697
|
170
....*....|....
gi 1988774674 2617 VLQLQQEAERLKKQ 2630
Cdd:pfam10168 698 IDELIKQVKDINKH 711
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2803-2933 |
5.47e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 46.70 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2803 LEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAarqRAEAERILKEklaAISEATRLKTEaeiALKEKEAENERLRR 2882
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEA---RAEAAEIIAE---ARKEAEAIAEE---AKAEAEAEAERIIA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774674 2883 QAEDEAYQ-----RKALEDQASQHKQEIEEKIVQlkksSEAEMERQKAIVDDTLKQ 2933
Cdd:COG0711 100 QAEAEIEQerakaLAELRAEVADLAVAIAEKILG----KELDAAAQAALVDRFIAE 151
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2620-3073 |
5.54e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 49.64 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2620 LQQEAERLKKQQEDAENSREEAEKELEKWRqKANEALRLRL---QAEDEAHKK--TLAQEEAEKQKEEAEREAKKRAKAE 2694
Cdd:pfam05701 47 VQEEIPEYKKQSEAAEAAKAQVLEELESTK-RLIEELKLNLeraQTEEAQAKQdsELAKLRVEEMEQGIADEASVAAKAQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2695 --------ESALKQKEMAEEELERQRKIAESTAQQK-----------------------LTAE-----QELIRLRADFDN 2738
Cdd:pfam05701 126 levakarhAAAVAELKSVKEELESLRKEYASLVSERdiaikraeeavsaskeiektveeLTIEliatkESLESAHAAHLE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2739 AEQQR------------------SLLEDELYRLKNEVAAAQQQRKQLE---DELAKVRSEMDILIQLKTKAEKETMSNTE 2797
Cdd:pfam05701 206 AEEHRigaalareqdklnwekelKQAEEELQRLNQQLLSAKDLKSKLEtasALLLDLKAELAAYMESKLKEEADGEGNEK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2798 KSKQLLEAEAAKMKDLAEEasrLRAISEEAKHQRQIAEEEAARQRAEAErilKEKlAAISEATRLKTEAEIALKEKEAEN 2877
Cdd:pfam05701 286 KTSTSIQAALASAKKELEE---VKANIEKAKDEVNCLRVAAASLRSELE---KEK-AELASLRQREGMASIAVSSLEAEL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2878 ERLRrqAEDEAYQRKALEDQasqhkqeieEKIVQL-KKSSEAEMErqkaiVDDTLKQRRVVEEEIRILKLNFEKASSGKL 2956
Cdd:pfam05701 359 NRTK--SEIALVQAKEKEAR---------EKMVELpKQLQQAAQE-----AEEAKSLAQAAREELRKAKEEAEQAKAAAS 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2957 DLELELnklkniadETQQSKIRAEEEAEKLRKLALEEEKRRREAEEkvkkiAAAEEEAARQRKAALEELERLRKKAEEAR 3036
Cdd:pfam05701 423 TVESRL--------EAVLKEIEAAKASEKLALAAIKALQESESSAE-----STNQEDSPRGVTLSLEEYYELSKRAHEAE 489
|
490 500 510
....*....|....*....|....*....|....*..
gi 1988774674 3037 KQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQ 3073
Cdd:pfam05701 490 ELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEE 526
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4476-4511 |
5.71e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 5.71e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1988774674 4476 LLEAQIVSGGIIDPVKSHRVPTDVAYQKNILSRDIA 4511
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2485-2644 |
5.82e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 47.75 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2485 AESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQA----EEELKRKSEAEKEAAKQKQKALE-DLEKLRMQA 2559
Cdd:pfam04012 34 MQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAAltkgNEELAREALAEKKSLEKQAEALEtQLAQQRSAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2560 EEAERQV-----KQAEIEKEKQIKVAHEAAQKSAAAELQSKH-MSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQED 2633
Cdd:pfam04012 114 EQLRKQLaaletKIQQLKAKKNLLKARLKAAKAQEAVQTSLGsLSTSSATDSFERIEEKIEEREARADAAAELASAVDLD 193
|
170
....*....|.
gi 1988774674 2634 AENSREEAEKE 2644
Cdd:pfam04012 194 AKLEQAGIQME 204
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2522-2654 |
6.33e-05 |
|
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: 45.71 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2522 QKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEaerqvkqaeiekekqikvaheaAQKSAAAELQsKHMSFAE 2601
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIARE----------------------AQQNYERELV-LHAEDIK 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 2602 KTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANE 2654
Cdd:pfam07926 58 ALQALREELNELKAEIAELKAEAESAKAELEESEESWEEQKKELEKELSELEK 110
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2513-2801 |
6.34e-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: 49.52 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2513 LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAE-EAERQVKQAEIEKEKqIKVAHEAAQKSAAAE 2591
Cdd:pfam15964 319 VRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELErQKERLEKELASQQEK-RAQEKEALRKEMKKE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2592 ---LQSKHMSFAEKTSKLEESL----KQEHGAVLQLQQEAERLKKQQED--------------AENSREEAEKELEKWRQ 2650
Cdd:pfam15964 398 reeLGATMLALSQNVAQLEAQVekvtREKNSLVSQLEEAQKQLASQEMDvtkvcgemryqlnqTKMKKDEAEKEHREYRT 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2651 KANEALRLrlqAEDEAHKKTLAQEEAEKQKEEAEREAkkrAKAEESALKQKEMAEE--------ELER---QRKIAESTA 2719
Cdd:pfam15964 478 KTGRQLEI---KDQEIEKLGLELSESKQRLEQAQQDA---ARAREECLKLTELLGEsehqlhltRLEKesiQQSFSNEAK 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2720 QQKLTAEQELIRLRADFDNAEQQRSLLEDELYRL---KNEVAAAQQQR-----KQLEDELAKVRSEMDILIQ----LKTK 2787
Cdd:pfam15964 552 AQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLltsQNTFIAKLKEEcctlaKKLEEITQKSRSEVEQLSQekeyLQDR 631
|
330
....*....|....
gi 1988774674 2788 AEKETMSNTEKSKQ 2801
Cdd:pfam15964 632 LEKLQKRNEELEEQ 645
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
3291-3613 |
6.40e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.48 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3291 EAQEAAR-LRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDkqlMQQRLEEETEEY 3369
Cdd:pfam02029 3 DEEEAAReRRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDR---TAKREERRQKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3370 HKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKV---ATRLHETEIATQEKMTVVERLEfERLNT 3446
Cdd:pfam02029 80 QEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYkeeETEIREKEYQENKWSTEVRQAE-EEGEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3447 SKEADDLRKAI--ADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQ 3524
Cdd:pfam02029 159 EEDKSEEAEEVptENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3525 FEEEVKKAKALKDEQERQKQQME-QEKKTLQatmdaalSKQKEAE---EEMLRKQKE---MQELERQRLEQERILA---- 3593
Cdd:pfam02029 239 EAEVFLEAEQKLEELRRRRQEKEsEEFEKLR-------QKQQEAElelEELKKKREErrkLLEEEEQRRKQEEAERklre 311
|
330 340
....*....|....*....|...
gi 1988774674 3594 -EENQKLREKLQ--QLEDAQKDQ 3613
Cdd:pfam02029 312 eEEKRRMKEEIErrRAEAAEKRQ 334
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
3184-3365 |
6.45e-05 |
|
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: 48.34 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3184 KQKFQ--VEQELTKVKLKLDETDKQKSV--LDEELQRLKDEVDDAVKQ---------------RGQVEEELFKVK---VQ 3241
Cdd:cd16269 88 DQKFQkkLMEQLEEKKEEFCKQNEEASSkrCQALLQELSAPLEEKISQgsysvpggyqlyledREKLVEKYRQVPrkgVK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3242 MEELLK--LKNKIEEENQRLiKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAaRLRQIAEDdlnQQRALAE--KML 3317
Cdd:cd16269 168 AEEVLQefLQSKEAEAEAIL-QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQR-ELEQKLED---QERSYEEhlRQL 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1988774674 3318 KEKMQaiQEASRLKAEAEMLQKQKDlaQEQAQKLLEDKQLMQQRLEEE 3365
Cdd:cd16269 243 KEKME--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEE 286
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2479-2647 |
6.58e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2479 EKQKYTAESELKQLRDRA-AEAEKLRKL----AQDEAEKLRKQVSEETQKKR-----------QAEEELKRKSeaekEAA 2542
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAkKEAEAIKKEalleAKEEIHKLRNEFEKELRERRnelqklekrllQKEENLDRKL----ELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2543 KQKQKALEDLEKlRMQAEEAERQVKQAEIEK--EKQIKVAHEAAQksaaaelqskhMSFAEKTSKLEESLKQEhgavlqL 2620
Cdd:PRK12704 106 EKREEELEKKEK-ELEQKQQELEKKEEELEEliEEQLQELERISG-----------LTAEEAKEILLEKVEEE------A 167
|
170 180
....*....|....*....|....*..
gi 1988774674 2621 QQEAERLKKQQEdaENSREEAEKELEK 2647
Cdd:PRK12704 168 RHEAAVLIKEIE--EEAKEEADKKAKE 192
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4400-4433 |
6.62e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 6.62e-05
10 20 30
....*....|....*....|....*....|....
gi 1988774674 4400 LLEAQAASGFIVDPVRNQCLSVDEAVKSGVVGPE 4433
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
3167-3558 |
6.62e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.91 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3167 QADTEMAKHKKLAEQTL---KQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQR------GQVEEELFK 3237
Cdd:PRK11281 53 LLEAEDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3238 VKVQMEEllkLKNKIEEENQRLIkkdkdsTQKLLAEEA-----ENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRAL 3312
Cdd:PRK11281 133 TLDQLQN---AQNDLAEYNSQLV------SLQTQPERAqaalyANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQAL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3313 AEKMLKEKMQAIQEASRLKaeaEMLQKQKDLAQEQAQKLLEDKQLMQ-----QRLE--EETEEYHKSLEVERKRQLE--I 3383
Cdd:PRK11281 204 LNAQNDLQRKSLEGNTQLQ---DLLQKQRDYLTARIQRLEHQLQLLQeainsKRLTlsEKTVQEAQSQDEAARIQANplV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3384 MAEAERlRLQVSQ--LSEAQARAEEEAK--KFKKQADkvatRLHETEIATQEKMTVVE------RLEFER---LNTSKEA 3450
Cdd:PRK11281 281 AQELEI-NLQLSQrlLKATEKLNTLTQQnlRVKNWLD----RLTQSERNIKEQISVLKgslllsRILYQQqqaLPSADLI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3451 DDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKkieHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVk 3530
Cdd:PRK11281 356 EGLADRIADLRLEQFEINQQRDALFQPDAYIDKLEAG---HKSEVTDEVRDALLQLLDERRELLDQLNKQLNNQLNLAI- 431
|
410 420
....*....|....*....|....*...
gi 1988774674 3531 kakalkdEQERQKQQMEQEKKTLQATMD 3558
Cdd:PRK11281 432 -------NLQLNQQQLLSVSDSLQSTLT 452
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2491-2747 |
6.72e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2491 QLRDRAAEAEKLRKLAQDEAEKLRKQVSEetqkKRQAEEELKRKS-----EAEKEAAKQKQKALED-LEKLRMQAEEAER 2564
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQKNglvdlSEEAKLLLQQLSELESqLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2565 QVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKkqqedaensreeaeke 2644
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR---------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2645 lekwRQKANEALRLRLQAEDEAhkktlaqeeaekqkeeaereakKRAKAEESALKQkemaeeELERQRKIAESTAQQklt 2724
Cdd:COG3206 305 ----AQLQQEAQRILASLEAEL----------------------EALQAREASLQA------QLAQLEARLAELPEL--- 349
|
250 260
....*....|....*....|....
gi 1988774674 2725 aEQELIRLRADFDNAEQQ-RSLLE 2747
Cdd:COG3206 350 -EAELRRLEREVEVARELyESLLQ 372
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2695-2989 |
6.91e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2695 ESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKV 2774
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2775 RSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLA 2854
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2855 AISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQR 2934
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2935 RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKL 2989
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADL 342
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2802-3048 |
7.09e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2802 LLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEeAARQRAEAERILKEKLAAISEATRL--KTEAEIALKEKEAE--N 2877
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAelE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2878 ERLRRQAEDEAYQRKALEDQ--ASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRvveEEIRILKLNFEKASSGK 2955
Cdd:COG4942 90 KEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2956 LDLELELNKLKNIADETQQSKIRAEEEAEKLRKLAleeekrrREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEA 3035
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLL-------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|...
gi 1988774674 3036 RKQKDEADKEAEK 3048
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
2424-2837 |
7.47e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.69 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2424 DAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESEL--KQLRDRAAEAEK 2501
Cdd:COG5022 814 SYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELaeRQLQELKIDVKS 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2502 LRKLA----QDEAE--KLRKQVSEETQKKRQA-------EEELKRKSEAEKEAAKQKQKaLEDLEKLRMQ-------AEE 2561
Cdd:COG5022 894 ISSLKlvnlELESEiiELKKSLSSDLIENLEFkteliarLKKLLNNIDLEEGPSIEYVK-LPELNKLHEVesklketSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2562 AERQVKQAEIEKEKQIKVAHEAAQ-KSAAAELQSKHMSFAEKTSkleeSLKQEHGAVLQLQQEAERLKkqQEDAENSREE 2640
Cdd:COG5022 973 YEDLLKKSTILVREGNKANSELKNfKKELAELSKQYGALQESTK----QLKELPVEVAELQSASKIIS--SESTELSILK 1046
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2641 AEKELEKWRQKANEALRLRLQAEDEAhKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQ 2720
Cdd:COG5022 1047 PLQKLKGLLLLENNQLQARYKALKLR-RENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKL 1125
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2721 QKLTAEQELIRLRADF-DNAEQQRSLLEDELYRLKNEvaaaqqqrKQLEDELAKVRsemdiLIQLKTKAEKETMSNTEKS 2799
Cdd:COG5022 1126 NLLQEISKFLSQLVNTlEPVFQKLSVLQLELDGLFWE--------ANLEALPSPPP-----FAALSEKRLYQSALYDEKS 1192
|
410 420 430
....*....|....*....|....*....|....*...
gi 1988774674 2800 KQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEE 2837
Cdd:COG5022 1193 KLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEG 1230
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2466-2613 |
7.74e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 49.23 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2466 EEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE--AAK 2543
Cdd:pfam05262 199 DMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKqvAEN 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2544 QKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSaAAELQSKHMSFAEKTSKLEESLKQE 2613
Cdd:pfam05262 279 QKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDK-ELEAQKKREPVAEDLQKTKPQVEAQ 347
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2520-2837 |
7.86e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 48.82 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2520 ETQKKRQAE--EELKRKSEAEKEAAKQKQKALEDLEKlrmqaeeAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHM 2597
Cdd:PRK07735 8 EDLKKEAARraKEEARKRLVAKHGAEISKLEEENREK-------EKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2598 SFAEKTSklEESLKQEHGAVLQLQQEAERLKKQQEdaENSREEAEKELEKWRQKANEALRLRLQAedeahkktlaqeeae 2677
Cdd:PRK07735 81 GTEEVTE--EEKAKAKAKAAAAAKAKAAALAKQKR--EGTEEVTEEEKAAAKAKAAAAAKAKAAA--------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2678 kqkeeaerEAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQqrslleDELYRLKNEV 2757
Cdd:PRK07735 142 --------LAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTE------EEKAKAKAKA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2758 AAAQQQRKQledELAKvrsemdiliQLKTKAEKETMSNTEKSKQlleAEAAKMKdlAEEASRLRAISEEAKHQRQIAEEE 2837
Cdd:PRK07735 208 AAAAKAKAA---ALAK---------QKASQGNGDSGDEDAKAKA---IAAAKAK--AAAAARAKTKGAEGKKEEEPKQEE 270
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2685-2969 |
8.07e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2685 REAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQR 2764
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2765 KQLEDELAKVRSEMDIL------IQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQ--RQIAEE 2836
Cdd:COG4372 83 EELNEQLQAAQAELAQAqeelesLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEleEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2837 EAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSS 2916
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 2917 EAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIA 2969
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALEL 295
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2685-2908 |
8.48e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.45 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2685 REAKKRAKAEESALKQKEMAEE-----ELERQRKIAE-STAQQKLTAEQELirlrADFDNAEQQRSLLEDELYRLKNEVA 2758
Cdd:NF012221 1548 SKHAKQDDAAQNALADKERAEAdrqrlEQEKQQQLAAiSGSQSQLESTDQN----ALETNGQAQRDAILEESRAVTKELT 1623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2759 AAQQQRKQLEDE-------------------LAKVRSEMDiliqlktKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASR 2819
Cdd:NF012221 1624 TLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLD-------DAKKISGKQLADAKQRHVDNQQKVKDAVAKSEA 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2820 LRAISEeakHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKAledQAS 2899
Cdd:NF012221 1697 GVAQGE---QNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQA---DAK 1770
|
....*....
gi 1988774674 2900 QHKQEIEEK 2908
Cdd:NF012221 1771 GAKQDESDK 1779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2286-2518 |
8.59e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2286 AKAYIDTIKDYELQLVAYKAQVEPLVSPLKKTKldSASDNIIQEYVTLRTRYSELMTL---TSQYIKFITDTQRRLDDEE 2362
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALK--KEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2363 KAAEKLKAEERKKMAEMQAELdkQKQLAEAHAKAIAKAEKEAQELK-LKMQEEVSKREIAAVDAEKQKTNiqlELQELKN 2441
Cdd:COG4942 93 AELRAELEAQKEELAELLRAL--YRLGRQPPLALLLSPEDFLDAVRrLQYLKYLAPARREQAEELRADLA---ELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774674 2442 LSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKL-RKLAQDEAEKLRKQVS 2518
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiARLEAEAAAAAERTPA 245
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
2561-2811 |
8.88e-05 |
|
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: 47.89 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2561 EAERQvkqaEIEKEKQIKVAHEAAqksaaaELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREE 2640
Cdd:pfam17045 5 EAELQ----ELMKQIDIMVAHKKS------EWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2641 AEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKR--AKAEESALKQKEMAEEELERQRKIAEST 2718
Cdd:pfam17045 75 LVAKYEQQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRlnGKLEEFRQKSLEWEQQRLQYQQQVASLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2719 AQQKLTAEQ-ELIRLRADFDNAEQQRSLLED---ELYRLKNEVAAAQQQRKQLEDELAKVRSEMDIL------IQLKTKA 2788
Cdd:pfam17045 155 AQRKALAEQsSLIQSAAYQVQLEGRKQCLEAsqsEIQRLRSKLERAQDSLCAQELELERLRMRVSELgdsnrkLLEEQQR 234
|
250 260
....*....|....*....|...
gi 1988774674 2789 EKETMSNTEKSKQLLEAEAAKMK 2811
Cdd:pfam17045 235 LLEELRMSQRQLQVLQNELMELK 257
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
3349-3625 |
9.10e-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: 48.92 E-value: 9.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3349 QKLLEDKQLMQQRLEEEteEYHKSLEVERKRQLeiMAEAERLRLQVSQLSEAQARAEEEAKKFKkQADKVATRLHEteia 3428
Cdd:pfam05622 3 SEAQEEKDELAQRCHEL--DQQVSLLQEEKNSL--QQENKKLQERLDQLESGDDSGTPGGKKYL-LLQKQLEQLQE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3429 tqekmtvverlEFERLNTSKeaDDLRKAIADLENEKARLKKEAEELQNKSKEmadAQQKKIEHEktVLQQTfmteKEMLL 3508
Cdd:pfam05622 74 -----------ENFRLETAR--DDYRIKCEELEKEVLELQHRNEELTSLAEE---AQALKDEMD--ILRES----SDKVK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3509 KKEKLIEDEKKRLES-----------------------QFEEEVKKAKALKDEQERQKQQMEQekktLQATMDAALSKQK 3565
Cdd:pfam05622 132 KLEATVETYKKKLEDlgdlrrqvklleernaeymqrtlQLEEELKKANALRGQLETYKRQVQE----LHGKLSEESKKAD 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3566 EAEEEMLRKQKEMQELERqrlEQERILAEENQkLREKLQQLEDAQKDQHTRETDKVLHKD 3625
Cdd:pfam05622 208 KLEFEYKKLEEKLEALQK---EKERLIIERDT-LRETNEELRCAQLQQAELSQADALLSP 263
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
3188-3611 |
9.18e-05 |
|
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: 49.09 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3188 QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDST 3267
Cdd:pfam09730 38 ELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3268 QKLLAEEA--ENMRKLAEDAARLSVEAQEAARLRQIaeddlnqqralAEKMLKEKMQAIQEASRLKAeaemlqkqkDLAQ 3345
Cdd:pfam09730 118 QNQVEFEGlkHEITRKEEETELLNSQLEEAIRLREI-----------AERQLDEALETLKTEREQKN---------SLRK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3346 EQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLhet 3425
Cdd:pfam09730 178 ELSHYMTLNDFDYVSHLSISLDGLKFSEDEGAGTEPNNDGEAMDGGENGGGGLKNSGLDNRTSTPRKSEVFPPAPSL--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3426 eiatqekmtvVERLeFERLNTSkEADDLRKAIADLENEKARLKKEAEELQnksKEMADAQQKKIEHEKTVLQqtfMTEKE 3505
Cdd:pfam09730 255 ----------VSDL-LSELNIS-EIQKLKQQLIQVEREKVSLLSTLQESQ---KQLEQAKGALSEQQEKVNR---LTENL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3506 MLLKKeklIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEqekkTLQATMDAALSKQKEAEEEMLRKQKEMQELERQR 3585
Cdd:pfam09730 317 EAMRG---LQASKERQDALDSEKDRDSHEDGDYYEVDINGPE----ILECKYRVAVEEAGELREELKALKARYNTLEERY 389
|
410 420
....*....|....*....|....*.
gi 1988774674 3586 LEQERILAEENQKLREKLQQLEDAQK 3611
Cdd:pfam09730 390 KEEKTRWEAEAQDLAEKIRQLEKASH 415
|
|
| SH3_and_anchor |
TIGR04211 |
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
3188-3277 |
9.62e-05 |
|
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.
Pssm-ID: 275056 [Multi-domain] Cd Length: 198 Bit Score: 46.92 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3188 QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLknkiEEENQRLIKKDKDST 3267
Cdd:TIGR04211 70 ELQQELAELQEELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIKQISANAIEL----DEENRELREELAELK 145
|
90
....*....|
gi 1988774674 3268 QKLLAEEAEN 3277
Cdd:TIGR04211 146 QENEALEAEN 155
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2639-2991 |
9.77e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2639 EEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQkemAEEELERQRKIAEST 2718
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ---ARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2719 AQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEM--------DILIQLKTKAEK 2790
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIaereeelkELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2791 ETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIAL 2870
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2871 KEKEAENER-LRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFE 2949
Cdd:COG4372 246 EDKEELLEEvILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1988774674 2950 KASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLAL 2991
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
2701-2923 |
1.12e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.99 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2701 KEMAEEELERQRKIAESTAQQKLTAEQELIRLRADfdnAEQQRSLLEDELyRLKNEV-AAAQQQRKQLEDE-LAKVRSEM 2778
Cdd:pfam00038 49 YSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLA---AEDFRQKYEDEL-NLRTSAeNDLVGLRKDLDEAtLARVDLEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2779 DI------LIQLKTKAE---KETMSNTEKSKQLLEAEAAKMKDLAeeasrlRAISEeakhQRQIAEEEAARQRAEAERIL 2849
Cdd:pfam00038 125 KIeslkeeLAFLKKNHEeevRELQAQVSDTQVNVEMDAARKLDLT------SALAE----IRAQYEEIAAKNREEAEEWY 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2850 KEKLAAISEATRLKTEAEIALKEKEAENERL--RRQAEDEAY--QRKALEDQ--------ASQHKQ------EIEEKIVQ 2911
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTiqSLEIELQSLkkQKASLERQlaeteeryELQLADyqelisELEAELQE 274
|
250
....*....|..
gi 1988774674 2912 LKksseAEMERQ 2923
Cdd:pfam00038 275 TR----QEMARQ 282
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
1058-1155 |
1.13e-04 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 45.73 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1058 QKKTFTKWVN---------KHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 1124
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1988774674 1125 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1155
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
1064-1154 |
1.13e-04 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 44.60 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1064 KWVNKHLIKAQR---HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM---RFHKLQNVQIALDFLRhrQVKLVN-IRN 1136
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 1988774674 1137 DDIADGNPKLTLGLIWTI 1154
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2754-2932 |
1.18e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 48.86 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2754 KNEVAAAQQQRKQLEDElAKVRSEmdiLIQLKTKAEKEtmsntEKSKQLLEAEAakmKDLAEEAS-RLRAISEeakhqrq 2832
Cdd:PTZ00491 662 KSQEAAARHQAELLEQE-ARGRLE---RQKMHDKAKAE-----EQRTKLLELQA---ESAAVESSgQSRAEAL------- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2833 iAEEEAARQRAEAErilkeklaaiSEATRLKTEAEIALKEKEAENERLRRQAEdeayqrkaLEDQASQHKQEIEEKivql 2912
Cdd:PTZ00491 723 -AEAEARLIEAEAE----------VEQAELRAKALRIEAEAELEKLRKRQELE--------LEYEQAQNELEIAKA---- 779
|
170 180
....*....|....*....|....
gi 1988774674 2913 KKSSEAEMERQKAIVD----DTLK 2932
Cdd:PTZ00491 780 KELADIEATKFERIVEalgrETLI 803
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2353-2646 |
1.19e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 48.44 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2353 DTQRRLDD-EEKAAEKLKAEERKKMAEMQAElDKQKQLAEAHAKAIAKAEKEAQELklkmqEEVSKREIAAVDAEKQKTN 2431
Cdd:PRK07735 2 DPEKDLEDlKKEAARRAKEEARKRLVAKHGA-EISKLEEENREKEKALPKNDDMTI-----EEAKRRAAAAAKAKAAALA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2432 IQLELQELKNLSEQQIKDKSQQVDEAlhsrtkieeeirliRIQLETTEKQKYTAESELKQlRDRAAEAEKLRKLAQDEAE 2511
Cdd:PRK07735 76 KQKREGTEEVTEEEKAKAKAKAAAAA--------------KAKAAALAKQKREGTEEVTE-EEKAAAKAKAAAAAKAKAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2512 KLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVaheAAQKSAAAE 2591
Cdd:PRK07735 141 ALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAA---AAAKAKAAA 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2592 LQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKkqQEDAENSREEAEKELE 2646
Cdd:PRK07735 218 LAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAK--TKGAEGKKEEEPKQEE 270
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2420-2641 |
1.20e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2420 IAAVDAEKQKTNIQLELQELKNLSEQ---QIKDKSQQVDEAlhsrtkiEEEIRLIRIQLETTEKQKYTAESELKQLRDRA 2496
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAaqaELDALQAELEEL-------NEEYNELQAELEALQAEIDKLQAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2497 AEA-EKLRKLAQDEAEK------------------------LRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQkalED 2551
Cdd:COG3883 82 EERrEELGERARALYRSggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKL---AE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2552 LEKLRMQAEEAERQVKQAEIEKEKQIkvaheaaqksaaAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQ 2631
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALL------------AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
250
....*....|
gi 1988774674 2632 EDAENSREEA 2641
Cdd:COG3883 227 AAAAAAAAAA 236
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2237-2515 |
1.23e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2237 IADAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKK 2316
Cdd:COG1340 24 IEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2317 TKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKaEERKKMAEMQAELDKQKQLAEAHAKA 2396
Cdd:COG1340 104 LNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKAL-EKNEKLKELRAELKELRKEAEEIHKK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2397 IAKAEKEAQELKLKMQEEVSKREiaavdaekqktniqlELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLE 2476
Cdd:COG1340 183 IKELAEEAQELHEEMIELYKEAD---------------ELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
250 260 270
....*....|....*....|....*....|....*....
gi 1988774674 2477 TTEKQKYTAEselkqlrdRAAEAEKLRKLAQDEAEKLRK 2515
Cdd:COG1340 248 KLRKKQRALK--------REKEKEELEEKAEEIFEKLKK 278
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
2514-2653 |
1.40e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 46.62 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2514 RKQvsEETQKKRQAEEELKRKSEAEKEAAKQ--KQKALEDLEKlrmqaeeaerqvKQAEIEKEKQIKVAHEAAQKSAAAE 2591
Cdd:pfam13904 63 AKQ--RQRQKELQAQKEEREKEEQEAELRKRlaKEKYQEWLQR------------KARQQTKKREESHKQKAAESASKSL 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 2592 LQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSR--EEAEKELEKWRQKAN 2653
Cdd:pfam13904 129 AKPERKVSQEEAKEVLQEWERKKLEQQQRKREEEQREQLKKEEEEQErkQLAEKAWQKWMKNVK 192
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3421-3585 |
1.40e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3421 RLHETEIATQEKMTVVERLE--FERLNTSKEADDLRKAIADLENEKARLKKEAEELQnksKEMADAQQKKIEHEKTVLQQ 3498
Cdd:COG4913 259 ELAERYAAARERLAELEYLRaaLRLWFAQRRLELLEAELEELRAELARLEAELERLE---ARLDALREELDELEAQIRGN 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3499 TfmTEKEMLLKKE----KLIEDEKKRLESQFEEEVKKA-----------KALKDEQERQKQQMEQEKKTLQATMDAALSK 3563
Cdd:COG4913 336 G--GDRLEQLEREierlERELEERERRRARLEALLAALglplpasaeefAALRAEAAALLEALEEELEALEEALAEAEAA 413
|
170 180
....*....|....*....|..
gi 1988774674 3564 QKEAEEEMLRKQKEMQELERQR 3585
Cdd:COG4913 414 LRDLRRELRELEAEIASLERRK 435
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2366-2609 |
1.41e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2366 EKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQ 2445
Cdd:pfam02029 124 RLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRG 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2446 QIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTE---KQKYTAESELKQLRDRAAEAEklrklaQDEAEKLRkqvseetQ 2522
Cdd:pfam02029 204 HPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREeeaEVFLEAEQKLEELRRRRQEKE------SEEFEKLR-------Q 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2523 KKRQAE---EELKRKSEaekeaakQKQKALEDlEKLRMQAEEAERQVKqaEIEKEKQIKvaheaaqksaaAELQSKHMSF 2599
Cdd:pfam02029 271 KQQEAElelEELKKKRE-------ERRKLLEE-EEQRRKQEEAERKLR--EEEEKRRMK-----------EEIERRRAEA 329
|
250
....*....|
gi 1988774674 2600 AEKTSKLEES 2609
Cdd:pfam02029 330 AEKRQKLPED 339
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
1058-1165 |
1.57e-04 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 45.00 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1058 QKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 1124
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1988774674 1125 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 1165
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2323-2668 |
1.58e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2323 SDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEK 2402
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2403 EAQELKLKMQEEVSKREiaavDAEKQKTNIQLELQELknlsEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQK 2482
Cdd:COG4372 81 ELEELNEQLQAAQAELA----QAQEELESLQEEAEEL----QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2483 YTAESELKQLRDRAAEAEK-----LRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRM 2557
Cdd:COG4372 153 KELEEQLESLQEELAALEQelqalSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2558 QAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENS 2637
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
330 340 350
....*....|....*....|....*....|.
gi 1988774674 2638 REEAEKELEKWRQKANEALRLRLQAEDEAHK 2668
Cdd:COG4372 313 LEDALLAALLELAKKLELALAILLAELADLL 343
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2388-2587 |
1.58e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 48.10 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2388 QLAEAHAKAIAKAEKEAQELKLKMQEEVSkreiaavdaekqktniqlELQELKNLSEQQIKDKSQQVDEALHSRTKIEEE 2467
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREEELE------------------ELQEQLEDLESSIQELEKEIKKLESSIKQVEEE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2468 IRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLrKQVSEETQKKRQAE-EELKRKSEAEKEAAKQKQ 2546
Cdd:pfam05667 372 LEELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLiEEYRALKEAKSNKEDESQ 450
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1988774674 2547 KALEDLEKLRMQAEEAERQVKQAEiEKEKQIKVAHEAAQKS 2587
Cdd:pfam05667 451 RKLEEIKELREKIKEVAEEAKQKE-ELYKQLVAEYERLPKD 490
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2541-2731 |
1.62e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2541 AAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKekqikvaheAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQL 2620
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAEL---------AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2621 QQEAERLKKQQEDAENSRE----EAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEkqKEEAEREAKKRAKAEES 2696
Cdd:COG1579 72 EARIKKYEEQLGNVRNNKEyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE--LAELEAELEEKKAELDE 149
|
170 180 190
....*....|....*....|....*....|....*
gi 1988774674 2697 ALKQKEMAEEELERQRKIAESTAQQKLTAEQELIR 2731
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKIPPELLALYERIR 184
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
1162-1275 |
1.69e-04 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 44.41 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1162 DIQVNGQSEDMTAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKHYPRLINMGKVYQQTN-LENLEQAFSVA 1240
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQ---NKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKpVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774674 1241 EKDLGVTRLLDPEDVDVPHPDEKSIITYVSSLYDA 1275
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2726-2985 |
1.79e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2726 EQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQlktkaeketmsNTEKSKQLLEA 2805
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNE-----------KVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2806 EAAKMKDLAEEASRLRAISEE--------AKHQRQIAEEEAARQRA----EAERILKEKLAAIS---EATRLKTEAEIAL 2870
Cdd:COG1340 83 LNEKLNELREELDELRKELAElnkaggsiDKLRKEIERLEWRQQTEvlspEEEKELVEKIKELEkelEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2871 KEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDdtlKQRRVVEEEIRILKLNFEK 2950
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVE---AQEKADELHEEIIELQKEL 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1988774674 2951 AssgklDLELELNKLKNIADETQQSKIRAEEEAEK 2985
Cdd:COG1340 240 R-----ELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2144-2556 |
1.80e-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: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2144 AKLKKMRTEAEDeqpvfdsLEEELKKASAVSDKMVRVHSerdveldHFRQQLSSLQDRW-----KAVFTQIDLRQRELEq 2218
Cdd:COG3096 785 KRLEELRAERDE-------LAEQYAKASFDVQKLQRLHQ-------AFSQFVGGHLAVAfapdpEAELAALRQRRSELE- 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2219 lgRQLGYYResydwlirwiADAKQRQEKIQAvpitdsktLKEQLAQEKKLL------------EEIEQNKDKVDECQkYA 2286
Cdd:COG3096 850 --RELAQHR----------AQEQQLRQQLDQ--------LKEQLQLLNKLLpqanlladetlaDRLEELREELDAAQ-EA 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2287 KAYIDtikdyelQLVAYKAQVEPLVSPLKKTKLDSasDNIIQEYVTLrtrySELMTLTSQYIKFIT------------DT 2354
Cdd:COG3096 909 QAFIQ-------QHGKALAQLEPLVAVLQSDPEQF--EQLQADYLQA----KEQQRRLKQQIFALSevvqrrphfsyeDA 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2355 QRRLDDEEKAAEKLKAeerkKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqeevskreiAAVDAEKQktniql 2434
Cdd:COG3096 976 VGLLGENSDLNEKLRA----RLEQAEEARREAREQLRQAQAQYSQYNQVLASLK------------SSRDAKQQ------ 1033
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2435 ELQELKN-LSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAE-- 2511
Cdd:COG3096 1034 TLQELEQeLEELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqa 1113
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2512 KLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQ---KAL-------EDLEKLR 2556
Cdd:COG3096 1114 KAGWCAVLRLARDNDVERRLHRRELAYLSADELRSmsdKALgalrlavADNEHLR 1168
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2813-2986 |
1.89e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2813 LAEEASRLRAiSEEAKHQRQIAEEEAARQRAEAERI---LKEKLAAISEATRLKTEAEIALKEKEAENERLRrqaEDEAY 2889
Cdd:pfam07888 40 LQERAELLQA-QEAANRQREKEKERYKRDREQWERQrreLESRVAELKEELRQSREKHEELEEKYKELSASS---EELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2890 QRKALEDQASQHKQEIEE------KIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELN 2963
Cdd:pfam07888 116 EKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170 180
....*....|....*....|...
gi 1988774674 2964 KLKNIADETQQSKIRAEEEAEKL 2986
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDTITTL 218
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2496-2647 |
1.89e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2496 AAEAEKLRKLAQ---------DEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQV 2566
Cdd:COG1579 3 PEDLRALLDLQEldseldrleHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2567 K-----------QAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAE 2635
Cdd:COG1579 83 GnvrnnkeyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|..
gi 1988774674 2636 NSREEAEKELEK 2647
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2511-2704 |
1.92e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.69 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2511 EKLRKQVSEETQKKRQAEEELKRKSEaekEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAA 2590
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERESQ---EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2591 ELQSKHMSFAEKtSKLEESLKQEhgavlqlqqeaerLKKQQEDAENSREEAEKELEkwrQKANEALRLRLQAEDEAHKKT 2670
Cdd:pfam05262 261 PKPADTSSPKED-KQVAENQKRE-------------IEKAQIEIKKNDEEALKAKD---HKAFDLKQESKASEKEAEDKE 323
|
170 180 190
....*....|....*....|....*....|....
gi 1988774674 2671 LAQEEAEKQKEEAEREAKKRAKAEESALKQKEMA 2704
Cdd:pfam05262 324 LEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAID 357
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2799-2942 |
1.94e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2799 SKQLLEAEAAKMKDLAEEASRLRAISEEAKHQrqiAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENE 2878
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLE---AKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774674 2879 RLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKsseaEMERQKAIVDDTLKQR--RVVEEEIR 2942
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEAR 168
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3816-3852 |
1.97e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.97e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1988774674 3816 IRVLEAQLATGGIIDPINSHRVPTETAYKQGHYDAEM 3852
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4067-4102 |
2.26e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.26e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1988774674 4067 LNLLEAQAGTGYLVDPVHNQKYTVDEAVKAGVVGPE 4102
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5395-5432 |
2.26e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.26e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1988774674 5395 QRFLEVQYLTGGLIEPDVEGRVSIDESIRKGTIDARTA 5432
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2356-2520 |
2.44e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2356 RRLDDEEKAAEKLKAEERKKMAEMQAELDKQKqlaeahaKAIAKAEKEAQELKLKMQEevSKREIAAVDAEKQKTNIQLE 2435
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLE-------KEIKRLELEIEEVEARIKK--YEEQLGNVRNNKEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2436 LQELKnlseQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQkytAESELKQLRDRAAEAEKLRKLAQDEAEKLRK 2515
Cdd:COG1579 98 IESLK----RRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEELAELEAELEELEAEREELAA 170
|
....*
gi 1988774674 2516 QVSEE 2520
Cdd:COG1579 171 KIPPE 175
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
3322-3490 |
2.63e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.17 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3322 QAIQEASRLKAEAEmlqKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQlEIMAEAERLRLQVSQlseAQ 3401
Cdd:COG2268 196 EIIRDARIAEAEAE---RETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKA-EERREAETARAEAEA---AY 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3402 ARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEferlntskeADDLRKAIADLENEKARLKKEAEELQNKSKEM 3481
Cdd:COG2268 269 EIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELE---------ADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAE 339
|
....*....
gi 1988774674 3482 ADAQQKKIE 3490
Cdd:COG2268 340 AEGKRALAE 348
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2386-2577 |
2.81e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2386 QKQLAEAHAKaIAKAEKEAQELKLK-----MQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQ---QIKDKSQQVDEA 2457
Cdd:COG3206 181 EEQLPELRKE-LEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAlraQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2458 LHSRTKIEEEIRLIRIQLE-TTEKQKYTAES-ELKQLRDRAAEAEK-LRKLAQDEAEKLRKQVSEETQKK---RQAEEEL 2531
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAElAELSARYTPNHpDVIALRAQIAALRAqLQQEAQRILASLEAELEALQAREaslQAQLAQL 339
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1988774674 2532 KRKSEAEKEAAkQKQKALE-DLEKLRMQAEEAERQVKQAEIEKEKQI 2577
Cdd:COG3206 340 EARLAELPELE-AELRRLErEVEVARELYESLLQRLEEARLAEALTV 385
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4437-4468 |
2.86e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.86e-04
10 20 30
....*....|....*....|....*....|..
gi 1988774674 4437 KLLSAEKAVTGYKDPFTGNKISLFEAMQKDLI 4468
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2751-3066 |
2.95e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.25 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2751 YRL-KNEVAAAQQQRKQleDELAKVRSEMDILIQLKTKAEKEtmsntEKSKQLLEAEAAKMKD-LAEEASRLRAISEEAK 2828
Cdd:PRK05035 431 YRQaKAEIRAIEQEKKK--AEEAKARFEARQARLEREKAARE-----ARHKKAAEARAAKDKDaVAAALARVKAKKAAAT 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2829 HQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAedeayqRKALEDQASQhkqEIEEK 2908
Cdd:PRK05035 504 QPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKA------KKAAQQAANA---EAEEE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2909 IVQLKKSSEAEMERQKAivddtlkqrrvveeeiRILKLNFEKASSGKLDLELELNKlkniadetqqSKIRAEEEAEKLRK 2988
Cdd:PRK05035 575 VDPKKAAVAAAIARAKA----------------KKAAQQAASAEPEEQVAEVDPKK----------AAVAAAIARAKAKK 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2989 LALEEEKRRREAEEKvkkiaaaeeeaarqRKAALE-ELERLR-KKAEEARKQKDEADKEAE-KQIVVAQQAAQKCSAAEQ 3065
Cdd:PRK05035 629 AEQQANAEPEEPVDP--------------RKAAVAaAIARAKaRKAAQQQANAEPEEAEDPkKAAVAAAIARAKAKKAAQ 694
|
.
gi 1988774674 3066 Q 3066
Cdd:PRK05035 695 Q 695
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2622-2843 |
3.08e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.76 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2622 QEAERLKKQQEDAENSREEAEKELEkwrQKAnEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQK 2701
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLE---QQA-EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2702 EMAEEELERQRK-IAESTAQQKLTAEQELIRLRADFDNAEQQRsllEDELYRLKNEVAAAQQQRKQLEDELAKVRSEmdi 2780
Cdd:TIGR02794 126 AKQAAEAKAKAEaEAERKAKEEAAKQAEEEAKAKAAAEAKKKA---EEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE--- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 2781 liQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRA 2843
Cdd:TIGR02794 200 --AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2361-2628 |
3.19e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 46.90 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2361 EEKAAEKLKAEErkKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNiqlELQELK 2440
Cdd:PRK07735 38 EEENREKEKALP--KNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAA---ALAKQK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2441 NLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEklrklAQDEAEKLRKqvsee 2520
Cdd:PRK07735 113 REGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAA-----AKAKAAALAK----- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2521 tQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSfa 2600
Cdd:PRK07735 183 -QKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAKTKGAE-- 259
|
250 260 270
....*....|....*....|....*....|
gi 1988774674 2601 ektSKLEESLKQEHGAVLQ--LQQEAERLK 2628
Cdd:PRK07735 260 ---GKKEEEPKQEEPSVNQpyLNKYVEVIK 286
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3454-3586 |
3.82e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3454 RKAIADLENEKARLKKEAE-ELQNKSKEM-----ADAQQKKIEHEKTV---------LQQTFMTEKEMLLKKEKLIEDEK 3518
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKkEAEAIKKEAlleakEEIHKLRNEFEKELrerrnelqkLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774674 3519 KRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATmdAALSKQkEAEEEMLRKQKEMQELERQRL 3586
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI--SGLTAE-EAKEILLEKVEEEARHEAAVL 174
|
|
| 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 ... |
2835-2934 |
3.87e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 43.84 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2835 EEEAARQRAEAERILKEKLAAISEAtrlkteaEIALKEKEAENERLRRQAEDEAYQ-RKALEDQASQHkqeieekIVQLK 2913
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAALAEA-------EQQLKEARAEAQEIIENAKKRAEKlKEEIVAAAEAE-------AERII 97
|
90 100
....*....|....*....|.
gi 1988774674 2914 KSSEAEMERQKAIVDDTLKQR 2934
Cdd:pfam00430 98 EQAAAEIEQEKDRALAELRQQ 118
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
2463-2576 |
3.91e-04 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 46.13 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2463 KIEEEIRLIRIQLETtEKQKYTAESELKQLRDRAAEAEklRKLAQDEAEKLRkQVSEETQKKRQAEEE-LKRKSEAEKEA 2541
Cdd:cd03406 159 KIPEAIRRNYEAMEA-EKTKLLIAEQHQKVVEKEAETE--RKRAVIEAEKDA-EVAKIQMQQKIMEKEaEKKISEIEDEM 234
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774674 2542 AKQKQKALEDLE--KLRMQAEEAERQVKQAEIEKEKQ 2576
Cdd:cd03406 235 HLAREKARADAEyyRALREAEANKLKLTPEYLELKKY 271
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2619-2773 |
3.99e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2619 QLQQEAERLKKQQEDAENSREEAEKELEKWRQ--KANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 2696
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTelEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774674 2697 ALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQrslLEDELYRLKNEVAAAQQQRKQLEDELAK 2773
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKIPP 174
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
3231-3580 |
4.05e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.87 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3231 VEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAE------- 3303
Cdd:COG5185 188 LLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEqntdlrl 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3304 DDLNQQRALAEKMLKEKMQAIQEASRLKAE-AEMLQKQKDLA-----QEQAQKLLEDKQLMQQRLEEETEEYHKSLEVEr 3377
Cdd:COG5185 268 EKLGENAESSKRLNENANNLIKQFENTKEKiAEYTKSIDIKKateslEEQLAAAEAEQELEESKRETETGIQNLTAEIE- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3378 KRQLEIMAEAERLRLQVSQLSEAQARAEEEAK--KFKKQADKVATRLHETEIATQEKMTVVER-LEFERLNTSKEADDLR 3454
Cdd:COG5185 347 QGQESLTENLEAIKEEIENIVGEVELSKSSEEldSFKDTIESTKESLDEIPQNQRGYAQEILAtLEDTLKAADRQIEELQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3455 KAIADLENEKARLKKEAEELQNkskEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKA 3534
Cdd:COG5185 427 RQIEQATSSNEEVSKLLNELIS---ELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEK 503
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1988774674 3535 LKDEQERQKQQMEQEKKTLQATMDAALSKQKEA---EEEMLRKQKEMQE 3580
Cdd:COG5185 504 LRAKLERQLEGVRSKLDQVAESLKDFMRARGYAhilALENLIPASELIQ 552
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2161-2508 |
4.08e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2161 DSLEEELKKASAVSDKMVRVHserdvelDHFRQQLSSLQDRWKAVFTQIDLR--QRELEQLGRQLGYYREsydwlirwia 2238
Cdd:PRK04863 796 EELAERYATLSFDVQKLQRLH-------QAFSRFIGSHLAVAFEADPEAELRqlNRRRVELERALADHES---------- 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2239 daKQRQEKIQAvpitdsKTLKEQLAQEKKLL------------EEIEQNKDKVDECQKyAKAYIDtikdyelQLVAYKAQ 2306
Cdd:PRK04863 859 --QEQQQRSQL------EQAKEGLSALNRLLprlnlladetlaDRVEEIREQLDEAEE-AKRFVQ-------QHGNALAQ 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2307 VEPLVSPLKktkldsaSDNiiQEYVTLRTRYSELMTLTSQYIKFI---------------TDTQRRLDDEEKAAEKLKAe 2371
Cdd:PRK04863 923 LEPIVSVLQ-------SDP--EQFEQLKQDYQQAQQTQRDAKQQAfaltevvqrrahfsyEDAAEMLAKNSDLNEKLRQ- 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2372 erkKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKlkmqeevskreiAAVDAEKQktNIQLELQELKNL-------SE 2444
Cdd:PRK04863 993 ---RLEQAEQERTRAREQLRQAQAQLAQYNQVLASLK------------SSYDAKRQ--MLQELKQELQDLgvpadsgAE 1055
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 2445 QQIKDKSQQVDEALHS----RTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEK----LRKLAQD 2508
Cdd:PRK04863 1056 ERARARRDELHARLSAnrsrRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAgwcaVLRLVKD 1127
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2532-2943 |
4.20e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.57 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2532 KRKSEAEKEAAKQKQKALEDLEKLRMQAEE----AERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLE 2607
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEaeqkAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2608 ESLKQEHGAVLQLQQEAERLKKQQEDAENSREEA----EKELEKWRQKANEALRLRLQAE-DEAHKKTLAQEEAEKQKEE 2682
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAaaaeKEKAEEAKRKAEEEAKRKAEEErKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2683 AEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQ 2762
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2763 QRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQR 2842
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2843 AEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMER 2922
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGL 400
|
410 420
....*....|....*....|.
gi 1988774674 2923 QKAIVDDTLKQRRVVEEEIRI 2943
Cdd:COG3064 401 LGLRLDLGAALLEAASAVELR 421
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3469-3611 |
4.55e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3469 KEAEELQNKSKEMADAQQKKiehEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfEEEVKKAKALKDEQERQKQQMEQ 3548
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQR---KKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQAEEAAKQAALKQKQAEEA 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774674 3549 EKKTLQATMDAALSKQKEAEEemLRKQKEMQELERQRLEQERILAEENQKLRE---KLQQLEDAQK 3611
Cdd:PRK09510 138 AAKAAAAAKAKAEAEAKRAAA--AAKKAAAEAKKKAEAEAAKKAAAEAKKKAEaeaAAKAAAEAKK 201
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2489-2627 |
4.80e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.63 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2489 LKQLRDRAAEAEKLRKLAQDEAEKLRKQV------------SEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLR 2556
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAAlleakelllrerNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 2557 MQAEEAERQVKQAEIE-KEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQ-LQQEAERL 2627
Cdd:PRK12705 105 NQLEEREKALSARELElEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEeADLEAERK 177
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2602-2735 |
4.95e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 46.53 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2602 KTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAHKKtlAQEEAEKQKE 2681
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKE--DKQVAENQKR 281
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2682 EAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK-LTAEQELIRLRAD 2735
Cdd:pfam05262 282 EIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKeLEAQKKREPVAED 336
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
3253-3393 |
5.27e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.48 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3253 EEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDdlnQQRALAEKMLKEKMQAIQEASRLKa 3332
Cdd:pfam15709 356 EQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEE---RKQRLQLQAAQERARQQQEEFRRK- 431
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 3333 eaeMLQKQKDLAQEQAQKLLEDKQlMQQRLEEETEEyhkslevERKRQLEiMAEAERLRLQ 3393
Cdd:pfam15709 432 ---LQELQRKKQQEEAERAEAEKQ-RQKELEMQLAE-------EQKRLME-MAEEERLEYQ 480
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2838-3083 |
5.34e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2838 AARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSsE 2917
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL-R 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2918 AEMERQKAIVDDTLkqrRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQqskiraeEEAEKLRKLALEEEKRR 2997
Cdd:COG4942 97 AELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR-------EQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2998 REAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIED 3077
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
....*.
gi 1988774674 3078 SITQKK 3083
Cdd:COG4942 247 GFAALK 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3416-3616 |
5.49e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3416 DKVATRLHETEIATQEKMTVVERLEFERlNTSKEADDLRKAIADLE-NEKARLKKEAEelqnKSKEMADAQQKKIEHEKT 3494
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRRER-EKAERYQALLKEKREYEgYELLKEKEALE----RQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3495 vlqqtfmtekemllKKEKLIEDEKKRLESqfeeevkKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRK 3574
Cdd:TIGR02169 255 --------------KLTEEISELEKRLEE-------IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEK 313
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1988774674 3575 QKEMQELErqrlEQERILAEENQKLREKLQQLEDAQKDQHTR 3616
Cdd:TIGR02169 314 ERELEDAE----ERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3166-3298 |
5.56e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3166 QQADTEMAKHKKLAEQTLKQKF-----QVEQELTKVKLKLDETDKQ----KSVLDEELQRLKDEVDDAVKQRGQVEEELF 3236
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIhklrnEFEKELRERRNELQKLEKRllqkEENLDRKLELLEKREEELEKKEKELEQKQQ 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 3237 KVKVQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENmrKLAEDAARLSVEAQEAARL 3298
Cdd:PRK12704 125 ELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVEE--EARHEAAVLIKEIEEEAKE 184
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2237-2463 |
5.60e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2237 IADAKQRQEKIQAvpitdskTLKEQLAQEKKLLEEIEQNKDKVDECQKYAKAYIDTIKDYELQLVAYKAQVEPLVSPLKK 2316
Cdd:COG3883 25 LSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2317 TKLDSASDNII---QEYVTLRTRYSelmtltsqYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAH 2393
Cdd:COG3883 98 SGGSVSYLDVLlgsESFSDFLDRLS--------ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 2394 AKAI--AKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTK 2463
Cdd:COG3883 170 KAELeaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4361-4397 |
5.98e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.98e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1988774674 4361 KYLQGSSSIAGLYLEPTKEKLSIYQAMKKKLLRHNTG 4397
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
1193-1274 |
6.24e-04 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 42.67 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1193 RCDNFTTSWRDGKLFNAVIHKHYPRLIN---MGKVYQQTNLE-NLEQAFSVAEKdLGVTRLLDPEDVDVPHPDEksIITY 1268
Cdd:cd21218 32 RVTNFSSDLKDGEVYALLLHSLAPELCDkelVLEVLSEEDLEkRAEKVLQAAEK-LGCKYFLTPEDIVSGNPRL--NLAF 108
|
....*.
gi 1988774674 1269 VSSLYD 1274
Cdd:cd21218 109 VATLFN 114
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3020-3613 |
6.28e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3020 AALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDsitqkkLKEEyekakklakeae 3099
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ------LERE------------ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3100 aakekAEREAALLRQQAEEAERQKTAAEEEAANQAKAQEDAERLRKEAEfeaakraqaeaaalMQKQQADTEMAKHKKLA 3179
Cdd:COG4913 347 -----IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA--------------ALLEALEEELEALEEAL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3180 EQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRgqvEEELFKVKvqmeELLKLKNKiEEENQ-- 3257
Cdd:COG4913 408 AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD---EAELPFVG----ELIEVRPE-EERWRga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3258 ----------RLIKKDKD-----------------STQKL-LAEEAENMRKLAED--AARLSVEAQEAarlRQIAEDDLN 3307
Cdd:COG4913 480 iervlggfalTLLVPPEHyaaalrwvnrlhlrgrlVYERVrTGLPDPERPRLDPDslAGKLDFKPHPF---RAWLEAELG 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3308 QQRALA----EKMLKEKMQAIQEASRLKAEAEMLQK--QKDLAQE-----QAQKLLEDKQLMQQRLEEETEEYHKSLEvE 3376
Cdd:COG4913 557 RRFDYVcvdsPEELRRHPRAITRAGQVKGNGTRHEKddRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLE-A 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3377 RKRQLEIMAEAERLRLQVSQLSeaqaraeeeakkfkkqADKVATRLHETEIATQEKMtvVERLE-----FERLNtsKEAD 3451
Cdd:COG4913 636 LEAELDALQERREALQRLAEYS----------------WDEIDVASAEREIAELEAE--LERLDassddLAALE--EQLE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3452 DLRKAIADLENEKARLKKEAEELQnksKEMADAQQkKIEHEKTVLQQtfMTEKEMLLKKEKLieDEKKRLESQFEEEVKK 3531
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLE---KELEQAEE-ELDELQDRLEA--AEDLARLELRALL--EERFAAALGDAVEREL 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3532 AKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELER--QRLEQERiLAEENQKLREKLQQLEDA 3609
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLAllDRLEEDG-LPEYEERFKELLNENSIE 846
|
....
gi 1988774674 3610 QKDQ 3613
Cdd:COG4913 847 FVAD 850
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2685-3083 |
6.32e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2685 REAKKRAKAEESALKqkemAEEELERQRKiaestaqqKLTAEQE-LIRLRADFDNAEQQRSLLEDELYRLK---NEVAAA 2760
Cdd:PRK04863 276 RHANERRVHLEEALE----LRRELYTSRR--------QLAAEQYrLVEMARELAELNEAESDLEQDYQAASdhlNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2761 QQQRKQLEdelakvRSEMDILiQLKTKAEKETMSNTEKSKQLLEAEAAKmkDLAEEaSRLRAISEEAKHQRQIaeeEAAR 2840
Cdd:PRK04863 344 LRQQEKIE------RYQADLE-ELEERLEEQNEVVEEADEQQEENEARA--EAAEE-EVDELKSQLADYQQAL---DVQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2841 QRAEAERilkEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHK--QEIEEKIVQLKKSSEA 2918
Cdd:PRK04863 411 TRAIQYQ---QAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQaaHSQFEQAYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2919 EMERQKAivDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNK---LKNIADETQQSKIRAEEEAEKLRKLALEEEK 2995
Cdd:PRK04863 488 EVSRSEA--WDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2996 RRREAEEKVKKIAAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEkQIVVAQQAAQKCSAAEQQVQSVL--AQ 3073
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLRE-QSGEEFEDSQDVTEYMQQLLEREreLT 644
|
410
....*....|
gi 1988774674 3074 QIEDSITQKK 3083
Cdd:PRK04863 645 VERDELAARK 654
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
3217-3616 |
6.42e-04 |
|
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: 46.37 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3217 LKDEVDDAVKQRGQVEEELFKVKVQMEELLK---LKNKIEEENQRLIKKDKDSTQKLLAE-EAENMRKLAEDAARLSVEA 3292
Cdd:pfam12128 198 VKSMIVAILEDDGVVPPKSRLNRQQVEHWIRdiqAIAGIMKIRPEFTKLQQEFNTLESAElRLSHLHFGYKSDETLIASR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3293 QEAarlRQIAEDDLNQQRALAEKMLKEKMQAI-QEASRLKAEAEMLQKQKDLAQEQAQklledkqlmqQRLEEETEEYHk 3371
Cdd:pfam12128 278 QEE---RQETSAELNQLLRTLDDQWKEKRDELnGELSAADAAVAKDRSELEALEDQHG----------AFLDADIETAA- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3372 sleverkrqleimAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRlheTEIATQEKMTVVERLEfERLNTSKEAD 3451
Cdd:pfam12128 344 -------------ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRR---RSKIKEQNNRDIAGIK-DKLAKIREAR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3452 DLRKAIA--DLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLK--KEKLIEDEKKRLESQFEE 3527
Cdd:pfam12128 407 DRQLAVAedDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLenFDERIERAREEQEAANAE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3528 ------EVKKAKALKDEQERQKQQMEQEKKTLQATMDAA--------------LSKQKEAEEEMLRKQKEMQELERQ--- 3584
Cdd:pfam12128 487 verlqsELRQARKRRDQASEALRQASRRLEERQSALDELelqlfpqagtllhfLRKEAPDWEQSIGKVISPELLHRTdld 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 3585 -----------------RLEQERILAEE----NQKLREKLQQLEDAQKDQHTR 3616
Cdd:pfam12128 567 pevwdgsvggelnlygvKLDLKRIDVPEwaasEEELRERLDKAEEALQSAREK 619
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2355-2557 |
6.88e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.02 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2355 QRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREiaavdaekqktnIQL 2434
Cdd:COG2268 225 EAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAERE------------REI 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2435 ELQELKnlseqqikdksqqvdealhsrtKIEEEIRLIRIQLETTEKQKYTAESElkqlrdRAAEAEKLRKLAQDEAEKLR 2514
Cdd:COG2268 293 ELQEKE----------------------AEREEAELEADVRKPAEAEKQAAEAE------AEAEAEAIRAKGLAEAEGKR 344
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1988774674 2515 KQVseETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRM 2557
Cdd:COG2268 345 ALA--EAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITI 385
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2710-2936 |
7.12e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.09 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2710 RQRKiAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELyRLKnevAAAQQQRKQLEDE----LAKVRSEMDILIQLK 2785
Cdd:PRK05035 432 RQAK-AEIRAIEQEKKKAEEAKARFEARQARLEREKAAREA-RHK---KAAEARAAKDKDAvaaaLARVKAKKAAATQPI 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2786 TKAEKETMSNTEkskqllEAEAAKMKDLAEEASRLRAISEEAKHQRQiAEEEAARQRAEAERILKEKLAAISEATRLKTE 2865
Cdd:PRK05035 507 VIKAGARPDNSA------VIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKKAAQQAANAEAEEEVDPKK 579
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 2866 AEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDtlKQRRV 2936
Cdd:PRK05035 580 AAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDP--RKAAV 648
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3166-3319 |
7.14e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3166 QQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVK------ 3239
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3240 -VQME-ELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKML 3317
Cdd:COG1579 93 aLQKEiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
..
gi 1988774674 3318 KE 3319
Cdd:COG1579 173 PP 174
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2476-2897 |
7.14e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.80 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2476 ETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKL 2555
Cdd:COG3064 30 EAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2556 RMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAE 2635
Cdd:COG3064 110 AEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2636 NSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIA 2715
Cdd:COG3064 190 VEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2716 ESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSN 2795
Cdd:COG3064 270 GAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2796 TEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEA 2875
Cdd:COG3064 350 AAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGA 429
|
410 420
....*....|....*....|..
gi 1988774674 2876 ENERLRRQAEDEAYQRKALEDQ 2897
Cdd:COG3064 430 AGAVVALLVKLVADLAGGLVGI 451
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3462-3613 |
7.23e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3462 NEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKL--IEDEKKRLESQFEEEVKKAKALKDEQ 3539
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIraLEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3540 ERQKQQMEQEKKTLQ-----------------------ATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQER-ILAEE 3595
Cdd:COG4942 100 EAQKEELAELLRALYrlgrqpplalllspedfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERaELEAL 179
|
170
....*....|....*...
gi 1988774674 3596 NQKLREKLQQLEDAQKDQ 3613
Cdd:COG4942 180 LAELEEERAALEALKAER 197
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2866-3607 |
7.81e-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: 45.90 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2866 AEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILK 2945
Cdd:pfam07111 7 SDIPLVQSPGHQDVLERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQQAELISRQLQELRRLEEEVRLLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2946 lnfekassgkldlelelnklkniaDETQQSKIRAEEEAEKLRKLAleeekrrreaeekvkkiaaaeeeaaRQRKAALEEL 3025
Cdd:pfam07111 87 ------------------------ETSLQQKMRLEAQAMELDALA-------------------------VAEKAGQAEA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3026 ERLRKK---AEEARKQKDEAD-KEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDsiTQKKLKEeyekakklakeaeaa 3101
Cdd:pfam07111 118 EGLRAAlagAEMVRKNLEEGSqRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEG--LEKSLNS--------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3102 kekaereaaLLRQQAEEAERqktaaeeeaanQAKAQEDAERLRKEaefeaakraqaeaaalMQKQQADTEmakhkklAEQ 3181
Cdd:pfam07111 181 ---------LETKRAGEAKQ-----------LAEAQKEAELLRKQ----------------LSKTQEELE-------AQV 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3182 TLKQ---KFQVEQELTKVKLKLDETDKQKsvLDEELQRLKDEVDDAvkqrgQVEEELFKVKVQmeellklknkieeenqr 3258
Cdd:pfam07111 218 TLVEslrKYVGEQVPPEVHSQTWELERQE--LLDTMQHLQEDRADL-----QATVELLQVRVQ----------------- 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3259 likkdkDSTQKLLAEEAENMRKLAEDAarlSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQ 3338
Cdd:pfam07111 274 ------SLTHMLALQEEELTRKIQPSD---SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQ 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3339 KQ-KDLAQEQA--QKLLEDK--QLMQQRLEEET--EEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKF 3411
Cdd:pfam07111 345 EQvTSQSQEQAilQRALQDKaaEVEVERMSAKGlqMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRV 424
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3412 KKQADKVATRLHETEIATQEKMTV---------VERLEFERLNTSKEAD----DLRKAIADLENEKARLKKE----AEEL 3474
Cdd:pfam07111 425 EQAVARIPSLSNRLSYAVRKVHTIkglmarkvaLAQLRQESCPPPPPAPpvdaDLSLELEQLREERNRLDAElqlsAHLI 504
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3475 QN---KSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKK 3551
Cdd:pfam07111 505 QQevgRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVA 584
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 3552 TLQATMDAALSKQKEAEEEMLRKQ------------KEMQELERQ---RLEQERILAEENQKLREKLQQLE 3607
Cdd:pfam07111 585 EVETRLREQLSDTKRRLNEARREQakavvslrqiqhRATQEKERNqelRRLQDEARKEEGQRLARRVQELE 655
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3246-3385 |
7.92e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3246 LKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQ 3325
Cdd:PRK00409 497 LGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ 576
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 3326 EA-SRLKAEAEMLQKQKDLAQEQAQKLLEDKQL--MQQRLEEETEEYHKSLEVERKRQLEIMA 3385
Cdd:PRK00409 577 QAiKEAKKEADEIIKELRQLQKGGYASVKAHELieARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2533-2727 |
8.44e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2533 RKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKtsklEESLKQ 2612
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK----EENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2613 EHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEAL-RL-RLQAEdEAHKKTLaqeeaekqkeeaeREAKKR 2690
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELeRIsGLTAE-EAKEILL-------------EKVEEE 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 1988774674 2691 AKAEESAL-KQKEM-AEEELERQRKIAESTAQQKLTAEQ 2727
Cdd:PRK12704 167 ARHEAAVLiKEIEEeAKEEADKKAKEILAQAIQRCAADH 205
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2471-2570 |
8.47e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2471 IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLA-QDEAEKLRKqvsEETQKKRQAEEeLKRKSEAEKEAAKQKQKAL 2549
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAsFERLAELRD---ELAELEEELEA-LKARWEAEKELIEEIQELK 477
|
90 100
....*....|....*....|.
gi 1988774674 2550 EDLEKLRMQAEEAERQVKQAE 2570
Cdd:COG0542 478 EELEQRYGKIPELEKELAELE 498
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3165-3393 |
8.68e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3165 KQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFK-VKVQME 3243
Cdd:pfam13868 58 EEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREeIDEFNE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3244 ELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARlsvEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQA 3323
Cdd:pfam13868 138 EQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEE---KEREIARLRAQQEKAQDEKAERDELRAKLYQEE 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 3324 IQEASRLKAEAEMLQKQK---DLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQ 3393
Cdd:pfam13868 215 QERKERQKEREEAEKKARqrqELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMK 287
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
1823-1867 |
9.08e-04 |
|
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212702 [Multi-domain] Cd Length: 54 Bit Score: 40.33 E-value: 9.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1988774674 1823 IQAVCDFK---QQEITVHKGDECALLNNSQPFKWKVLNRSGHEAMVPS 1867
Cdd:cd11768 2 VVALYDFQpiePGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3781-3811 |
9.21e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 9.21e-04
10 20 30
....*....|....*....|....*....|.
gi 1988774674 3781 LLAERAVVGYKDPYTGGKISVFEAMKKGLIE 3811
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2490-2590 |
9.35e-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: 42.85 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2490 KQLRDRAAEAEKLRKlaqdEAEKLRKQVSEETQK-KRQAEEELKrksEAEKEAAKQKQKALEDLEklrmqaEEAERQVKQ 2568
Cdd:COG0711 34 EKIADGLAEAERAKE----EAEAALAEYEEKLAEaRAEAAEIIA---EARKEAEAIAEEAKAEAE------AEAERIIAQ 100
|
90 100
....*....|....*....|..
gi 1988774674 2569 AEIEKEKQIKVAHEAAQKSAAA 2590
Cdd:COG0711 101 AEAEIEQERAKALAELRAEVAD 122
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
3183-3642 |
9.75e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3183 LKQKFQVEQ-ELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFkvkvQMEELLKLKNKIEEEnqrliK 3261
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN----ELSSLEDMKNRYESE-----I 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3262 KDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQK 3341
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3342 DlAQEQAQKLLEDkqLMQQRLEEETEE-----YHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKK--- 3413
Cdd:PRK01156 339 N-DYIKKKSRYDD--LNNQILELEGYEmdynsYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNein 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3414 -------------QADKVATRLHETEIatQEKMTVVE-RLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSK 3479
Cdd:PRK01156 416 vklqdisskvsslNQRIRALRENLDEL--SRNMEMLNgQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3480 EMAD--AQQKKIEH-------EKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQK------- 3543
Cdd:PRK01156 494 DIDEkiVDLKKRKEyleseeiNKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKrtswlna 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3544 --QQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHT-RETDK 3620
Cdd:PRK01156 574 laVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKlRGKID 653
|
490 500
....*....|....*....|..
gi 1988774674 3621 VLHKDIIHLTTIETTKTVYNGQ 3642
Cdd:PRK01156 654 NYKKQIAEIDSIIPDLKEITSR 675
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1536-1630 |
9.76e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.55 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1536 LRYVQDLLAWVEENQRRIDNAEWGSDLPSMESQLGSHRGLHQTVEDFKSKIERAKADETQL---SPVSKGTYREYLGKLD 1612
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1988774674 1613 LQYGKLLNSSKSRLRNLE 1630
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3298-3489 |
1.02e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3298 LRQIAEDDLNQQRALAEKMLKEKmqaiqeasrlKAEAEMLQKQKDL-AQEQAQKLledkqlmQQRLEEETEEYHKSLEve 3376
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEA----------KKEAEAIKKEALLeAKEEIHKL-------RNEFEKELRERRNELQ-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3377 rkrQLEimaeaERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETE--IATQEKMTVVERLEFERLN--TSKEADD 3452
Cdd:PRK12704 86 ---KLE-----KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEkkEEELEELIEEQLQELERISglTAEEAKE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1988774674 3453 --LRKAIADLENEKARLKKEAEElqnKSKEMADAQQKKI 3489
Cdd:PRK12704 158 ilLEKVEEEARHEAAVLIKEIEE---EAKEEADKKAKEI 193
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
2383-2539 |
1.05e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 43.38 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2383 LDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQEL---KNLSEQQIKDKSQQVDEAlh 2459
Cdd:pfam08614 13 LDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELyrsRGELAQRLVDLNEELQEL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2460 srtkiEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEE--------L 2531
Cdd:pfam08614 91 -----EKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEKEnrelverwM 165
|
....*....
gi 1988774674 2532 KRKS-EAEK 2539
Cdd:pfam08614 166 KRKGqEAEA 174
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
3514-3595 |
1.07e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 42.21 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3514 IEDEKKRLES---QFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEM--LRKQKEMQELERQRLEQ 3588
Cdd:pfam20492 4 AEREKQELEErlkQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKerLEESAEMEAEEKEQLEA 83
|
....*..
gi 1988774674 3589 ERILAEE 3595
Cdd:pfam20492 84 ELAEAQE 90
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
2411-2664 |
1.09e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2411 MQEEVSKREIAAVDAEKQKTniqleLQELKNLSEQQIKDKSQQVD-----EALHSRTKIEEEIRLIRiQLETTEKqkyTA 2485
Cdd:PRK05771 2 APVRMKKVLIVTLKSYKDEV-----LEALHELGVVHIEDLKEELSnerlrKLRSLLTKLSEALDKLR-SYLPKLN---PL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2486 ESELKQLRDRaaEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKsEAEKEAAKqKQKALE-DLEKLRM------- 2557
Cdd:PRK05771 73 REEKKKVSVK--SLEELIKDVEEELEKIEKEIKELEEEISELENEIKEL-EQEIERLE-PWGNFDlDLSLLLGfkyvsvf 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2558 -------QAEEAERQVKQAEIEKEKQIK-------VAHEAAQKSAAAELQSkhMSFAEKTSKLEESLKQehgAVLQLQQE 2623
Cdd:PRK05771 149 vgtvpedKLEELKLESDVENVEYISTDKgyvyvvvVVLKELSDEVEEELKK--LGFERLELEEEGTPSE---LIREIKEE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1988774674 2624 AERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAED 2664
Cdd:PRK05771 224 LEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAE 264
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2831-3007 |
1.11e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2831 RQIAEEEAARQRAEAERILKEklaAISEATRLKTEAEIALKEkeaENERLRRQAEDEAYQRKA----LEDQASQHKQEIE 2906
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEE---AKKEAEAIKKEALLEAKE---EIHKLRNEFEKELRERRNelqkLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2907 EKIVQLKKSsEAEMERQKAIVDDTLKQRRVVEEEIRILKLnfekassgKLDLELE--------------LNKLKNIADET 2972
Cdd:PRK12704 100 RKLELLEKR-EEELEKKEKELEQKQQELEKKEEELEELIE--------EQLQELErisgltaeeakeilLEKVEEEARHE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1988774674 2973 QQSKIR-----AEEEAEKlrklaleeekrrreaeeKVKKI 3007
Cdd:PRK12704 171 AAVLIKeieeeAKEEADK-----------------KAKEI 193
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
769-949 |
1.14e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 45.48 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 769 AETLPSTDTRPLHEAAVKN------SPDMASGLTetnvslkMTLERMCSeeVRQAAAVLSEAPADKREVEPAllfaeKIK 842
Cdd:PRK14951 322 AALMPADETQLLYSICLHGraelglAPDEYAALT-------MVLLRLLA--FKPAAAAEAAAPAEKKTPARP-----EAA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 843 REAPKPETSSSVSEAPAAGELAS----AARALTAEPAAAQAQASplfereEPPKVAQHSAARAAECstEERLSVSEALKQ 918
Cdd:PRK14951 388 APAAAPVAQAAAAPAPAAAPAAAasapAAPPAAAPPAPVAAPAA------AAPAAAPAAAPAAVAL--APAPPAQAAPET 459
|
170 180 190
....*....|....*....|....*....|..
gi 1988774674 919 EGEKKRDLVE-DTPSATATPVTRPDQPHLRDT 949
Cdd:PRK14951 460 VAIPVRVAPEpAVASAAPAPAAAPAAARLTPT 491
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2507-2586 |
1.15e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.71 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2507 QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAK------QKQKALE-DLEKLRMQAEEAERQvkqaeiEKEKQIKV 2579
Cdd:PRK11448 148 QQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGlaaeleEKQQELEaQLEQLQEKAAETSQE------RKQKRKEI 221
|
....*..
gi 1988774674 2580 AHEAAQK 2586
Cdd:PRK11448 222 TDQAAKR 228
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
3449-3550 |
1.18e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3449 EADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKkeklIEDEKKRLESQFEEE 3528
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEE----IQELKEELEQRYGKI 487
|
90 100
....*....|....*....|..
gi 1988774674 3529 VKKAKALKDEQERQKQQMEQEK 3550
Cdd:COG0542 488 PELEKELAELEEELAELAPLLR 509
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
2500-2722 |
1.18e-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: 45.76 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2500 EKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQikv 2579
Cdd:TIGR00927 628 GDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEA--- 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2580 ahEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLR 2659
Cdd:TIGR00927 705 --DHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGE 782
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 2660 LQA-EDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQK 2722
Cdd:TIGR00927 783 IQAgEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAK 846
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
3329-3600 |
1.33e-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: 45.48 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3329 RLKAEAEMLQKQKDLaqEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEA 3408
Cdd:pfam05483 94 KVSIEAELKQKENKL--QENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3409 KKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEAddlrkaiadleneKARLKKEAEELQNKSKEMADAQQKK 3488
Cdd:pfam05483 172 KKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEM-------------HFKLKEDHEKIQHLEEEYKKEINDK 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3489 IEHEKTVLQQTfmTEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAE 3568
Cdd:pfam05483 239 EKQVSLLLIQI--TEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
250 260 270
....*....|....*....|....*....|..
gi 1988774674 3569 EEMLRKQKEMQELERQRLEQerilAEENQKLR 3600
Cdd:pfam05483 317 EDLQIATKTICQLTEEKEAQ----MEELNKAK 344
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3501-3616 |
1.37e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3501 MTEKEMLLKKEKlieDEKKRLESQFEEEVKKAKALKDEQERQ-KQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQ 3579
Cdd:pfam13868 28 IAEKKRIKAEEK---EEERRLDEMMEEERERALEEEEEKEEErKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMD 104
|
90 100 110
....*....|....*....|....*....|....*..
gi 1988774674 3580 ELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTR 3616
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAE 141
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2740-2876 |
1.38e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2740 EQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSemdiliqLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASR 2819
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEA-------LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1988774674 2820 LR--AISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEAE 2876
Cdd:PRK00409 578 AIkeAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
2509-2638 |
1.40e-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: 44.21 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2509 EAEKLRKQVSEETQK--KRQAEEELKR-KSEAEKEAakqkqkaleDLEKLRMQA--EEAERQVKQAEIEKEkqikvAHEA 2583
Cdd:cd03406 172 EAEKTKLLIAEQHQKvvEKEAETERKRaVIEAEKDA---------EVAKIQMQQkiMEKEAEKKISEIEDE-----MHLA 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2584 AQKSAAAelqskhmsfAEKTSKleesLKQEHGAVLQLQQEAERLKKQQEDAENSR 2638
Cdd:cd03406 238 REKARAD---------AEYYRA----LREAEANKLKLTPEYLELKKYQAIANNTK 279
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2716-2861 |
1.42e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.33 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2716 ESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEmdiLIQLKTKAEKETMSN 2795
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQ---LEQLQEKAAETSQER 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2796 TEKSKQLLEaEAAKMKDLAEEASR------LRAISEEAKHQR----QIAEEEAARQRAEAERILKE------------KL 2853
Cdd:PRK11448 215 KQKRKEITD-QAAKRLELSEEETRilidqqLRKAGWEADSKTlrfsKGARPEKGRNLAIAEWPTGKtgradyalfiglKP 293
|
....*...
gi 1988774674 2854 AAISEATR 2861
Cdd:PRK11448 294 VGVVEAKR 301
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
3162-3326 |
1.42e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.09 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3162 LMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQ 3241
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3242 MEELLKLKNKIEEENQRLIKKDKDSTQKLlaEEAENMRK---LAEDAARLSVEAQE--AARLRQIAEDDLNQQRALAEKM 3316
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNEL--YRVAGLTPeqaRKLLLKLLDAELEEekAQRVKKIEEEADLEAERKAQNI 181
|
170
....*....|
gi 1988774674 3317 LKEKMQAIQE 3326
Cdd:PRK12705 182 LAQAMQRIAS 191
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
3146-3465 |
1.45e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 44.67 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3146 EAEFEAAKRAQAEAAALMQKQQADTE-----MAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRLKDE 3220
Cdd:pfam19220 82 EGELEELVARLAKLEAALREAEAAKEelrieLRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3221 VDDAVKQRGQVEEELFKVKVQMEE----LLKLKNKIEEENQRLikkdkdstqkllaeeAENMRKLAEDAARLSVEAQEAA 3296
Cdd:pfam19220 162 LATARERLALLEQENRRLQALSEEqaaeLAELTRRLAELETQL---------------DATRARLRALEGQLAAEQAERE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3297 RLRQIAEDDLNQQRAlAEKMLKEKMQAIQE----ASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEyhks 3372
Cdd:pfam19220 227 RAEAQLEEAVEAHRA-ERASLRMKLEALTAraaaTEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAG---- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3373 LEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLhETEIATQEKMTVVERLEFERLNtskeadd 3452
Cdd:pfam19220 302 LEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASL-SDRIAELTKRFEVERAALEQAN------- 373
|
330
....*....|...
gi 1988774674 3453 lRKAIADLENEKA 3465
Cdd:pfam19220 374 -RRLKEELQRERA 385
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3442-3619 |
1.46e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3442 ERLNTSKEADDLRKAIADLEN-----EKARLKKEA-EELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIE 3515
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealEDAREQIELlEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3516 DEkkrlesqfEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEA-EEEMLRKQKEMQELERQRLEQER---- 3590
Cdd:COG4913 299 EL--------RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEAllaa 370
|
170 180 190
....*....|....*....|....*....|....*....
gi 1988774674 3591 ----------ILAEENQKLREKLQQLEDAQKDQHTRETD 3619
Cdd:COG4913 371 lglplpasaeEFAALRAEAAALLEALEEELEALEEALAE 409
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2335-2572 |
1.53e-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: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2335 TRYSELMtltSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEahakaiaKAEKEAQELkLKMQEE 2414
Cdd:cd16269 44 AHYEEQM---EQRVQLPTETLQELLDLHAACEKEALEVFMKRSFKDEDQKFQKKLME-------QLEEKKEEF-CKQNEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2415 VSK-------REIAAVDAEKQKTNI-------QLELQELKNLSE--QQIKDKSQQVDEALH----SRTKIEEEIRLIRIQ 2474
Cdd:cd16269 113 ASSkrcqallQELSAPLEEKISQGSysvpggyQLYLEDREKLVEkyRQVPRKGVKAEEVLQeflqSKEAEAEAILQADQA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2475 LETTEKQKytaeselKQLRDRAAEAEKLRKLAQDEAEKLRKQVseETQKKRQAE--EELKRKSEAEKE-AAKQKQKALED 2551
Cdd:cd16269 193 LTEKEKEI-------EAERAKAEAAEQERKLLEEQQRELEQKL--EDQERSYEEhlRQLKEKMEEEREnLLKEQERALES 263
|
250 260
....*....|....*....|...
gi 1988774674 2552 L--EKLRMQAEEAERQVKQAEIE 2572
Cdd:cd16269 264 KlkEQEALLEEGFKEQAELLQEE 286
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4810-4843 |
1.54e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.54e-03
10 20 30
....*....|....*....|....*....|....
gi 1988774674 4810 LEAQTATGGIIDPEFQFHLPTDVAMQRGYINKET 4843
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
3434-3613 |
1.60e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.86 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3434 TVVERLEFERLNTSKE----------ADDLRK--------AIADLENEK-----------ARLKKEAEELQN---KSKEM 3481
Cdd:COG2268 135 AVAAQMTVEELNEDREkfaekvqevaGTDLAKnglelesvAITDLEDENnyldalgrrkiAEIIRDARIAEAeaeRETEI 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3482 ADAQQKKIEHEKTVLQQTfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAK---ALKDEQERQKQQMEQEKKTLQATMD 3558
Cdd:COG2268 215 AIAQANREAEEAELEQER---EIETARIAEAEAELAKKKAEERREAETARAEaeaAYEIAEANAEREVQRQLEIAERERE 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3559 AALsKQKEAEEEMLRKQKEMQ---ELERQRLEQE------------RILAEENQKLREKLQQLEDAQKDQ 3613
Cdd:COG2268 292 IEL-QEKEAEREEAELEADVRkpaEAEKQAAEAEaeaeaeairakgLAEAEGKRALAEAWNKLGDAAILL 360
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2242-2546 |
1.61e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.00 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2242 QRQEKIQAVPITDSKTLKEQLAQ-EKKLLE-EIEQNKDKVDECQKYakayiDTIKDYELQLVAYKAQVeplvSPLKKTKL 2319
Cdd:NF033838 158 QKEEDRRNYPTNTYKTLELEIAEsDVEVKKaELELVKEEAKEPRDE-----EKIKQAKAKVESKKAEA----TRLEKIKT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2320 D--SASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAE------LDKQKQLAE 2391
Cdd:NF033838 229 DreKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGEEtlpspsLKPEKKVAE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2392 AHaKAIAKAEKeaqelKLKMQEEVSKR------------EIAAVDAEKQKTNIQLELQELKnlsEQQIKDKSQQVDEALH 2459
Cdd:NF033838 309 AE-KKVEEAKK-----KAKDQKEEDRRnyptntyktlelEIAESDVKVKEAELELVKEEAK---EPRNEEKIKQAKAKVE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2460 SRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEA-----EKLRKQVSEETQKKRQAEEELKRK 2534
Cdd:NF033838 380 SKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKpapkpEKPAEQPKAEKPADQQAEEDYARR 459
|
330
....*....|..
gi 1988774674 2535 SEAEKEAAKQKQ 2546
Cdd:NF033838 460 SEEEYNRLTQQQ 471
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
2445-2556 |
1.68e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.
Pssm-ID: 214019 [Multi-domain] Cd Length: 161 Bit Score: 42.38 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2445 QQIKDKSQQVDEALHSRTKIEEEIRL-----------IRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQdeAEKL 2513
Cdd:cd12926 15 QQYQDKSREYDQLYEEYTRTSQELQMkrtaieafnetIKIFEEQGQTQEKCSKEYLERFRREGNEKEMQRILLN--SERL 92
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1988774674 2514 RKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLR 2556
Cdd:cd12926 93 KSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKPDLMQLR 135
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
1031-1161 |
1.75e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 41.51 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1031 EVDWDHSLGEPEEKtwpnfiederdrvqkKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVL---------SGET 1101
Cdd:cd21330 2 DIDWSSIEGETREE---------------RTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPP 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 1102 LPREKGRMRfhKLQNVQIALDFLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 1161
Cdd:cd21330 65 YPKLGENMK--KLENCNYAVELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4362-4400 |
1.75e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.85 E-value: 1.75e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1988774674 4362 YLQGSSSIAGLYLEPTKEKLSIYQAMKKKLLRHNTGLSL 4400
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
2494-2578 |
1.77e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 44.10 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2494 DRAAEAEKLRKLAQDEAEKLRKQVSEETQKkrQAEEElkrKSEAEKEAAKQKQKALEDLEKLRMQAEEaerQVKQAEIEK 2573
Cdd:pfam07946 246 DKLAKRAKLRPEALKKAKKTREEEIEKIKK--AAEEE---RAEEAQEKKEEAKKKEREEKLAKLSPEE---QRKYEEKER 317
|
....*
gi 1988774674 2574 EKQIK 2578
Cdd:pfam07946 318 KKEQR 322
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
351-793 |
1.91e-03 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 44.57 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 351 VTNVSATAANDQVKPQQVTSTGSVKEAKRKVNKELIK----ATEVKAPPVSAAskiindkaeKVTDAA---ATQETAKVK 423
Cdd:pfam17823 21 APADPRHFVLNKMWNGAGKQNASGDAVPRADNKSSEQ*nfcAATAAPAPVTLT---------KGTSAAhlnSTEVTAEHT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 424 PHsATNKPKGSTNE-VKDSKTDEVPlevTTTQKSSTLEVKSTITTTTlAAPLTNAEDAQPITAKAAEMTAEEKKTNSKAI 502
Cdd:pfam17823 92 PH-GTDLSEPATREgAADGAASRAL---AAAASSSPSSAAQSLPAAI-AALPSEAFSAPRAAACRANASAAPRAAIAAAS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 503 PP-VGKEAPKGSVQEPTVKVQDESESTQPPQNAVT-----TEVLKETTQAVEGGSKSKrkkkksqAEALKSVESVegSPE 576
Cdd:pfam17823 167 APhAASPAPRTAASSTTAASSTTAASSAPTTAASSapatlTPARGISTAATATGHPAA-------GTALAAVGNS--SPA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 577 NKTELRPVASSEPLIVSTCSK--GTKKNEAKLHTDGEKTEDVPKQITAYSEETSLPLGQIPAAPLVEGQIKEKSEESNAG 654
Cdd:pfam17823 238 AGTVTAAVGTVTPAALATLAAaaGTVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVSTDQPVH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 655 KIAQGPlSPKgESNVTsphMEPVNPEEITVTkvetvtvqKMSGVELMQASPKSKQENPAP-LSEPQKPTIEAKSPmntek 733
Cdd:pfam17823 318 NTAGEP-TPS-PSNTT---LEPNTPKSVAST--------NLAVVTTTKAQAKEPSASPVPvLHTSMIPEVEATSP----- 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 734 ATQ-EPLKGKKKGKGRKQPKEPESevINTNPVPLTEaetlpSTDTRPLHEAAVKnSPDMAS 793
Cdd:pfam17823 380 TTQpSPLLPTQGAAGPGILLAPEQ--VATEATAGTA-----SAGPTPRSSGDPK-TLAMAS 432
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
3426-3547 |
1.94e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3426 EIATQ----EKMTVVERLEFErlntSKEADDLRKAIADLENEKAR---LKKEAE----ELQNKSKEMADAQQK--KIEHE 3492
Cdd:PTZ00491 658 EITTKsqeaAARHQAELLEQE----ARGRLERQKMHDKAKAEEQRtklLELQAEsaavESSGQSRAEALAEAEarLIEAE 733
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 3493 KTVlQQTFMTEKEMLLKKEKLIEDEKKRLE-------SQFEEEVKKAKALKD-EQERQKQQME 3547
Cdd:PTZ00491 734 AEV-EQAELRAKALRIEAEAELEKLRKRQEleleyeqAQNELEIAKAKELADiEATKFERIVE 795
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
3338-3570 |
1.97e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3338 QKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLE--IMAEAERLRLQVSQLSeaqaraeeeakkfKKQA 3415
Cdd:PRK05035 441 IEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAKDKdaVAAALARVKAKKAAAT-------------QPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3416 DKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKE-------------MA 3482
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEeevdpkkaavaaaIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3483 DAQQKKIEHEKTVLQQTFMTEKEMLLK--------KEKLIEDEKKRLESQFEEE----------VKKAKALKDEQERQKQ 3544
Cdd:PRK05035 588 RAKAKKAAQQAASAEPEEQVAEVDPKKaavaaaiaRAKAKKAEQQANAEPEEPVdprkaavaaaIARAKARKAAQQQANA 667
|
250 260
....*....|....*....|....*...
gi 1988774674 3545 QMEQEKKTLQATMDAALS--KQKEAEEE 3570
Cdd:PRK05035 668 EPEEAEDPKKAAVAAAIAraKAKKAAQQ 695
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
2413-2570 |
1.99e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2413 EEVSKREIAAVDAEKQKTNIQLELQELKNLS--EQQIKDKSQQVDEalhsrtkIEEEIRLIRIQLETTEKQKYTAESELK 2490
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHEERELTeeEEEIRRLEEQVER-------LEAEVEELEAELEEKDERIERLERELS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2491 QLRDRA-AEAEKLRKLA--QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQA-EEAERQV 2566
Cdd:COG2433 452 EARSEErREIRKDREISrlDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEAiRRLEEEY 531
|
....
gi 1988774674 2567 KQAE 2570
Cdd:COG2433 532 GLKE 535
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
1057-1159 |
2.04e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 41.52 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1057 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLRHRQVKLV 1132
Cdd:cd21337 20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
|
90 100
....*....|....*....|....*..
gi 1988774674 1133 NIRNDDIADGNPKLTLGLIWTIILHFQ 1159
Cdd:cd21337 100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
1060-1152 |
2.05e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 44.55 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1060 KTFTKWVNKHLIKAQrhVTDLYEDLRDGHNLISLLEVLSGE---TLPREKGR-------MRFHKLQNVQIALDFLRHRQV 1129
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100
....*....|....*....|...
gi 1988774674 1130 KLVNIRNDDIADGNpKLTLGLIW 1152
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVW 481
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
3117-3285 |
2.12e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 44.75 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3117 EEAERQKTAAEEEAANQAKAQEDAERLRKEAEFEAAKRAQAEAAALMQ-KQQADTEMAKHKKLAEQT---LKQKFQVEQE 3192
Cdd:COG1193 521 EELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKaREEAEEILREARKEAEELireLREAQAEEEE 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3193 LTKVKLKLDETDKQksvLDEELQRLKD-----------EVDDAVK-----QRGQVEEE-----------LFKVKVQMEEL 3245
Cdd:COG1193 601 LKEARKKLEELKQE---LEEKLEKPKKkakpakppeelKVGDRVRvlslgQKGEVLEIpkggeaevqvgILKMTVKLSDL 677
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1988774674 3246 LKLKNKIEEENQRLIKKDKDSTQKLLAEEAE-NMR-KLAEDA 3285
Cdd:COG1193 678 EKVEKKKPKKPKKRPAGVSVSVSKASTVSPElDLRgMRVEEA 719
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2523-2613 |
2.14e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 41.65 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2523 KKRQA--EEELKRKSEAEKEAAKQKQKALEDLEKLRmqaEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFA 2600
Cdd:cd06503 29 DEREEkiAESLEEAEKAKEEAEELLAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIE 105
|
90
....*....|...
gi 1988774674 2601 EKTSKLEESLKQE 2613
Cdd:cd06503 106 QEKEKALAELRKE 118
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
1051-1155 |
2.20e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 41.28 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1051 EDERdrvqkKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGETL-------PREKGRM--RFH 1112
Cdd:cd21294 5 EDER-----REFTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIdervlnkPPRKNKPlnNFQ 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1988774674 1113 KLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1155
Cdd:cd21294 80 MIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3138-3350 |
2.21e-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: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3138 EDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVKLKLDETDKQKSVLDEELQRL 3217
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3218 KdevdDAVKQRGQVEEELFKVK----VQMEELLKLKNKIEEENQRLIKKDKDSTQKLLAEEAEnmrkLAEDAARLSVEAQ 3293
Cdd:COG4942 110 L----RALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE----LEAERAELEALLA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774674 3294 EAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQK 3350
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3409-3589 |
2.25e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.03 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3409 KKFKKQADKVATRLHETEIATQEKmtvVERLEFERLntskEADDLRKAIADLENEKARLKKEAEELQNKSKEM----ADA 3484
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQER---LKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAakakAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3485 QQK-------KIEHEKTVLQQTFMTEKEMLLKKEKLIEDEKKRLESQfeeevKKAKALKDEQERQKQQMEQEKKTLQATM 3557
Cdd:PRK09510 152 EAKraaaaakKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAE-----AKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
170 180 190
....*....|....*....|....*....|..
gi 1988774674 3558 DAALSKQKEAEEEMLRKQKEMQELERQRLEQE 3589
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2622-2845 |
2.25e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.03 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2622 QEAERLKKQQEDAENSREEAEKELEkwrQKANEalrlrLQAEDEAHkktlaqeeaekqkeeaeRE-----AKKRAKAEES 2696
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQ---QQAEE-----LQQKQAAE-----------------QErlkqlEKERLAAQEQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2697 ALKQKEMAEEELERQRKIAESTAQQ----KLTAEQELIRLRADFDNAEQQrslledelyrlKNEVAAAQQQRKQLEDELA 2772
Cdd:PRK09510 117 KKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAAKKAAAE-----------AKKKAEAEAAKKAAAEAKK 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 2773 KVRSEMdiliqlKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEA 2845
Cdd:PRK09510 186 KAEAEA------AAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2383-2555 |
2.29e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2383 LDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNiqLELQELKNLSEQQIKDKSQQVDEAlhsrt 2462
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEAR--REREELQREEERLVQKEEQLDARA----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2463 kieEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEaeKLRKLAQDEAEKLRKQVSEETQKKrqAEEELKrkseaeKEAA 2542
Cdd:PRK12705 98 ---EKLDNLENQLEEREKALSARELELEELEKQLDN--ELYRVAGLTPEQARKLLLKLLDAE--LEEEKA------QRVK 164
|
170
....*....|...
gi 1988774674 2543 KQKQKALEDLEKL 2555
Cdd:PRK12705 165 KIEEEADLEAERK 177
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
3244-3397 |
2.32e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.62 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3244 ELLKLKNKIEEENQRlikkdkdstQKLLAEEAENmrklaedaarLSVEAQEAARlrqiaeddlnqqrALAEkmlkekmqA 3323
Cdd:PTZ00491 684 ERQKMHDKAKAEEQR---------TKLLELQAES----------AAVESSGQSR-------------AEAL--------A 723
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774674 3324 IQEASRLKAEAEMLQKQkdlAQEQAQKLLEDKQLMQQRLEEETE-EYHKS---LEVERKRQLEiMAEAERLRLQVSQL 3397
Cdd:PTZ00491 724 EAEARLIEAEAEVEQAE---LRAKALRIEAEAELEKLRKRQELElEYEQAqneLEIAKAKELA-DIEATKFERIVEAL 797
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
2493-2570 |
2.44e-03 |
|
Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.
Pssm-ID: 459956 [Multi-domain] Cd Length: 136 Bit Score: 41.56 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2493 RDRAAEAEKLRKLA---QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALedLEKLRMQAEEAERQVKQA 2569
Cdd:pfam00836 57 RRKSLEAQKLKQLAekrEKEEEALQKADEENNNFSKMAEEKLKQKMEAYKENREAQIAAL--KEKLKEKEKHVEEVRKNK 134
|
.
gi 1988774674 2570 E 2570
Cdd:pfam00836 135 E 135
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2601-2702 |
2.48e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2601 EKTSKLEESLKQEHGAVLQLQQEAERLKKQQED-AENSREEAEKELEKWRQKANEALRlrlQAEDEAHK--KTLAQEEAE 2677
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEkKEKLQEEEDKLLEEAEKEAQQAIK---EAKKEADEiiKELRQLQKG 599
|
90 100
....*....|....*....|....*
gi 1988774674 2678 KQKEEAEREAKKRAKAEESALKQKE 2702
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKE 624
|
|
| Mcm10 |
pfam09332 |
Mcm10 replication factor; Mcm10 is a eukaryotic DNA replication factor that regulates the ... |
2497-2611 |
2.53e-03 |
|
Mcm10 replication factor; Mcm10 is a eukaryotic DNA replication factor that regulates the stability and chromatin association of DNA polymerase alpha.
Pssm-ID: 462760 Cd Length: 349 Bit Score: 43.98 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2497 AEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQ 2576
Cdd:pfam09332 133 AEAAKLAAIAKLKAKGGVLEKEDPNAVKRKRSDSGEIKERVEKNLESSSSSSPDEEEPALKKRREQLAYLKSEEFQKILN 212
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774674 2577 IKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLK 2611
Cdd:pfam09332 213 AKSKHTGELKEAEAEMQERYFEPLVKKEQMEEKMR 247
|
|
| PLEC |
smart00250 |
Plectin repeat; |
5285-5318 |
2.56e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.56e-03
10 20 30
....*....|....*....|....*....|....
gi 1988774674 5285 EETGPVAGILDIDTLEKVSVTEAIHRNLVDNITG 5318
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
2358-2656 |
2.57e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.46 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2358 LDDEEKAAEKLKAEERKKMAEMQAELDK-QKQLAEAHAKAIAKAEKEAQELKLKMQEEvskreiaaVDAEKQKTNIQLEL 2436
Cdd:PLN03229 413 VDPERKVNMKKREAVKTPVRELEGEVEKlKEQILKAKESSSKPSELALNEMIEKLKKE--------IDLEYTEAVIAMGL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2437 QE-LKNLSEQQIKDKSQqvDEALHSRTKIEEEIRLIRIQLETTEKQKYTAeseLKQLRDRAAEAEKLRKLAQ--DEAEKL 2513
Cdd:PLN03229 485 QErLENLREEFSKANSQ--DQLMHPVLMEKIEKLKDEFNKRLSRAPNYLS---LKYKLDMLNEFSRAKALSEkkSKAEKL 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2514 RKQVSEETqKKRQAEEELKRKSEAEK-EAAKQKQKALEDLEK-LRMQAEEA--ERQVKQAEIEKEKQIKVAHEAAQKSAA 2589
Cdd:PLN03229 560 KAEINKKF-KEVMDRPEIKEKMEALKaEVASSGASSGDELDDdLKEKVEKMkkEIELELAGVLKSMGLEVIGVTKKNKDT 638
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988774674 2590 AElQSKHMSFAEKTSKLEESLKQEHGAVLQ---LQQEAERLKKQQEDAENSREEAEKE-LEKWRQKANEAL 2656
Cdd:PLN03229 639 AE-QTPPPNLQEKIESLNEEINKKIERVIRssdLKSKIELLKLEVAKASKTPDVTEKEkIEALEQQIKQKI 708
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2917-3484 |
2.61e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.35 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2917 EAEMERQKAI---VDDTLKQRRVVEEEIRILKLNfeKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEE 2993
Cdd:pfam05557 1 RAELIESKARlsqLQNEKKQMELEHKRARIELEK--KASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2994 EKRRREAEEKVKKIAAAEEEAA-----------------RQRKAALEELERLRKKAEEARKQKDEADK---EAEKQIVVA 3053
Cdd:pfam05557 79 RLKKKYLEALNKKLNEKESQLAdarevisclknelselrRQIQRAELELQSTNSELEELQERLDLLKAkasEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3054 QQAAQKCSAAEQQVQSV---LAQQIEDSITQKKLKEEyekakklakeaeaaKEKAEREAALLRQQAEEAERQKTAAEEEA 3130
Cdd:pfam05557 159 EKQQSSLAEAEQRIKELefeIQSQEQDSEIVKNSKSE--------------LARIPELEKELERLREHNKHLNENIENKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3131 ANQAKAQEDAERLRKEAEfeaakraqaeaaalMQKQQADTEMAKHKKLAEQTLKQKFQVEQELTKVK-----LKLDETDK 3205
Cdd:pfam05557 225 LLKEEVEDLKRKLEREEK--------------YREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpedlsRRIEQLQQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3206 QKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKLKNKIEEENQRLIKKDKDSTQ-----KLLAEEAENMRK 3280
Cdd:pfam05557 291 REIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKerdgyRAILESYDKELT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3281 LAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQ--------EQAQKLL 3352
Cdd:pfam05557 371 MSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADpsyskeevDSLRRKL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3353 EDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQADKVATRLHETEiATQEK 3432
Cdd:pfam05557 451 ETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLE-DDLEQ 529
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 3433 MTVVERLEFERLNtsKEADDLRKaiaDLENEKARLKKEAEELQNKSKEMADA 3484
Cdd:pfam05557 530 VLRLPETTSTMNF--KEVLDLRK---ELESAELKNQRLKEVFQAKIQEFRDV 576
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
2692-2859 |
2.68e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 43.43 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2692 KAEESALKQKEMAEEELerQRKIAESTAQQkltAEQELIRLRADfdnAEQQRSLLEDElyrlknevAAAQQQRKQLEDEL 2771
Cdd:pfam12037 46 KALELMKKQEQTRQAEL--QAKIKEYEAAQ---EQLKIERQRVE---YEERRKTLQEE--------TKQKQQRAQYQDEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2772 AKVRSEMDILIQLKTKAE-----------KETMSNTEKSKQLLEAEAakmkDLAEEASRLRAISE-EAK-HQRQIAEE-- 2836
Cdd:pfam12037 110 ARKRYQDQLEAQRRRNEEllrkqeesvakQEAMRIQAQRRQTEEHEA----ELRRETERAKAEAEaEARaKEERENEDln 185
|
170 180
....*....|....*....|....
gi 1988774674 2837 -EAARQRAEAERilKEKLAAISEA 2859
Cdd:pfam12037 186 lEQLREKANEER--ETVLESINTA 207
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2339-2645 |
2.75e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2339 ELMTLTSQYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELdkqKQLAEAHAKAIAKaEKEAQELKLKMQEEvsKR 2418
Cdd:pfam07888 45 ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEEL---RQSREKHEELEEK-YKELSASSEELSEE--KD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2419 EIAAVDAEKQktniqlelQELKNLsEQQIKDKSQQVDEalhsrtkIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAE 2498
Cdd:pfam07888 119 ALLAQRAAHE--------ARIREL-EEDIKTLTQRVLE-------RETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2499 AEK-LRKLAQD-------------EAEKLRKQVSEETQKKRQAEeelkrKSEAEKEAAKQKQKALEDLEKLRMQAEEA-E 2563
Cdd:pfam07888 183 TEEeLRSLSKEfqelrnslaqrdtQVLQLQDTITTLTQKLTTAH-----RKEAENEALLEELRSLQERLNASERKVEGlG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2564 RQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSK---------LEESLKQEHGAVLQLQQEAERLKKQQEDA 2634
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRarwaqeretLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330
....*....|.
gi 1988774674 2635 ENSREEAEKEL 2645
Cdd:pfam07888 338 RMEREKLEVEL 348
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
3440-3622 |
2.75e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3440 EFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMAdaQQKKI----EHEKTVLQQTFMTEKEMLLKKEKLIE 3515
Cdd:COG3206 160 AYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR--QKNGLvdlsEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3516 DEKKR--LESQFEEEVKKAKALKdeQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILA 3593
Cdd:COG3206 238 AEARLaaLRAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180
....*....|....*....|....*....
gi 1988774674 3594 EENQKLREKLQQLEDAQKDQHTRETDKVL 3622
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLA 344
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
2740-2905 |
2.76e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 41.58 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2740 EQQRSLLEDELYRLKNEVAaaqqqRKQLEDELAKVRSEMDILIQLKTKAEKETMsntekskqlleaeaakMKDLAEEASR 2819
Cdd:pfam15346 2 EAESKLLEEETARRVEEAV-----AKRVEEELEKRKDEIEAEVERRVEEARKIM----------------EKQVLEELER 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2820 LRAISEEAKHQRqiaEEEAARQRAEAERILKEKLAAISEATRLKTEAEIALKEKEaenerlrRQAEDEAYQRKALEDQAS 2899
Cdd:pfam15346 61 EREAELEEERRK---EEEERKKREELERILEENNRKIEEAQRKEAEERLAMLEEQ-------RRMKEERQRREKEEEERE 130
|
....*.
gi 1988774674 2900 QHKQEI 2905
Cdd:pfam15346 131 KREQQK 136
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2504-2922 |
2.78e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.41 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2504 KLAQDEAEKLRKQVS------EETQKkrQAEEELKRKSEAEKEAAKQKQKALEDLEKL------------RMQAEEAERQ 2565
Cdd:PRK10246 194 KSARTELEKLQAQASgvalltPEQVQ--SLTASLQVLTDEEKQLLTAQQQQQQSLNWLtrldelqqeasrRQQALQQALA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2566 VKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEK-- 2643
Cdd:PRK10246 272 AEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNtw 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2644 --ELEKWRQKANEALRLRL----QAEDEAHKKTLAQEEAEKQkeeaereaKKRAKAEESALkqkEMAEEELERQRkiAES 2717
Cdd:PRK10246 352 laEHDRFRQWNNELAGWRAqfsqQTSDREQLRQWQQQLTHAE--------QKLNALPAITL---TLTADEVAAAL--AQH 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2718 TAQQKLtaEQELIRLRAdfdnaeqQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEM----DILIQLKTKAEKE-T 2792
Cdd:PRK10246 419 AEQRPL--RQRLVALHG-------QIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYkektQQLADVKTICEQEaR 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2793 MSNTEKSKQLLEA---------------EAAKMKDLAEEASRLRAISEEAKhqrQIAEEEAA-------------RQRAE 2844
Cdd:PRK10246 490 IKDLEAQRAQLQAgqpcplcgstshpavEAYQALEPGVNQSRLDALEKEVK---KLGEEGAAlrgqldaltkqlqRDESE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2845 AERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAY-----QRKALEDQASQHKQEI---EEKIVQLKKSS 2916
Cdd:PRK10246 567 AQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQlrllsQRHELQGQIAAHNQQIiqyQQQIEQRQQQL 646
|
....*.
gi 1988774674 2917 EAEMER 2922
Cdd:PRK10246 647 LTALAG 652
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2705-2925 |
2.88e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2705 EEELERQRKIAESTAQQKLTAEQELI-RLRADfdNAEQQRslLEDELYRLKNEVAAAQQQRKQLEDElaKVRSEMDILIQ 2783
Cdd:pfam15709 310 ESEEERSEEDPSKALLEKREQEKASRdRLRAE--RAEMRR--LEVERKRREQEEQRRLQQEQLERAE--KMREELELEQQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2784 LKTKAEKETMSNTEKSKQLLEAEAAKmKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKlaaiseatRLK 2863
Cdd:pfam15709 384 RRFEEIRLRKQRLEEERQRQEEEERK-QRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEK--------QRQ 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 2864 TEAEIALKEkeaENERLRRQAEDE--AYQRKaledqasqhKQEIEEKIVQlkkssEAEMERQKA 2925
Cdd:pfam15709 455 KELEMQLAE---EQKRLMEMAEEErlEYQRQ---------KQEAEEKARL-----EAEERRQKE 501
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
2373-2541 |
2.88e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 42.57 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2373 RKKMAEmqaeldkqKQLAEAHAKA---IAKAEKEAQELK----LKMQEEVSKREiaaVDAEKQKTNIQLELQELKNL--- 2442
Cdd:pfam12072 21 RKSIAE--------AKIGSAEELAkriIEEAKKEAETKKkealLEAKEEIHKLR---AEAERELKERRNELQRQERRllq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2443 SEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLEttEKQKYTAESELKQLrdraAEAEKLRKLAQDEAEK-LRKQVSEET 2521
Cdd:pfam12072 90 KEETLDRKDESLEKKEESLEKKEKELEAQQQQLE--EKEEELEELIEEQR----QELERISGLTSEEAKEiLLDEVEEEL 163
|
170 180
....*....|....*....|....*
gi 1988774674 2522 QKK-----RQAEEELKRksEAEKEA 2541
Cdd:pfam12072 164 RHEaavmiKEIEEEAKE--EADKKA 186
|
|
| SH3_Eps8 |
cd11764 |
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ... |
1832-1867 |
2.90e-03 |
|
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar proteins; This group is composed of Eps8 and Eps8-like proteins including Eps8-like 1-3, among others. These proteins contain N-terminal Phosphotyrosine-binding (PTB), central SH3, and C-terminal effector domains. Eps8 binds either Abi1 (also called E3b1) or Rab5 GTPase activating protein RN-tre through its SH3 domain. With Abi1 and Sos1, it becomes part of a trimeric complex that is required to activate Rac. Together with RN-tre, it inhibits the internalization of EGFR. The SH3 domains of Eps8 and similar proteins recognize peptides containing a PxxDY motif, instead of the classical PxxP motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212698 [Multi-domain] Cd Length: 54 Bit Score: 38.78 E-value: 2.90e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1988774674 1832 QEITVHKGDECALLNNSQPFkWKVLNRSGHEAMVPS 1867
Cdd:cd11764 14 KELSVLKGEYLEVLDDSRQW-WKVRNSRGQVGYVPH 48
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
2813-2911 |
3.03e-03 |
|
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex
Pssm-ID: 339878 [Multi-domain] Cd Length: 104 Bit Score: 40.50 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2813 LAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKE---KLAAISEATRLKTEAEIALKEKEAenerlRRQAEDEAy 2889
Cdd:pfam16999 7 LSELAEREAALDQQIEAARKEAEREVEAAEAEAARILREaeaKAKALQAEYRQELAAETARIREEA-----RARAEAEA- 80
|
90 100
....*....|....*....|..
gi 1988774674 2890 qrKALEDQASQHKQEIEEKIVQ 2911
Cdd:pfam16999 81 --QAVRTRAEGRLQQAVELILR 100
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2639-2893 |
3.06e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2639 EEAE-KELEKWRQKANEAlRLRLQA-----EDEAhkktlaqeeaekqkeeAEREAKKRAKAEESALKQKEMAEEELERQR 2712
Cdd:PRK05035 434 AKAEiRAIEQEKKKAEEA-KARFEArqarlEREK----------------AAREARHKKAAEARAAKDKDAVAAALARVK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2713 kiaestAQQKLTAEQELIRLRADFDNAE-----QQRSLLEDELYRLKNEVAAAQQQRKQLEDELAkvRSEMDILIQLKTK 2787
Cdd:PRK05035 497 ------AKKAAATQPIVIKAGARPDNSAviaarEARKAQARARQAEKQAAAAADPKKAAVAAAIA--RAKAKKAAQQAAN 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2788 AEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAISEATRLKT--- 2864
Cdd:PRK05035 569 AEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKaav 648
|
250 260 270
....*....|....*....|....*....|
gi 1988774674 2865 EAEIA-LKEKEAENERLRRQAEDEAYQRKA 2893
Cdd:PRK05035 649 AAAIArAKARKAAQQQANAEPEEAEDPKKA 678
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1195-1272 |
3.13e-03 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 39.98 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1195 DNFTTSWRDGKLFNAVIHK------HYPRLInmgkvyQQTNLENLEQAFSvAEKDLGVTRLLDPEDVDVPHPDEKSIITY 1268
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNAlggsvpGWPNLD------PEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAY 92
|
....
gi 1988774674 1269 VSSL 1272
Cdd:cd21185 93 AAQL 96
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2607-2841 |
3.21e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.79 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2607 EESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQaedeahkktlaqeeaekqkeeaere 2686
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQ------------------------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2687 akkraKAEESALKQkemaeEELERQRKIAESTAQQKLTAEQELIRLRAdfdnAEQQRSLLEDELYRlkneVAAAQQQRKQ 2766
Cdd:pfam15709 395 -----RLEEERQRQ-----EEEERKQRLQLQAAQERARQQQEEFRRKL----QELQRKKQQEEAER----AEAEKQRQKE 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774674 2767 LEDELA---KVRSEMDILIQLKTKAEKEtmsnTEKSKQLLEAEAAKMKdlAEEASRLraISEEAKHQRQiaeeEAARQ 2841
Cdd:pfam15709 457 LEMQLAeeqKRLMEMAEEERLEYQRQKQ----EAEEKARLEAEERRQK--EEEAARL--ALEEAMKQAQ----EQARQ 522
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
2785-2887 |
3.29e-03 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 44.15 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2785 KTKaeKETMSNT-EKSKqLLEAEAAKMKDLAEE------------ASRLRAISEEAKHQRQIAEEEAARQRAEAE--RIL 2849
Cdd:pfam04147 162 KSK--KEVMEEViAKSK-LHKYERQKAKEEDEElreeldkelkdlRSLLSGSKRPKPEQAKKPEEKPDRKKPDDDydKLV 238
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1988774674 2850 KE----KLAAISEatRLKTEAEIALKEKE----AENERLRR-QAEDE 2887
Cdd:pfam04147 239 RElafdKRAKPSD--RTKTEEELAEEEKErlekLEEERLRRmRGEED 283
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
3211-3366 |
3.32e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 44.21 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3211 DEELQRLKDEVDDAVkQRGQVEEELFKvkvQMEELlklknkieeenqrlikkdKDSTQKLLAEEAENMRKLAEDAARLSV 3290
Cdd:pfam13779 488 ERRLRAAQERLSEAL-ERGASDEEIAK---LMQEL------------------REALDDYMQALAEQAQQNPQDLQQPDD 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3291 EAQEAAR-------LRQIAEDDLNQQRALAEKMLKEkMQAIQEasRLKAeAEMlQKQKDLAQEQAQKLLEDKQLM---QQ 3360
Cdd:pfam13779 546 PNAQEMTqqdlqrmLDRIEELARSGRRAEAQQMLSQ-LQQMLE--NLQA-GQP-QQQQQQGQSEMQQAMDELGDLlreQQ 620
|
....*.
gi 1988774674 3361 RLEEET 3366
Cdd:pfam13779 621 QLLDET 626
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
244-530 |
3.39e-03 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 43.80 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 244 TSSAPAQTAalkqdvSQTALTSSRTALPLAVAAVAEATGAAASKIPAKPSAPKTNEEMKTKDRPNIAEE--QTSMKPTQM 321
Cdd:pfam17823 111 ASRALAAAA------SSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPapRTAASSTTA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 322 ITSKPVLTMLPDFDAKEdkmKMAVVDPVKVTNVSATAAndqVKPQQVTST---GSVKEAKRKVNKELIKATEVKAPPVSA 398
Cdd:pfam17823 185 ASSTTAASSAPTTAASS---APATLTPARGISTAATAT---GHPAAGTALaavGNSSPAAGTVTAAVGTVTPAALATLAA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 399 AskiindkAEKVTDAAATQETAkvKPHSATNKPKGSTNEVKDSKTDEVPL----EVTTTQKSSTLEVKSTITTTTLAAPL 474
Cdd:pfam17823 259 A-------AGTVASAAGTINMG--DPHARRLSPAKHMPSDTMARNPAAPMgaqaQGPIIQVSTDQPVHNTAGEPTPSPSN 329
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774674 475 TNAEdaqPITAKAAEMTAEEKKTNSKAippVGKEAPKGSVQEPTVKVQDESESTQP 530
Cdd:pfam17823 330 TTLE---PNTPKSVASTNLAVVTTTKA---QAKEPSASPVPVLHTSMIPEVEATSP 379
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2770-3087 |
3.47e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2770 ELAKVRSEMDILIQLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERIL 2849
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2850 KEKLAAISEATRLKTEAEialkEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLK--KSSEAEMERQKAIV 2927
Cdd:COG4372 94 AELAQAQEELESLQEEAE----ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKelEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2928 DDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEKRRREAEEKVKKI 3007
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3008 AAAEEEAARQRKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSVLAQQIEDSITQKKLKEE 3087
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
3460-3629 |
3.47e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.95 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3460 LENEKARLKKEAEELQNKSKEMADAQQKKIE-----HEKTVLQQTFMTEKEMLLKKEKLIEDE--KKRLESQ--FEEEVK 3530
Cdd:cd16269 108 KQNEEASSKRCQALLQELSAPLEEKISQGSYsvpggYQLYLEDREKLVEKYRQVPRKGVKAEEvlQEFLQSKeaEAEAIL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3531 KAKALKDEQERQKQqmEQEKKTLQATMDAALSKQKEAEEEMLRKQ-----KEMQELERQRLEQER--ILAEENQKLREKL 3603
Cdd:cd16269 188 QADQALTEKEKEIE--AERAKAEAAEQERKLLEEQQRELEQKLEDqersyEEHLRQLKEKMEEERenLLKEQERALESKL 265
|
170 180
....*....|....*....|....*.
gi 1988774674 3604 QQLEDAQKDQHtRETDKVLHKDIIHL 3629
Cdd:cd16269 266 KEQEALLEEGF-KEQAELLQEEIRSL 290
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3322-3636 |
3.50e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3322 QAIQEASRLKAEAEMLQKQKDLAQEQAQKL---LEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEAERLRLQVSQLS 3398
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLeeeLEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3399 EAQARAEEEAKKFKKQADKVATRLHETEIATQEKMTVVERLEFERLNTSKEADDLRK-----AIADLENEKARLKKEAEE 3473
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelqalSEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3474 LQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEKLIED------EKKRLESQFEEEVKKAKALKDEQERQKQQME 3547
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAlldaleLEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3548 QEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKDII 3627
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
....*....
gi 1988774674 3628 HLTTIETTK 3636
Cdd:COG4372 355 VLELLSKGA 363
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2464-2554 |
3.50e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.31 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2464 IEEEIRLIRIQLETTEKQKYTAESELKQLRDR----AAEAEKLRKLAQDEAEKLRKqvseetQKKRQAEEELKR-KSEAE 2538
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKlaeaRAEAAEIIAEARKEAEAIAE------EAKAEAEAEAERiIAQAE 102
|
90
....*....|....*.
gi 1988774674 2539 KEAAKQKQKALEDLEK 2554
Cdd:COG0711 103 AEIEQERAKALAELRA 118
|
|
| iSH2_PIK3R1 |
cd12924 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
2445-2575 |
3.55e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 1, PIK3R1, also called p85alpha; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In addition, p85alpha, also called PIK3R1, contains N-terminal SH3 and GAP domains. p85alpha carry functions independent of its PI3K regulatory role. It can independently stimulate signaling pathways involved in cytoskeletal rearrangements. Insulin-sensitive tissues express splice variants of the PIK3R1 gene, p50alpha and p55alpha, which may play important roles in insulin signaling during lipid and glucose metabolism. Mice deficient with PIK3R1 die perinatally, indicating its importance in development.
Pssm-ID: 214017 [Multi-domain] Cd Length: 161 Bit Score: 41.60 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2445 QQIKDKSQQVDEALHSRTKIEEEIRLIRIQLET-TEKQKYTAESELKQLRDRAAEAEKLRKLAQDEA--------EKLRK 2515
Cdd:cd12924 15 TQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAfNETIKIFEEQCQTQERYSKEYIEKFKREGNEKEiqrimhnyEKLKS 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2516 QVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEK 2575
Cdd:cd12924 95 RISEIVDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKK 154
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2507-2766 |
3.66e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2507 QDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAeRQVKQAEIEKEKQIKvaheaAQK 2586
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQEL-REKRDELNEKVKELK-----EER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2587 SAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEA 2666
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2667 HKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAE--EELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRS 2744
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIElyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260
....*....|....*....|..
gi 1988774674 2745 LLEDELYRLKNEVAAAQQQRKQ 2766
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEK 262
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
3480-3598 |
3.77e-03 |
|
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.
Pssm-ID: 434558 [Multi-domain] Cd Length: 154 Bit Score: 41.32 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3480 EMADAQQKKIEHEKTVLQQtfMTEKEmllkKEKLIEDEKKRLESQFEEEvkkakALKDEQERQKQQMEQEKKtlqatmda 3559
Cdd:pfam15236 46 ERERKRQKALEHQNAIKKQ--LEEKE----RQKKLEEERRRQEEQEEEE-----RLRREREEEQKQFEEERR-------- 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1988774674 3560 alsKQKEAEEEMLRKQKEM-QELER-----QRLEQERILAEENQK 3598
Cdd:pfam15236 107 ---KQKEKEEAMTRKTQALlQAMQKaqelaQRLKQEQRIRELAEK 148
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
3165-3387 |
3.82e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3165 KQQADTEMAKHKKLAEQ--TLKQKF-QVEQELTKVKLKLDETDKQKSVLDEELQRLKDEVDDAVKQRGQVEeelfKVKVQ 3241
Cdd:COG1340 42 AEKRDELNAQVKELREEaqELREKRdELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSID----KLRKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3242 MEELL-KLKNKI---EEENQrLIKKDKDSTQKLlaEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKML 3317
Cdd:COG1340 118 IERLEwRQQTEVlspEEEKE-LVEKIKELEKEL--EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELH 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3318 KEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEYHKSLEVERKRQLEIMAEA 3387
Cdd:COG1340 195 EEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEE 264
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3332-3570 |
3.84e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3332 AEAEMLQKQKDL--AQEQAQKLLEDKQLMQQRLEEETEEYhKSLEVERKrqlEIMAEAERLRLQVSQLSeaqaraeeeaK 3409
Cdd:COG3883 14 ADPQIQAKQKELseLQAELEAAQAELDALQAELEELNEEY-NELQAELE---ALQAEIDKLQAEIAEAE----------A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3410 KFKKQADKVATRLHeteiATQEKMTVVERLEFerLNTSKEADDLRKAIADLENEKARLKKEAEELQnkskemadAQQKKI 3489
Cdd:COG3883 80 EIEERREELGERAR----ALYRSGGSVSYLDV--LLGSESFSDFLDRLSALSKIADADADLLEELK--------ADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3490 EHEKTVLQQtfmtEKEMLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEE 3569
Cdd:COG3883 146 EAKKAELEA----KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
.
gi 1988774674 3570 E 3570
Cdd:COG3883 222 A 222
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
3511-3611 |
3.94e-03 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 43.88 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3511 EKLIEDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLqATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQER 3590
Cdd:pfam14817 65 DKGKAESRQSAAARRLELQKEIERLRAEISRLDKQLEARELEL-SREEAERERALDEISDSRHRQLLLEAYDQQCEEARK 143
|
90 100
....*....|....*....|.
gi 1988774674 3591 ILAEENQKLREKLQQLEDAQK 3611
Cdd:pfam14817 144 ILAEDHQRLQGQLQQLRDAAR 164
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
3423-3543 |
3.95e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3423 HETEIATQEKMTVVERLEferlntsKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVlqQTFMT 3502
Cdd:COG2433 402 EHEERELTEEEEEIRRLE-------EQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREI--SRLDR 472
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1988774674 3503 EKEMLlkkEKLIEDEKKRLEsQFEEEVKKAKALKDEQERQK 3543
Cdd:COG2433 473 EIERL---ERELEEERERIE-ELKRKLERLKELWKLEHSGE 509
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2497-2576 |
4.06e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.88 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2497 AEAEKLRKlaqdEAEKLRKQVSEETQK-KRQAEEELKrksEAEKEAAKQKQKALEDLEklrmqaEEAERQVKQA--EIEK 2573
Cdd:cd06503 40 EEAEKAKE----EAEELLAEYEEKLAEaRAEAQEIIE---EARKEAEKIKEEILAEAK------EEAERILEQAkaEIEQ 106
|
...
gi 1988774674 2574 EKQ 2576
Cdd:cd06503 107 EKE 109
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2693-3037 |
4.07e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2693 AEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELA 2772
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2773 KVRSEMDILIQlktkAEKETMSNTEKSKQLLEAEAAKMKDLAEeaSRLRAISEEAKHQRQIAEEEaaRQRAEAERILKEK 2852
Cdd:pfam02029 84 ERQKEFDPTIA----DEKESVAERKENNEEEENSSWEKEEKRD--SRLGRYKEEETEIREKEYQE--NKWSTEVRQAEEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2853 LAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQH---KQEIEEKIVQLKKSSEAEMERQKAIVD- 2928
Cdd:pfam02029 156 GEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHpevKSQNGEEEVTKLKVTTKRRQGGLSQSQe 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2929 DTLKQRRVVEEEIRILKLN----------FEKASSGKLDLELELNKLKNIADEtqQSKIRAEEEaeklrklaleeekRRR 2998
Cdd:pfam02029 236 REEEAEVFLEAEQKLEELRrrrqekeseeFEKLRQKQQEAELELEELKKKREE--RRKLLEEEE-------------QRR 300
|
330 340 350
....*....|....*....|....*....|....*....
gi 1988774674 2999 EAEEKVKKIaaAEEEAARQRKaalEELERLRKKAEEARK 3037
Cdd:pfam02029 301 KQEEAERKL--REEEEKRRMK---EEIERRRAEAAEKRQ 334
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
3302-3612 |
4.11e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.52 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3302 AEDDLNQQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLledkqlmqQRLEEETEEYHKSLE--VERKR 3379
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKV--------KKLEATVETYKKKLEdlGDLRR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3380 QLEIMAEAERLRLQVSQLSEAQARAEEEAKK----FKKQADKVATRLheteiatQEKMTVVERLEFERLNTSKEADDLRK 3455
Cdd:pfam05622 153 QVKLLEERNAEYMQRTLQLEEELKKANALRGqletYKRQVQELHGKL-------SEESKKADKLEFEYKKLEEKLEALQK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3456 AIADLENEKARLKKEAEEL-----QNKSKEMADAQQKKIEHEKTVLQQTFMTekemLLKKEKLIedekkRLESQfeeevk 3530
Cdd:pfam05622 226 EKERLIIERDTLRETNEELrcaqlQQAELSQADALLSPSSDPGDNLAAEIMP----AEIREKLI-----RLQHE------ 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3531 kAKALKdeqERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEE----------NQKLR 3600
Cdd:pfam05622 291 -NKMLR---LGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQgskaedssllKQKLE 366
|
330
....*....|..
gi 1988774674 3601 EKLQQLEDAQKD 3612
Cdd:pfam05622 367 EHLEKLHEAQSE 378
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
3341-3605 |
4.12e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3341 KDLAQEQAQKLLEDKQLMQQRleeeteeyhKSLEVERKRQLEIMAEAER-LRLQVSQLSeaqaraeeeakKFKKQADKVA 3419
Cdd:PRK11637 50 KSIQQDIAAKEKSVRQQQQQR---------ASLLAQLKKQEEAISQASRkLRETQNTLN-----------QLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3420 TRLH--ETEIATQEKMTvverleferlntskeADDLRKAIADLENEKARLKKEAEELQNKSKEMA------DAQQKKIEH 3491
Cdd:PRK11637 110 ASIAklEQQQAAQERLL---------------AAQLDAAFRQGEHTGLQLILSGEESQRGERILAyfgylnQARQETIAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3492 ektvLQQTfmtekemllkKEKLIEdEKKRLESQFEEEvkkaKALKDEQERQKQQMEQ----EKKTLqATMDAALSKQKE- 3566
Cdd:PRK11637 175 ----LKQT----------REELAA-QKAELEEKQSQQ----KTLLYEQQAQQQKLEQarneRKKTL-TGLESSLQKDQQq 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1988774674 3567 -----AEEEMLRKQKEMQELE-RQRLEQErilAEENQKLREKLQQ 3605
Cdd:PRK11637 235 lselrANESRLRDSIARAEREaKARAERE---AREAARVRDKQKQ 276
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2685-2776 |
4.24e-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: 40.70 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2685 REAKKRAKAEESALKQKE-MAEEELERQRKIAEsTAQQKLTAE--------QELIRLRADFDNAEQQRSLLEDELYRLKN 2755
Cdd:pfam07926 7 QSEIKRLKEEAADAEAQLqKLQEDLEKQAEIAR-EAQQNYERElvlhaediKALQALREELNELKAEIAELKAEAESAKA 85
|
90 100
....*....|....*....|....*
gi 1988774674 2756 EVAAAQ----QQRKQLEDELAKVRS 2776
Cdd:pfam07926 86 ELEESEesweEQKKELEKELSELEK 110
|
|
| PRK01558 |
PRK01558 |
V-type ATP synthase subunit E; Provisional |
2500-2591 |
4.25e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 179302 Cd Length: 198 Bit Score: 42.05 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2500 EKLRKLAQDEAEKLRKQVSEETQKKRqaeEELKRKseAEKEAAKQKQKALEDLEKLRMQAEEAERQ-VKQAEIEKEKQIK 2578
Cdd:PRK01558 10 NKIKKDGLEEAERLANEIILEAKEEA---EEIIAK--AEEEAKELKAKAEKEANDYKRHALEASRQaGRDLLISFEKSIK 84
|
90
....*....|...
gi 1988774674 2579 VAHEAAQKSAAAE 2591
Cdd:PRK01558 85 SLFKAALKDEVAE 97
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
2571-2888 |
4.27e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2571 IEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEhgAVLQLQQEAERLKKQ--------------QEDAEN 2636
Cdd:PLN03229 413 VDPERKVNMKKREAVKTPVRELEGEVEKLKEQILKAKESSSKP--SELALNEMIEKLKKEidleyteaviamglQERLEN 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2637 SREEAEKELEKwRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEeSALKQKEMAEE-ELERQRKIA 2715
Cdd:PLN03229 491 LREEFSKANSQ-DQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAK-ALSEKKSKAEKlKAEINKKFK 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2716 ESTAQQKLTAEQELIRlradfDNAEQQRSLLEDELYR-LKNEVAAAqqqRKQLEDELAKVRSEMDILIQLKTKAEKETMS 2794
Cdd:PLN03229 569 EVMDRPEIKEKMEALK-----AEVASSGASSGDELDDdLKEKVEKM---KKEIELELAGVLKSMGLEVIGVTKKNKDTAE 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2795 NT------EKSKQLLEAEAAKMKDLAeEASRLRAISEEAKhqRQIAEEEAARQRAEAERI------LKEKLAAISEATRL 2862
Cdd:PLN03229 641 QTpppnlqEKIESLNEEINKKIERVI-RSSDLKSKIELLK--LEVAKASKTPDVTEKEKIealeqqIKQKIAEALNSSEL 717
|
330 340 350
....*....|....*....|....*....|...
gi 1988774674 2863 KT-----EAEIALKEK--EAENERLRRQAEDEA 2888
Cdd:PLN03229 718 KEkfeelEAELAAAREtaAESNGSLKNDDDKEE 750
|
|
| MRP-S27 |
pfam10037 |
Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins ... |
2698-2851 |
4.31e-03 |
|
Mitochondrial 28S ribosomal protein S27; Members of this family of small ribosomal proteins possess one of three conserved blocks of sequence found in proteins that stimulate the dissociation of guanine nucleotides from G-proteins, leaving open the possibility that MRP-S27 might be a functional partner of GTP-binding ribosomal proteins.
Pssm-ID: 462947 [Multi-domain] Cd Length: 395 Bit Score: 43.20 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2698 LKQKEMAEEELERQRKIAESTAQQKLTAE--QELIRLRADFDNAEqqrsllEDELYRLKNEVAAAQQQRKQLEdELAKVR 2775
Cdd:pfam10037 259 LGKVGYLDRALSVMEKVASSPGDLKLHKEvlDVLQDILETLDELE------ESEQSKLPEYVKSFQELLSKLQ-SLGKVE 331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774674 2776 SEmdILIQLKTKAEKETMSNTEKskQLLEAEAAKMKDLAEEasRLRAISEEAKHQrqiaeeEAARQRAEAERILKE 2851
Cdd:pfam10037 332 SE--SLLTLLENLVKESLPACEE--KDLANYEQLYQEWEEE--RRQLIQREKEMR------EKAEREDEARKALKE 395
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2465-2572 |
4.32e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.18 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2465 EEEIRLIRIQLETTEKQKYTAESE----LKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE 2540
Cdd:pfam05672 17 AEKRRQAREQREREEQERLEKEEEerlrKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1988774674 2541 AAKQKQK------ALEDLEKLR------MQAEEAERQVKQAEIE 2572
Cdd:pfam05672 97 ERLQKQKeeaeakAREEAERQRqerekiMQQEEQERLERKKRIE 140
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2612-2875 |
4.36e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2612 QEHGAVLQLQQEAER--LKKQQEDAENSREEAEKELEKWRQKANEAlrlRLQAEDEAHKKtlaqeeaekqkeeaerEAKK 2689
Cdd:PRK05035 433 QAKAEIRAIEQEKKKaeEAKARFEARQARLEREKAAREARHKKAAE---ARAAKDKDAVA----------------AALA 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2690 RAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQ----RK 2765
Cdd:PRK05035 494 RVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAAnaeaEE 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2766 QLEDELAKVRSEMdiliqLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEA-SRLRAISEEAKHQRQIAEEEAARQRAE 2844
Cdd:PRK05035 574 EVDPKKAAVAAAI-----ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKAAV 648
|
250 260 270
....*....|....*....|....*....|.
gi 1988774674 2845 AERILKEKlAAISEATRLKTEAEIALKEKEA 2875
Cdd:PRK05035 649 AAAIARAK-ARKAAQQQANAEPEEAEDPKKA 678
|
|
| PTZ00332 |
PTZ00332 |
paraflagellar rod protein; Provisional |
3162-3615 |
4.52e-03 |
|
paraflagellar rod protein; Provisional
Pssm-ID: 240364 [Multi-domain] Cd Length: 589 Bit Score: 43.41 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3162 LMQKQQADTEMAKhkkLAEQTLKQKFQVeQELTKVKLKLDETDKQKSVLDEELQRLKdEVDDAVKQRG--QVEEELFKVK 3239
Cdd:PTZ00332 146 LRRSQLDATQLAQ---VPTATLKNIEDI-MNVTQIQNALASTDDQIKTQLAQLEKTN-EIQNVAMHDGemQVAEEQMWTK 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3240 VQMEELL--------KLKNKIEEENQRLikKDKDSTQKLLAEEAENMRklaeDAARlsveaqeaaRLRQIAEDDLNQQRA 3311
Cdd:PTZ00332 221 VQLQERLielvadkfRLIGKCEEENKSF--SKIHEVQKQANQETSQMK----DAKR---------RLKQRCETDLKHIHD 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3312 LAEKMLKEKMQAIQEASRLKAEAEMLQKQKDLAQEQAQKLLEDKQLMQQRLEEETEEyhkslevERKRQLEIMAEAERLR 3391
Cdd:PTZ00332 286 AIQKADLEDAEAMKRYATNKEKSERFIRENEDRQEEAWNKIQDLERQLQRLGTERFE-------EVKRRIEENDREEKRR 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3392 LQVSQLseaqaraeeeakkfkkqadkvatrlheTEIATQEKmtvvERLEFERLNTskeadDLRKAIADLENE-------- 3463
Cdd:PTZ00332 359 VEYQQF---------------------------LEVAGQHK----KLLELTVYNC-----DLALRCTGLVEElvsegcaa 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3464 -KARLKKEAEELqnkSKEMADAQQKKIEHektvLQQTFMTEKEMLLKKEKLIEDEKKRLESQ----------FEEEVKKA 3532
Cdd:PTZ00332 403 vKARHDKTNQDL---AALRLQVHKEHLEY----FRMLYLTLGSLIYKKEKRLEEIDRNIRTThiqlefcvetFDPNAKKH 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3533 KALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEE------------------EMLRKQKEMQELERQRLEQE--RIL 3592
Cdd:PTZ00332 476 ADMKKELYKLRQGVEEELAMLKEKQAQALEMFKESEEaldaagiefvhpvdenneEVLTRRSKMVEYRSHLAKQEevKIA 555
|
490 500
....*....|....*....|...
gi 1988774674 3593 AEENQKLREKLQQLEDAQKDQHT 3615
Cdd:PTZ00332 556 AEREEIKRARLLRSQGYRGEQIR 578
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2355-2623 |
4.73e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.88 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2355 QRRLDDEEKAAEKLKAEERKKMAEMQAELDK-----QKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQK 2429
Cdd:pfam15905 75 QKELEKEIRALVQERGEQDKRLQALEEELEKveaklNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQKKM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2430 TNIQLELQELKNLSEQQIKdksqqvdEALHSRTKIEeeirlirIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDE 2509
Cdd:pfam15905 155 SSLSMELMKLRNKLEAKMK-------EVMAKQEGME-------GKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2510 AEKLRKQVSEETQKKRQAeEELKRKSEAEKEAAKQKQKALEDL--------EKLRMQAEEAERQVKQAEIEKEKQIKVAH 2581
Cdd:pfam15905 221 TEKLLEYITELSCVSEQV-EKYKLDIAQLEELLKEKNDEIESLkqsleekeQELSKQIKDLNEKCKLLESEKEELLREYE 299
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1988774674 2582 EAAQkSAAAELQSkhmsfaektskLEESLKQEHGAVLQLQQE 2623
Cdd:pfam15905 300 EKEQ-TLNAELEE-----------LKEKLTLEEQEHQKLQQK 329
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2393-2726 |
4.77e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2393 HAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELK----------NLSEQQIKDKSQQVDEALHSRT 2462
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLReeleqareelEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2463 KIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELKRkseaEKEAA 2542
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE----LEEQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2543 KQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQ 2622
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2623 EAERLKKQQEDAENSREEAEKElekwrQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKE 2702
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIE-----ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330 340
....*....|....*....|....
gi 1988774674 2703 MAEEELERQRKIAESTAQQKLTAE 2726
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAE 338
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2765-3086 |
4.78e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2765 KQLEDEL--AKVRSEMDILIQLKTKAEKETMsnTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQR-----QIAEEE 2837
Cdd:pfam13868 9 RELNSKLlaAKCNKERDAQIAEKKRIKAEEK--EEERRLDEMMEEERERALEEEEEKEEERKEERKRYRqeleeQIEERE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2838 AARQRaEAERILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQASQHKQEIEEKIVQLKKSSE 2917
Cdd:pfam13868 87 QKRQE-EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2918 AEMERQKAivddtLKQRRVVEEEIRILKLNF--EKASSGKLDLElELNKLKNIADETQQSKIRAEEEAEKLRKLALEEEK 2995
Cdd:pfam13868 166 EREEEREA-----EREEIEEEKEREIARLRAqqEKAQDEKAERD-ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2996 RRREAEEKVKKIAAAEEEAARQ-----RKAALEELERLRKKAEEARKQKDEADKEAEKQIVVAQQAAQKCSAAEQQVQSV 3070
Cdd:pfam13868 240 AREEQIELKERRLAEEAEREEEefermLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGER 319
|
330 340
....*....|....*....|..
gi 1988774674 3071 LAQQIE------DSITQKKLKE 3086
Cdd:pfam13868 320 LREEEAerreriEEERQKKLKE 341
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2607-2956 |
4.85e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.17 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2607 EESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELekwrQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAERE 2686
Cdd:pfam03528 3 DEDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKEL----YLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2687 AKKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAEQELIR--LRADFDNAE--QQRSLLEDELYRLKNEVAAAQQ 2762
Cdd:pfam03528 79 NIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVREYEVQfhRRLEQERAQwnQYRESAEREIADLRRRLSEGQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2763 QrKQLEDELAKVRSEMDILIQLKTKAEKETMS----NTEKSKQLLEAEAAKMKDL-----AEEASR--LRAISEEAKHQR 2831
Cdd:pfam03528 159 E-ENLEDEMKKAQEDAEKLRSVVMPMEKEIAAlkakLTEAEDKIKELEASKMKELnhyleAEKSCRtdLEMYVAVLNTQK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2832 QIAEEEAARQRAEAERILKEKLAAISEATRLKTEAEIAlKEKEAENERLRRQaedeAYQRKALEDQASQHKQEIEEKivq 2911
Cdd:pfam03528 238 SVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKA-NDQFLESQRLLMR----DMQRMESVLTSEQLRQVEEIK--- 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1988774674 2912 lKKSSEAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKL 2956
Cdd:pfam03528 310 -KKDQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPL 353
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2501-2728 |
4.89e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2501 KLRKLAQDEAEKlRKQVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVA 2580
Cdd:PRK11637 48 QLKSIQQDIAAK-EKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2581 heaAQKSAAAELQSKHmsfaektSKLEESLKQEHGavlqlqQEAERLKKQQEDAENSREEAEKELEKWRQKANEALRLrL 2660
Cdd:PRK11637 127 ---AAQLDAAFRQGEH-------TGLQLILSGEES------QRGERILAYFGYLNQARQETIAELKQTREELAAQKAE-L 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 2661 QAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAE-ESALKQK-----EMAEEELERQRKIAESTAQQKLTAEQE 2728
Cdd:PRK11637 190 EEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGlESSLQKDqqqlsELRANESRLRDSIARAEREAKARAERE 263
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
2375-2608 |
5.06e-03 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 43.41 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2375 KMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIA---AVDAEKQKTNIQLELQELK----NLSEQQI 2447
Cdd:PRK15374 107 RLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKTDTAksvYDAAEKKLTQAQNKLQSLDpadpGYAQAEA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2448 KdKSQQVDEALHSRTKIEeeirliriqlettekQKYTAESelKQLRDRAAEAEKlrklAQDEAEKLRKQVSEETQkkrqa 2527
Cdd:PRK15374 187 A-VEQAGKEATEAKEALD---------------KATDATV--KAGTDAKAKAEK----ADNILTKFQGTANAASQ----- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2528 eeelkrkseaeKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLE 2607
Cdd:PRK15374 240 -----------NQVSQGEQDNLSNVARLTMLMAMFIEIVGKNTEESLQNDLALFNALQEGRQAEMEKKSAEFQEETRKAE 308
|
.
gi 1988774674 2608 E 2608
Cdd:PRK15374 309 E 309
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3204-3389 |
5.10e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3204 DKQKSVLDEELQRLKDEVDDAVKQRGQVEEELFKVKVQMEELLKL--KNKIEEENQRLIKKdkdstQKLLAEEAenmRKL 3281
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAqeQKKQAEEAAKQAAL-----KQKQAEEA---AAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3282 AEDAARLSVEAQE---AARLRQIAEDDLNQQRALAEKMLKEKMQAIQEA-SRLKAEAEMLQKQKDLAQEQAQKLLEDKQL 3357
Cdd:PRK09510 141 AAAAAKAKAEAEAkraAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAeAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|..
gi 1988774674 3358 MQQRLEEETEEYHKSLEVERKRQLEIMAEAER 3389
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
3346-3609 |
5.12e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.60 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3346 EQAQKLLEDK--QLMQQRLEEET---EEYHKSLEVERKRQLEIMAEAERLRLQVSQLseaqaraeeeakkfKKQADKVAT 3420
Cdd:pfam00038 24 EQQNKLLETKisELRQKKGAEPSrlySLYEKEIEDLRRQLDTLTVERARLQLELDNL--------------RLAAEDFRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3421 RLhETEIAtqEKMTVVERLEFERlntsKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQ--- 3497
Cdd:pfam00038 90 KY-EDELN--LRTSAENDLVGLR----KDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEmda 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3498 --QTFMTE--KEMLLKKEKLIEDEKKRLESQFE---EEVKKAKALKDEQERQ-KQQMEQEKKTLQAtmdaalskqKEAEE 3569
Cdd:pfam00038 163 arKLDLTSalAEIRAQYEEIAAKNREEAEEWYQsklEELQQAAARNGDALRSaKEEITELRRTIQS---------LEIEL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1988774674 3570 EMLRKQKEmqELERQRLEQERILAEENQKLREKLQQLEDA 3609
Cdd:pfam00038 234 QSLKKQKA--SLERQLAETEERYELQLADYQELISELEAE 271
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
2689-2922 |
5.20e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 43.51 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2689 KRAKAEESALKQkemaeeELErqrkiaeSTAQQKLTAEQELIRLRADFDNAEQQ-RSLLEDELYRLKNevaAAQQQRKQL 2767
Cdd:pfam05911 20 EKAEAEALALKQ------QLE-------SVTLQKLTAEERAAHLDGALKECMQQlRNVKEEQEQKIHD---VVLKKTKEW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2768 EdelakvrsemdiliqlKTKAEKETmSNTEKSKQLLEAEAakmkdlaeEASRL-RAISEEAKHQRQIAEEEAarqRAEAE 2846
Cdd:pfam05911 84 E----------------KIKAELEA-KLVETEQELLRAAA--------ENDALsRSLQERENLLMKLSEEKS---QAEAE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2847 -RILKEKLAAIS-EATRLKTEAEIALKEKEAENERL---RRQAEdeayqrkaledqaSQHKQEIE--EKIVQLkkssEAE 2919
Cdd:pfam05911 136 iEALKSRLESCEkEINSLKYELHVLSKELEIRNEEKnmsRRSAD-------------AAHKQHLEsvKKIAKL----EAE 198
|
...
gi 1988774674 2920 MER 2922
Cdd:pfam05911 199 CQR 201
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2621-2825 |
5.56e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2621 QQEAERLKKQQEDAENSREEAE----KELEKWRQKANEAlrlRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEES 2696
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEqerlKQLEKERLAAQEQ---KKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2697 ALkqKEMAEEELERQRKIAESTAQQKLTAEQElirlradfdnaeqqrslLEDELYRLKNEVAAAQQQRKQLEDELAKVRS 2776
Cdd:PRK09510 155 RA--AAAAKKAAAEAKKKAEAEAAKKAAAEAK-----------------KKAEAEAAAKAAAEAKKKAEAEAKKKAAAEA 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1988774674 2777 EMdiliqlKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASRLRAISE 2825
Cdd:PRK09510 216 KK------KAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2811-2940 |
5.68e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2811 KDLAEEASRLRAISE-EAKHQRQIAEEEAARQRAEAErilKEKLAAISEATRLKTEAEIALK--EKEAENERLRRQAEDE 2887
Cdd:COG2268 191 RRKIAEIIRDARIAEaEAERETEIAIAQANREAEEAE---LEQEREIETARIAEAEAELAKKkaEERREAETARAEAEAA 267
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774674 2888 AYQRKALEDQASQHKQEIEEKIVQLK---KSSEAEMERQKAIVDDTLK-QRRVVEEE 2940
Cdd:COG2268 268 YEIAEANAEREVQRQLEIAEREREIElqeKEAEREEAELEADVRKPAEaEKQAAEAE 324
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4694-4730 |
5.69e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 5.69e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1988774674 4694 KQYLYGTGCVAGIT-TDSSSKLSIYQAMKRGFIKPEIG 4730
Cdd:smart00250 1 QRLLEAQSAIGGIIdPETGQKLSVEEALRRGLIDPETG 38
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2404-2855 |
5.69e-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: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2404 AQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKY 2483
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2484 TAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEE--ELKRKSEAEKEAAKQKQKALEDLEKLRMQAEE 2561
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRkaEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2562 AERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEA 2641
Cdd:COG3064 162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2642 EKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEMAEEELERQRKIAESTAQQ 2721
Cdd:COG3064 242 EAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2722 KLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILIQLKTKAEKETMSNTEKSKQ 2801
Cdd:COG3064 322 AAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 2802 LLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAA 2855
Cdd:COG3064 402 GLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKAL 455
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2623-2899 |
5.82e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2623 EAERLKKQQEDAENSREEAEKELEKWRQKANEALRLRLQAEDEAhkktlaqeeaekqkeeaeREAKKRAKAEESALKQke 2702
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL------------------EALQAEIDKLQAEIAE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2703 mAEEELERQRKIAESTAQQKLTAEQELIRLRA-----DFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSE 2777
Cdd:COG3883 77 -AEAEIEERREELGERARALYRSGGSVSYLDVllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2778 MDILIQLKTKAEKETmsnTEKSKQLLEAEAAKMKDLAEEASRLRAISEEAKHQRQIAEEEAARQRAEAERILKEKLAAIS 2857
Cdd:COG3883 156 LAELEALKAELEAAK---AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1988774674 2858 EATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALEDQAS 2899
Cdd:COG3883 233 AAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
3355-3549 |
6.23e-03 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 42.63 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3355 KQLMQQRLEEETEEYHKSLEVERKRQLEI-MAEAERLRLQVSQLSeaqaraeeeakkfKKQADKVATRLHETEIATQEKM 3433
Cdd:COG4487 21 ADIVKQRRAEFEKELAERLADAAKREAALeLAEAKAKAQLQEQVA-------------EKDAEIAELRARLEAEERKKAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3434 TVVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQ-QTFMTEKEMLLKKEK 3512
Cdd:COG4487 88 AVAEEKEKELAALQEALAEKDAKLAELQAKELELLKKERELEDAKREAELTVEKERDEELDELKeKLKKEEEEKQLAEKS 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1988774674 3513 LIEDEKkrlESQFEEEVKKAKALKDEQERQKQQMEQE 3549
Cdd:COG4487 168 LKVAEY---EKQLKDMQEQIEELKRKKEQGSTQLQGE 201
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2366-2665 |
6.24e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.97 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2366 EKLKAE-ERKK---MAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKN 2441
Cdd:pfam15964 359 EQLKSElERQKerlEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQK 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2442 lseqqiKDKSQQVDEalhsrTKIEEEIRLiriQLETTEKQKYTAESELKQLRdraAEAEKLRKLAQDEAEKLRKQVSEET 2521
Cdd:pfam15964 439 ------QLASQEMDV-----TKVCGEMRY---QLNQTKMKKDEAEKEHREYR---TKTGRQLEIKDQEIEKLGLELSESK 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2522 QkkrqaeeelkRKSEAEKEAAKQKQKALEDLEKLrmqaEEAERQVKQAEIEKE--------------------------- 2574
Cdd:pfam15964 502 Q----------RLEQAQQDAARAREECLKLTELL----GESEHQLHLTRLEKEsiqqsfsneakaqalqaqqreqeltqk 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2575 -KQIKVAHEAAQKSAAAELQSKHmSFAEK--------TSKLEESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKEL 2645
Cdd:pfam15964 568 mQQMEAQHDKTVNEQYSLLTSQN-TFIAKlkeecctlAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEQC 646
|
330 340
....*....|....*....|
gi 1988774674 2646 EKwRQKANEALRLRLQAEDE 2665
Cdd:pfam15964 647 VQ-HGRMHERMKQRLRQLDK 665
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
3289-3568 |
6.38e-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: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3289 SVEAQEAARLRQIAEDDLNQQRALAEKmlkekmqAIQEASRLKAEAEMLQKQKDLAQEQAQklLEDKQlmQQRLEEETEE 3368
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK-------ERAEADRQRLEQEKQQQLAAISGSQSQ--LESTD--QNALETNGQA 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3369 YHKSLEVERKrqlEIMAEAERLRLQVSQLSEAQARAEEEAKKFKKQ-----ADKVATRLHETEIATQEKMTVVERLEFER 3443
Cdd:NF012221 1607 QRDAILEESR---AVTKELTTLAQGLDALDSQATYAGESGDQWRNPfagglLDRVQEQLDDAKKISGKQLADAKQRHVDN 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3444 LNTSKEAddLRKAIADLENEKaRLKKEAEelQNKSKEMADAQQKKiehektvlqqtfmteKEMLLKKEkliedEKKRLES 3523
Cdd:NF012221 1684 QQKVKDA--VAKSEAGVAQGE-QNQANAE--QDIDDAKADAEKRK---------------DDALAKQN-----EAQQAES 1738
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1988774674 3524 QFEEEVKKAKalkdeQERQKQQMEQEKKTLQATMDAALSKQKEAE 3568
Cdd:NF012221 1739 DANAAANDAQ-----SRGEQDASAAENKANQAQADAKGAKQDESD 1778
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
3485-3611 |
6.41e-03 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 40.24 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3485 QQKKIEHEKTVLQQTFMTEKEMLLKKEKLIEDEkkrLESQFEEEVKK-AKALKDEQERQ----KQQMEQEKKTLQATMDA 3559
Cdd:pfam12474 8 QKDRFEQERQQLKKRYEKELEQLERQQKQQIEK---LEQRQTQELRRlPKRIRAEQKKRlkmfRESLKQEKKELKQEVEK 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 3560 AlskQKEAEEEMLRKQKEMQELErQRLEQERILAEENQKLREKLQQLEDAQK 3611
Cdd:pfam12474 85 L---PKFQRKEAKRQRKEELELE-QKHEELEFLQAQSEALERELQQLQNEKR 132
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
2475-2613 |
6.41e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 42.31 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2475 LETTEKQKYTAESELKQlrdraaeaEKLRKLAQDEAEKLRKQVSEETQKKRQAEEElkrksEAEKEAAKQKQKALEDLEK 2554
Cdd:PRK06669 30 LSIKEKERLREEEEEQV--------EQLREEANDEAKEIIEEAEEDAFEIVEAAEE-----EAKEELLKKTDEASSIIEK 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 2555 LRMQaeeAERQVKQAEIEKEKQIKVA----HEAAQKSAAAELQSKHMSFAEKTSKLEESLKQE 2613
Cdd:PRK06669 97 LQMQ---IEREQEEWEEELERLIEEAkaegYEEGYEKGREEGLEEVRELIEQLNKIIEKLIKK 156
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
2544-2944 |
6.48e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 42.74 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2544 QKQKALEDLEkLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAAAELQSKHMSFAEKTSKLEESLKQEHGavlQLQQE 2623
Cdd:pfam04747 50 QRKEAFASLE-LTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEARRAEAEAKKRAAQEEEHK---QWKAE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2624 AERLKKQQEdaenSREEAEKELEKWRQKANEALRLRLQAEDEAHKKTLAQEEAEKQKEEAEREAKKRAKAEESALKQKEM 2703
Cdd:pfam04747 126 QERIQKEQE----KKEADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTPTNTP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2704 AEEELERQRKIAESTAQQKLTAEQELIRLRADFDN-AEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAKVRSEMDILI 2782
Cdd:pfam04747 202 AEPAEQVQEITGKKNKKNKKKSESEATAAPASVEQvVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETPVEP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2783 -----------QLKTKAEKETMSNTEKSKQLLEAEAAKMKDLAEEASR--LRAISEEAKHQRQIAEEEAARQRAEAERIL 2849
Cdd:pfam04747 282 vvettppasenQKKNKKDKKKSESEKVVEEPVQAEAPKSKKPTADDNMdfLDFVTAKEEPKDEPAETPAAPVEEVVENVV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2850 KEKLAAISEATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKALED--QASQHKQEIEEKIVQLKKSSEAEMERQKAIV 2927
Cdd:pfam04747 362 ENVVEKSTTPPATENKKKNKKDKKKSESEKVTEQPVESAPAPPQVEQvvETTPPASENKKKNKKDKKKSESEKAVEEPVQ 441
|
410
....*....|....*..
gi 1988774674 2928 DDTLKQRRVVEEEIRIL 2944
Cdd:pfam04747 442 AAPSSKKPTADDNMDFL 458
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
1058-1155 |
6.49e-03 |
|
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 39.82 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 1058 QKKTFTKWVNKHL---------IKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 1123
Cdd:cd21293 2 EKGSYVDHINRYLgddpflkqfLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1988774674 1124 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1155
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3435-3540 |
6.60e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3435 VVERLEFERLNTSKEADDLRKAIADLENEKARLKKEAEELQN-KSKEMADAQQK--------KIEHEKTVLQQTFMTEKE 3505
Cdd:PRK00409 521 LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeEDKLLEEAEKEaqqaikeaKKEADEIIKELRQLQKGG 600
|
90 100 110
....*....|....*....|....*....|....*
gi 1988774674 3506 MLLKKEKLIEDEKKRLESQFEEEVKKAKALKDEQE 3540
Cdd:PRK00409 601 YASVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
3247-3394 |
6.70e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.68 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3247 KLKNKIEEENQRLIKKDKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQ---IAEDDLNQQRALAEKMLKEKMQA 3323
Cdd:pfam05262 181 KVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQkadFAQDNADKQRDEVRQKQQEAKNL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3324 ------------IQEASRLKAEAEMLQKQKDLAQEQAQKLLEDK--QLMQQRLEEETEEYHKSLEVERKRqLEIMAEAER 3389
Cdd:pfam05262 261 pkpadtsspkedKQVAENQKREIEKAQIEIKKNDEEALKAKDHKafDLKQESKASEKEAEDKELEAQKKR-EPVAEDLQK 339
|
....*
gi 1988774674 3390 LRLQV 3394
Cdd:pfam05262 340 TKPQV 344
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2440-2722 |
6.71e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.49 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2440 KNLSEQQIKDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRKQVSE 2519
Cdd:pfam15905 54 RKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2520 ETQkkrqAEEELKRKSEAEKEAAKQKQKALEdLEKLRMQAEEAERQVKQAEIEKEKQIKVAHEAAQKSAA--AELQSKHM 2597
Cdd:pfam15905 134 LTR----VNELLKAKFSEDGTQKKMSSLSME-LMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGkvAQLEEKLV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2598 SFA-EKTSKLEESLKQEHgAVLQLQQEAERLKKQQEDAENSREEAEKelekwRQKANEALRLRLQAEDEAHKKTLAQEEA 2676
Cdd:pfam15905 209 STEkEKIEEKSETEKLLE-YITELSCVSEQVEKYKLDIAQLEELLKE-----KNDEIESLKQSLEEKEQELSKQIKDLNE 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1988774674 2677 EKQKEEAEREAKKRAKAEESALKQKEMAE-EELERQRKIAESTAQQK 2722
Cdd:pfam15905 283 KCKLLESEKEELLREYEEKEQTLNAELEElKEKLTLEEQEHQKLQQK 329
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2705-2881 |
6.76e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2705 EEELER-QRKIAEST------AQQKLTAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVAAAQQQRKQLEDELAkvrSE 2777
Cdd:PRK09039 52 DSALDRlNSQIAELAdllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELD---SE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2778 mdiliqlktkaeketmsnteksKQLLEAEAAKMKDLAEEASRLRaiseeakhqRQIAEEEAARQRAEAERilKEKLAAIS 2857
Cdd:PRK09039 129 ----------------------KQVSARALAQVELLNQQIAALR---------RQLAALEAALDASEKRD--RESQAKIA 175
|
170 180
....*....|....*....|....
gi 1988774674 2858 EatrLKTEAEIALKEKEAENERLR 2881
Cdd:PRK09039 176 D---LGRRLNVALAQRVQELNRYR 196
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
2479-2566 |
6.86e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 40.37 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2479 EKQKYTAESElKQLRDRAAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEElkrksEAEKEAAKQKQKALEDLEKlrmQ 2558
Cdd:PRK07353 54 EAEKLEAQYE-QQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQASKE-----KARREIEQQKQAALAQLEQ---Q 124
|
....*...
gi 1988774674 2559 AEEAERQV 2566
Cdd:PRK07353 125 VDALSRQI 132
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
753-941 |
7.20e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 42.77 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 753 EPESEVINTnpvpltEAETLPSTDTRPLHEAAVKNSPDMASGLTEtNVSLKMTLERMCSEEVRQAAAVLSEAPADKREVE 832
Cdd:PRK08691 306 DPDSDILHR------LAQTISGEQIQLYYQIAVHGKRDLSLAPDE-YAGFMMTLLRMLAFAPLAAASCDANAVIENTELQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 833 -PALLFAEK---IKREAPKPETSSSVSEAPAAGELASAARALTAEPAAAQAQA---------SPLFEREEPPKVAQHSAA 899
Cdd:PRK08691 379 sPSAQTAEKetaAKKPQPRPEAETAQTPVQTASAAAMPSEGKTAGPVSNQENNdvppwedapDEAQTAAGTAQTSAKSIQ 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1988774674 900 RAAECST--EERLSVSEALKQEGEKKRDLVEDTPSATATPVTRP 941
Cdd:PRK08691 459 TASEAETppENQVSKNKAADNETDAPLSEVPSENPIQATPNDEA 502
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2239-2574 |
7.29e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 42.74 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2239 DAKQRQEKIQAVPITDSKTLKEQLAQEKKLLEEI-EQNKDKVDEC-----------QKYAKAYIDTIKDYElqlvayKAQ 2306
Cdd:pfam13166 104 EIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECwKKIKRKKNSAlsealngfkyeANFKSRLLREIEKDN------FNA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2307 VEPLVSPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYI---------KFITDTQRRLDDEEKAAE----------- 2366
Cdd:pfam13166 178 GVLLSDEDRKAALATVFSDNKPEIAPLTFNVIDFDALEKAEIliqkvigksSAIEELIKNPDLADWVEQglelhkahldt 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2367 ------KLKAEERKKMAEM--QAELDKQKQLAEAHAKAIAKAEKEAQELKlKMQEEVSKREIAAVDAEKQKTNIQL---E 2435
Cdd:pfam13166 258 cpfcgqPLPAERKAALEAHfdDEFTEFQNRLQKLIEKVESAISSLLAQLP-AVSDLASLLSAFELDVEDIESEAEVlnsQ 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2436 LQELKNLSEQQIKDKSQqvdealhsrtkieeEIRLIRIQLETtEKQKYTAESELKQLRDRAAEAEKLRKLAQDEAEKLRK 2515
Cdd:pfam13166 337 LDGLRRALEAKRKDPFK--------------SIELDSVDAKI-ESINDLVASINELIAKHNEITDNFEEEKNKAKKKLRL 401
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2516 QVSEETQKKRQAEEELKRKSEAEKEAAKQKQKALED-LEKLRMQAEEAERQVKQ-----AEIEKE 2574
Cdd:pfam13166 402 HLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAeIKKLREEIKELEAQLRDhkpgaDEINKL 466
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
3241-3388 |
7.34e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3241 QMEELLKLKNKIEEENQRLIKKdKDSTQKLLAEEAENMRKLAEDAARLSVEAQEAARLRQIAEDDLNQQRALAEKMLKEK 3320
Cdd:COG2268 193 KIAEIIRDARIAEAEAERETEI-AIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIA 271
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988774674 3321 MQAIQEASRLKAEAEMLQKQKDLAQEQAQKlledkqlmqqRLEEETEEYHKSLEVERKRQlEIMAEAE 3388
Cdd:COG2268 272 EANAEREVQRQLEIAEREREIELQEKEAER----------EEAELEADVRKPAEAEKQAA-EAEAEAE 328
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5291-5321 |
7.50e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 37.31 E-value: 7.50e-03
10 20 30
....*....|....*....|....*....|.
gi 1988774674 5291 AGILDIDTLEKVSVTEAIHRNLVDNITGQRL 5321
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
3448-3613 |
8.48e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.20 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3448 KEADDLRKAIADLENEKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLlkkEKLIEDEKKRLEsQFEE 3527
Cdd:pfam04012 36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEKKSL---EKQAEALETQLA-QQRS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3528 EVKKAKALKDEQERQKQQMEQEKKTLQATMDAAlsKQKEAEEEMLRK---QKEMQELER-----QRLEQERILAEENQKL 3599
Cdd:pfam04012 112 AVEQLRKQLAALETKIQQLKAKKNLLKARLKAA--KAQEAVQTSLGSlstSSATDSFERieekiEEREARADAAAELASA 189
|
170
....*....|....
gi 1988774674 3600 REKLQQLEDAQKDQ 3613
Cdd:pfam04012 190 VDLDAKLEQAGIQM 203
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3436-3625 |
8.60e-03 |
|
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: 42.65 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3436 VERLEFERLNTSKEADDLRKAIADLENEKAR---LKKEAEELQNKSKEMADAQQKKIEHEKTVLQQTFMTEKEMLLKKEK 3512
Cdd:TIGR00618 172 LFPLDQYTQLALMEFAKKKSLHGKAELLTLRsqlLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3513 LIE-DEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQ--KEAEEEMLRKQKEMQELE-----RQ 3584
Cdd:TIGR00618 252 QEEqLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQieQQAQRIHTELQSKMRSRAkllmkRA 331
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1988774674 3585 RLEQERILAEENQKLREKLQQLEDAQKDQHTRETDKVLHKD 3625
Cdd:TIGR00618 332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC 372
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2511-2652 |
8.66e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2511 EKLRKQVSEETQKKrqaeEELKRKSEAEKEAAKQK----QKALEDLEKLRM----QAEEAERQVKQAEIEKEKQIKVAHE 2582
Cdd:PRK00409 505 EEAKKLIGEDKEKL----NELIASLEELERELEQKaeeaEALLKEAEKLKEeleeKKEKLQEEEDKLLEEAEKEAQQAIK 580
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988774674 2583 AAQKSAAAELQS-----KHMSFAEKTSKLEESLKQEHGAVLQLQqeaERLKKQQEDAENSREEAEKELEKWRQKA 2652
Cdd:PRK00409 581 EAKKEADEIIKElrqlqKGGYASVKAHELIEARKRLNKANEKKE---KKKKKQKEKQEELKVGDEVKYLSLGQKG 652
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
2767-2915 |
8.66e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.05 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2767 LEDELAKVRSEMDILiqlktkaeKETMSNTEKSKQLLEAEAAKMKD-LAEEASRLRaiSEEAKHQRQIAEEEAARQRAEA 2845
Cdd:pfam09787 45 LTLELEELRQERDLL--------REEIQKLRGQIQQLRTELQELEAqQQEEAESSR--EQLQELEEQLATERSARREAEA 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988774674 2846 E--RILKEKLAAISEATRLKTEAEIALKEKEAENERLRRQAedeayqrkALEDQASQHKQEIEEKIVQLKKS 2915
Cdd:pfam09787 115 EleRLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQL--------TSKSQSSSSQSELENRLHQLTET 178
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
3437-3605 |
8.70e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 42.61 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3437 ERLEFERLN-TSKE------ADDLRkaiADLENEKARLKKEAEELQNKSK---EMADAQQKKIE-HEKTVLQQTFMTEKE 3505
Cdd:PLN03188 1047 KKLEQERLRwTEAEskwislAEELR---TELDASRALAEKQKHELDTEKRcaeELKEAMQMAMEgHARMLEQYADLEEKH 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3506 MLL-----KKEKLIEDEKKRL--------ESQFEEEVK-KAKALKDEQERQKQQMEQEKKTLQATM-DAA---------L 3561
Cdd:PLN03188 1124 IQLlarhrRIQEGIDDVKKAAaragvrgaESKFINALAaEISALKVEREKERRYLRDENKSLQAQLrDTAeavqaagelL 1203
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1988774674 3562 SKQKEAEEEMLRKQKEMQELERQrleqerilAEENQKLREKLQQ 3605
Cdd:PLN03188 1204 VRLKEAEEALTVAQKRAMDAEQE--------AAEAYKQIDKLKR 1239
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
816-944 |
8.83e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 42.53 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 816 QAAAVLSEAPAdkREVEPALLfAEKIKREAPKPETSSSVSEAPAAGELASAARALTAEPAAAQAQASPlfeREEPPKVAQ 895
Cdd:PRK07003 417 AAAATRAEAPP--AAPAPPAT-ADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPA---SDAPPDAAF 490
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1988774674 896 HSAARAAECSTEERLSVSEALKQEGEKKRDlvEDTPSATATPVTRPDQP 944
Cdd:PRK07003 491 EPAPRAAAPSAATPAAVPDARAPAAASRED--APAAAAPPAPEARPPTP 537
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2237-2643 |
8.87e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2237 IADAKQRQEKIQAVpitdsktLKEQLAQEKKLLEEIEQNKDKVDECQKyakayidtikdyelQLVAYKAQVEPLVSPLKK 2316
Cdd:PRK04778 114 LDLIEEDIEQILEE-------LQELLESEEKNREEVEQLKDLYRELRK--------------SLLANRFSFGPALDELEK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2317 tKLDSASDNiIQEYVTLRT------------RYSELMTLTSQYIKFI--------TDTQRRLDDEEKAAEKLKAE----E 2372
Cdd:PRK04778 173 -QLENLEEE-FSQFVELTEsgdyveareildQLEEELAALEQIMEEIpellkelqTELPDQLQELKAGYRELVEEgyhlD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2373 RKKMAEMQAELDKQKQLAEAHAKA--IAKAEKEAQELKLKMQE--EVSKREIAA-VDAEKQKTNIQLELQELKNlSEQQI 2447
Cdd:PRK04778 251 HLDIEKEIQDLKEQIDENLALLEEldLDEAEEKNEEIQERIDQlyDILEREVKArKYVEKNSDTLPDFLEHAKE-QNKEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2448 KDKSQQVDEALHSRTKIEEEIRLIRIQLETTEKQkytaeseLKQLRDRAAEAEKLRKLAQDEAEKLRKQVS--EETQKKR 2525
Cdd:PRK04778 330 KEEIDRVKQSYTLNESELESVRQLEKQLESLEKQ-------YDEITERIAEQEIAYSELQEELEEILKQLEeiEKEQEKL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2526 QaeEELK--RKSEAE-KEAAKQKQKALED----LEKLRM---------QAEEAERQVKQAEIE-KEKQIKVaHEAAQKSA 2588
Cdd:PRK04778 403 S--EMLQglRKDELEaREKLERYRNKLHEikryLEKSNLpglpedyleMFFEVSDEIEALAEElEEKPINM-EAVNRLLE 479
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1988774674 2589 AAELQSKHmsFAEKTSKLEESlkqehgAVL--QLQQEAERLKKQQEDAENSREEAEK 2643
Cdd:PRK04778 480 EATEDVET--LEEETEELVEN------ATLteQLIQYANRYRSDNEEVAEALNEAER 528
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
3445-3560 |
8.89e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.97 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3445 NTSKEADDLRKAIADLENEkarLKKEAEELQNKSKEMADA----------QQKKIEHEKTVLQQTFMTEKEMLLKKEklI 3514
Cdd:cd22656 107 TDDEELEEAKKTIKALLDD---LLKEAKKYQDKAAKVVDKltdfenqtekDQTALETLEKALKDLLTDEGGAIARKE--I 181
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1988774674 3515 EDEKKRLESQFEEEVKKAKALKDEQERQKQQMEQEKKTLQATMDAA 3560
Cdd:cd22656 182 KDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADL 227
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2710-2900 |
8.94e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.55 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2710 RQRKIAESTAQQKLTAEQELIRLRADFD-NAEQQRSLLEDELYRLKNE--VAAAQQQRKQLEDELAKVRSEMDILIQLKT 2786
Cdd:PRK00106 25 KMKSAKEAAELTLLNAEQEAVNLRGKAErDAEHIKKTAKRESKALKKEllLEAKEEARKYREEIEQEFKSERQELKQIES 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2787 KAEKETMSNTEKSKQLLEAEaaKMKDLAEEAsrlraISEEAKH----QRQIAEEEAaRQRAEAERI----LKEKLAAISE 2858
Cdd:PRK00106 105 RLTERATSLDRKDENLSSKE--KTLESKEQS-----LTDKSKHiderEEQVEKLEE-QKKAELERVaalsQAEAREIILA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1988774674 2859 ATRLKTEAEIALKEKEAENE---RLRRQAED---EAYQRKALEDQASQ 2900
Cdd:PRK00106 177 ETENKLTHEIATRIREAEREvkdRSDKMAKDllaQAMQRLAGEYVTEQ 224
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
3479-3612 |
9.03e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3479 KEMADAQQKKIEHE-KTVLQQTFmteKEMLLKKEKLIEDEKKRLeSQFEEEVK----KAKALKDEQERQKQQMEQEKKTL 3553
Cdd:smart00787 123 KTFARLEAKKMWYEwRMKLLEGL---KEGLDENLEGLKEDYKLL-MKELELLNsikpKLRDRKDALEEELRQLKQLEDEL 198
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988774674 3554 ----QATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERILAEENQKLREKLQQLEDAQKD 3612
Cdd:smart00787 199 edcdPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKK 261
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2529-2783 |
9.24e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.52 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2529 EELKRKSEAEKEAAKQKQKALEDLEKLRMQAEEAERQVKQAEiEKEKQIKVAHEA-AQKSAAAELQSKHMSFAEKTSKLE 2607
Cdd:pfam12795 6 EKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALD-DAPAELRELRQElAALQAKAEAAPKEILASLSLEELE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2608 ESLKQEHGAVLQLQQEAERLKKQQEDAENSREEAEKELEkwrqkanealrlrlqaedeahkktlaqeeaekqkeeaerEA 2687
Cdd:pfam12795 85 QRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLS---------------------------------------EA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2688 KKRAKAEESALKQKEMAEEELERQRKIAESTAQQKLTAE--------------QELIRLRADFDNAEQQRslLEDELYRL 2753
Cdd:pfam12795 126 RQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKAQidmleqellsnnnrQDLLKARRDLLTLRIQR--LEQQLQAL 203
|
250 260 270
....*....|....*....|....*....|....*
gi 1988774674 2754 KNEVAA-----AQQQRKQLEDELAKVRSEMDILIQ 2783
Cdd:pfam12795 204 QELLNEkrlqeAEQAVAQTEQLAEEAAGDHPLVQQ 238
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4971-5005 |
9.30e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.08 E-value: 9.30e-03
10 20 30
....*....|....*....|....*....|....*
gi 1988774674 4971 LLESQAATGYVIDPIKNLKLTVNEAVKMGIVGPEF 5005
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2624-2722 |
9.34e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 40.14 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2624 AERLKKQQEDAEnsrEEAEKELEKWRQKANEalrLRLQAEDEAHKktlaqeeaekqkeeAEREAKKRAKAEesALKQKEM 2703
Cdd:PRK05759 47 AERAKKELELAQ---AKYEAQLAEARAEAAE---IIEQAKKRAAQ--------------IIEEAKAEAEAE--AARIKAQ 104
|
90
....*....|....*....
gi 1988774674 2704 AEEELERQRKIAESTAQQK 2722
Cdd:PRK05759 105 AQAEIEQERKRAREELRKQ 123
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2522-2778 |
9.39e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2522 QKKRQAEEELKrksEAEKEAAKQK--QKALE-DLEKLRMQAEEAERQVKQAeiekekqIKVAHEAAQKSAAAELQSkhms 2598
Cdd:COG1842 30 QAIRDMEEDLV---EARQALAQVIanQKRLErQLEELEAEAEKWEEKARLA-------LEKGREDLAREALERKAE---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2599 faektskLEESLKQEHGAVLQLQQEAERLKKQqedaensREEAEKELEKWRQKANEaLRLRLQAedeahkktlaqeeaek 2678
Cdd:COG1842 96 -------LEAQAEALEAQLAQLEEQVEKLKEA-------LRQLESKLEELKAKKDT-LKARAKA---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2679 qkeeaeREAKKRAKAEESALKQKEmAEEELER-QRKIAESTAQQKLTAEqelirLRADFDnaeqqrslLEDELyrlknev 2757
Cdd:COG1842 145 ------AKAQEKVNEALSGIDSDD-ATSALERmEEKIEEMEARAEAAAE-----LAAGDS--------LDDEL------- 197
|
250 260
....*....|....*....|.
gi 1988774674 2758 aAAQQQRKQLEDELAKVRSEM 2778
Cdd:COG1842 198 -AELEADSEVEDELAALKAKM 217
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
2374-2572 |
9.41e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.17 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2374 KKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQelKLKMQEEVSKREIAAVDAEKQKTNIQLELQELKNLSEQQIKDKSQQ 2453
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAE--KAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2454 VDEALHSRT-KIEEEIRLIRIQLettEKQKYTAESELKQLrdraAEAEKLRKLAQDEAEKLRKQVSEETQKKRQAEEELK 2532
Cdd:pfam00261 79 GRKVLENRAlKDEEKMEILEAQL---KEAKEIAEEADRKY----EEVARKLVVVEGDLERAEERAELAESKIVELEEELK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1988774674 2533 ------RKSEAEKEAAKQKQKALED--------LEKLRMQAEEAERQVKQAEIE 2572
Cdd:pfam00261 152 vvgnnlKSLEASEEKASEREDKYEEqirfltekLKEAETRAEFAERSVQKLEKE 205
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2360-2483 |
9.41e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2360 DEEKAAEKLKAEE-RKKMAEMQAeldkQKQLAEAHAKAIAKAEKEAQELKLKMQEEVskrEIAAVDAEKQKTNIQLELQE 2438
Cdd:PTZ00491 684 ERQKMHDKAKAEEqRTKLLELQA----ESAAVESSGQSRAEALAEAEARLIEAEAEV---EQAELRAKALRIEAEAELEK 756
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1988774674 2439 LKNLSEQQIKdksqqvdealHSRTKIEEEIRLIRiQLETTEKQKY 2483
Cdd:PTZ00491 757 LRKRQELELE----------YEQAQNELEIAKAK-ELADIEATKF 790
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
3442-3619 |
9.50e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.30 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3442 ERLNTSKEAD-DLRKAIADLeneKARLKKEAEELQNKSKEMADAQQKKIEHEKTVLQQtfmteKEMLLKKEKLIEDEKKR 3520
Cdd:pfam05262 184 EALREDNEKGvNFRRDMTDL---KERESQEDAKRAQQLKEELDKKQIDADKAQQKADF-----AQDNADKQRDEVRQKQQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3521 LESQFEE--EVKKAKALKDEQERQKQQMEQEKKTLQATMDAALSKQKEAEEEMLRKQKEMQELERQRLEQERilaEENQK 3598
Cdd:pfam05262 256 EAKNLPKpaDTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQ---KKREP 332
|
170 180
....*....|....*....|.
gi 1988774674 3599 LREKLQQLEDAQKDQHTRETD 3619
Cdd:pfam05262 333 VAEDLQKTKPQVEAQPTSLNE 353
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2346-2540 |
9.58e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2346 QYIKFITDTQRRLDDEEKAAEKLKAEERKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLKMQEEVSKREiaavda 2425
Cdd:pfam13868 159 EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKAR------ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2426 ekqktniqlELQELKNLSEQQIKDKSQQVDEALhsRTKIEEEIRLIRIQLETTEKQKYTAESELKQLRDRAAEAEKLRKL 2505
Cdd:pfam13868 233 ---------QRQELQQAREEQIELKERRLAEEA--EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
170 180 190
....*....|....*....|....*....|....*
gi 1988774674 2506 AQDEAEKLRKQVSEETQKKRQAEEELKRKSEAEKE 2540
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2870-3605 |
9.67e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2870 LKEKEAENERLRRQAEdeayqrkaLEDQASQHKQEIEEKIVQLKKSSEAEMERQKAIVDDTLK-QRRVVEEEIRILKLNF 2948
Cdd:pfam10174 5 LRDLQRENELLRRELD--------IKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKeQYRVTQEENQHLQLTI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 2949 EkASSGKLDLELELNKLKNiaDETQQSKIRAEEeaeklrklaleeekrrREAEEKVKKIAAAEEEAARQRKAalEELERL 3028
Cdd:pfam10174 77 Q-ALQDELRAQRDLNQLLQ--QDFTTSPVDGED----------------KFSTPELTEENFRRLQSEHERQA--KELFLL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3029 RKKAEEArkqkdEADKEAEKQIVVAQ-QAAQKCSAAEQ-QVQSVLAQQIEDSITQKKLKEEYEKAKKLAKEAEAAKEKAE 3106
Cdd:pfam10174 136 RKTLEEM-----ELRIETQKQTLGARdESIKKLLEMLQsKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIH 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3107 REAALLRQQAEEAERQKTAAEEEAANQAKAQ-EDAERLRKEAEFEAAKRAQAEAAALMQKQQADTEM------AKHKKLA 3179
Cdd:pfam10174 211 LREELHRRNQLQPDPAKTKALQTVIEMKDTKiSSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMevykshSKFMKNK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3180 EQTLKQKFQ-VEQELTKVKLKLDETDKQKSVLDEELQRLKDEVdDAVKQRGQV-EEELFKVKVQMEELLKLKNKIEEENQ 3257
Cdd:pfam10174 291 IDQLKQELSkKESELLALQTKLETLTNQNSDCKQHIEVLKESL-TAKEQRAAIlQTEVDALRLRLEEKESFLNKKTKQLQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3258 RLikKDKDSTqklLAEEAENMRKLaedaarLSVEAQEAARLRQIAEDDLNQQRALAEKM--LKEKMQAIQEASrlkaeae 3335
Cdd:pfam10174 370 DL--TEEKST---LAGEIRDLKDM------LDVKERKINVLQKKIENLQEQLRDKDKQLagLKERVKSLQTDS------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3336 mlqKQKDLAQEQAQKLLEDKQLMQQRLEEEteeyHKSLEVERKRQLEIM-AEAERLRLQVSQLSEAQARAEEEAKKFKKQ 3414
Cdd:pfam10174 432 ---SNTDTALTTLEEALSEKERIIERLKEQ----REREDRERLEELESLkKENKDLKEKVSALQPELTEKESSLIDLKEH 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3415 ADKVA-------TRLHETEIATQEKMTVVERLEFERLNTSKEADDLRKA------IADLENEKARLKKEAEELQNKSKEM 3481
Cdd:pfam10174 505 ASSLAssglkkdSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNpeindrIRLLEQEVARYKEESGKAQAEVERL 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988774674 3482 ADAqQKKIEHEKtvlqqtfmtekemlLKKEKLIEDEKKRLESQFEEEVKKAKALKD-EQERQKQQMEQEKKTLQATMDAA 3560
Cdd:pfam10174 585 LGI-LREVENEK--------------NDKDKKIAELESLTLRQMKEQNKKVANIKHgQQEMKKKGAQLLEEARRREDNLA 649
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1988774674 3561 L-SKQKEAEEEMLRKQKEMQELE--RQRL--------EQERILAEENQKLREKLQQ 3605
Cdd:pfam10174 650 DnSQQLQLEELMGALEKTRQELDatKARLsstqqslaEKDGHLTNLRAERRKQLEE 705
|
|
| |
