|
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 ... |
42-151 |
1.14e-72 |
|
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: 238.46 E-value: 1.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 42 DRVQKKTFTKWVNKHLIKHWRaeaqrHVNDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKLRQV 121
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARR-----RVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKI 75
|
90 100 110
....*....|....*....|....*....|
gi 1072265250 122 KLVNIRNDDIADGNPKLTLGLIWTIILHFQ 151
Cdd:cd21188 76 KLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
39-162 |
6.77e-69 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 228.37 E-value: 6.77e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 39 DERDRVQKKTFTKWVNKHLIKhwraeAQRHVNDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKL 118
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK-----AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1072265250 119 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVTGQSE 162
Cdd:cd21235 76 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
164-269 |
8.59e-69 |
|
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: 227.21 E-value: 8.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 164 MTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLD 243
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1072265250 244 PEDVDVPQPDEKSIITYVSSLYDAMP 269
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
34-160 |
1.31e-68 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 227.95 E-value: 1.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 34 LQDAEDERDRVQKKTFTKWVNKHLIKhwraeAQRHVNDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIAL 113
Cdd:cd21236 7 LERYKDERDKVQKKTFTKWINQHLMK-----VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIAL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1072265250 114 DFLKLRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVTGQ 160
Cdd:cd21236 82 DYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
165-269 |
2.19e-64 |
|
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: 214.56 E-value: 2.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDP 244
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1072265250 245 EDVDVPQPDEKSIITYVSSLYDAMP 269
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
39-161 |
1.24e-59 |
|
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: 201.80 E-value: 1.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 39 DERDRVQKKTFTKWVNKHLIKhwraeAQRHVNDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKL 118
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMK-----VRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQ 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1072265250 119 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVTGQS 161
Cdd:cd21237 76 RQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
165-269 |
8.57e-56 |
|
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: 190.20 E-value: 8.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAEReLGVTRLLDP 244
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1072265250 245 EDVDVPQPDEKSIITYVSSLYDAMP 269
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
163-269 |
9.43e-51 |
|
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: 176.00 E-value: 9.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 163 DMTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAEReLGVTRLL 242
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1072265250 243 DPEDVDVPQPDEKSIITYVSSLYDAMP 269
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
44-152 |
2.03e-47 |
|
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: 166.40 E-value: 2.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 44 VQKKTFTKWVNKHLIKhwraEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKLRQVKL 123
Cdd:cd21186 2 VQKKTFTKWINSQLSK----ANKPPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKL 77
|
90 100
....*....|....*....|....*....
gi 1072265250 124 VNIRNDDIADGNPKLTLGLIWTIILHFQI 152
Cdd:cd21186 78 VNISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
39-148 |
3.77e-46 |
|
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: 162.92 E-value: 3.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 39 DERDRVQKKTFTKWVNKHLIKHwraeaQRHVNDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLK 117
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARV-----GCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLK 85
|
90 100 110
....*....|....*....|....*....|.
gi 1072265250 118 LRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 148
Cdd:cd21246 86 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
165-265 |
1.23e-44 |
|
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: 158.34 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDP 244
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1072265250 245 EDVDVPQPDEKSIITYVSSLY 265
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
40-152 |
1.33e-44 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 158.31 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 40 ERDRVQKKTFTKWVNKHLIKHwraEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLK 117
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKR---KPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLE 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1072265250 118 LRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 152
Cdd:cd21241 78 SKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
165-265 |
3.55e-42 |
|
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: 151.39 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDP 244
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1072265250 245 EDVDVPQPDEKSIITYVSSLY 265
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
38-265 |
5.31e-42 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 166.27 E-value: 5.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 38 EDERDRVQKKTFTKWVNKHLIKhwraEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDF 115
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLIS----GGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 116 LKLRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvtgQSEDMTAKEKLLLWSQRMSEGYQ-GLRCDNFTSNWR 194
Cdd:COG5069 79 IKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 195 DGRLFSAIIHRHKPMLIDMNRVYRQTNLE--NLDQAFTVAERELGVTRLLDPEDV-DVPQPDEKSIITYVSSLY 265
Cdd:COG5069 156 DGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
33-148 |
1.54e-41 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 149.75 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 33 ALQDaedERDRVQKKTFTKWVNKHLIKHwraeaQRHVNDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQI 111
Cdd:cd21193 8 ALQE---ERINIQKKTFTKWINSFLEKA-----NLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNK 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 1072265250 112 ALDFLKlRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 148
Cdd:cd21193 80 ALAFLK-TKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
40-152 |
2.40e-41 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 149.26 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 40 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhVNDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLK 117
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIV---INDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1072265250 118 LRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 152
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
39-148 |
6.26e-40 |
|
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: 146.32 E-value: 6.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 39 DERDRVQKKTFTKWVNKHLikhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLK 117
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHL-----ARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLK 107
|
90 100 110
....*....|....*....|....*....|.
gi 1072265250 118 LRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 148
Cdd:cd21318 108 EQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1362-2385 |
7.76e-39 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 161.15 E-value: 7.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1362 AEVEDQLEKQRQLAEAHAQAkAVAEKEALELRMNMQEE------VTRREVVAVDAEQQKKTIQQELHQMKNNSETEIKAK 1435
Cdd:NF041483 185 AEAERLAEEARQRLGSEAES-ARAEAEAILRRARKDAErllnaaSTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1436 VKLIEEAEYN-RKKVEEEIRIIRIQLETSQKQKSGAE--DELRALRARAE------EAERQKKLAQEEAERLRKQVKDEA 1506
Cdd:NF041483 264 EQRMQEAEEAlREARAEAEKVVAEAKEAAAKQLASAEsaNEQRTRTAKEEiarlvgEATKEAEALKAEAEQALADARAEA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1507 QKKREAEDELHRKVQAEKDAAREKQ----------KALEDL-EKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADA 1575
Cdd:NF041483 344 EKLVAEAAEKARTVAAEDTAAQLAKaartaeevltKASEDAkATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGA 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1576 ELQSKRmSFLEKTTQLemslkqehitvthlQEEAERLK--KQQLEAETAKEEAEKELEKWR---QKANEALRlrlQAEEI 1650
Cdd:NF041483 424 AKDDTK-EYRAKTVEL--------------QEEARRLRgeAEQLRAEAVAEGERIRGEARReavQQIEEAAR---TAEEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1651 AHK--------KTLAQEEAEKQKEDA-ERETRKRTKAEESALRqkdlAEEELEKQRKLAEETA-SHKLSAEQELIRLKAE 1720
Cdd:NF041483 486 LTKakadadelRSTATAESERVRTEAiERATTLRRQAEETLER----TRAEAERLRAEAEEQAeEVRAAAERAARELREE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1721 VDSG-EQHRIVLEEDLFRLKNEvneAIQRRRGLEEELAKVRAEMEILlkAKSKAEEDSRSTSEKS------KQMLEVEAS 1793
Cdd:NF041483 562 TERAiAARQAEAAEELTRLHTE---AEERLTAAEEALADARAEAERI--RREAAEETERLRTEAAerirtlQAQAEQEAE 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1794 KLR-ELAEEAARLRAVSE------------EAKRQRQLAEEDATRQRAEA----ERILKEKLTAIN----EATRMRTEAE 1852
Cdd:NF041483 637 RLRtEAAADASAARAEGEnvavrlrseaaaEAERLKSEAQESADRVRAEAaaaaERVGTEAAEALAaaqeEAARRRREAE 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1853 IAL--KEKEAENERLR--------------RLAEDEAYQRKLLEEQ----------AAQHKQDI-----------EEKIH 1895
Cdd:NF041483 717 ETLgsARAEADQERERareqseellasarkRVEEAQAEAQRLVEEAdrratelvsaAEQTAQQVrdsvaglqeqaEEEIA 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1896 QLKQSSENELERQKTIVDETLKHRRVIEEEIRilkinfEKASVGKSDLELELQklkniaDETQKSKEKAEQD-----AEK 1970
Cdd:NF041483 797 GLRSAAEHAAERTRTEAQEEADRVRSDAYAER------ERASEDANRLRREAQ------EETEAAKALAERTvseaiAEA 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1971 QRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKikaDEAKKQKDLAEKEAekqiqlAQDAARLKIDAEE 2050
Cdd:NF041483 865 ERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIR---SDAAAQADRLIGEA------TSEAERLTAEARA 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2051 KAyyaavqqkEQEMLQTRIQEQSIYDKLKEEAEK-AKRAAEEAERAKIKAEHEAALSRQQAE----EAERLKQKAEIEA- 2124
Cdd:NF041483 936 EA--------ERLRDEARAEAERVRADAAAQAEQlIAEATGEAERLRAEAAETVGSAQQHAErirtEAERVKAEAAAEAe 1007
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2125 QAKGQAQEDAEKVRKEAELEAAKR-----GQAEQAALKLKQMADAEMEKHKQFAEKTVRQKEqvegeltkvklqlEETDH 2199
Cdd:NF041483 1008 RLRTEAREEADRTLDEARKDANKRrseaaEQADTLITEAAAEADQLTAKAQEEALRTTTEAE-------------AQADT 1074
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2200 QKAILDDELGRLKEEVTesLRQKKLVEeelfKVKIQMEELVKLKLRIEQENKmlilkgkDNTQQFLAEEAEKMKQVAEEA 2279
Cdd:NF041483 1075 MVGAARKEAERIVAEAT--VEGNSLVE----KARTDADELLVGARRDATAIR-------ERAEELRDRITGEIEELHERA 1141
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2280 ARLSVEAQEAA-----RLRKIAEDDLNEQRALAEKILKE--------KMQAVQEASRLKAEAEmlQKQKEMAMEqAKKLQ 2346
Cdd:NF041483 1142 RRESAEQMKSAgercdALVKAAEEQLAEAEAKAKELVSDanseaskvRIAAVKKAEGLLKEAE--QKKAELVRE-AEKIK 1218
|
1130 1140 1150
....*....|....*....|....*....|....*....
gi 1072265250 2347 EDKEQMQQQLAEETegfQKTLEAERRRQLDISAEAERLK 2385
Cdd:NF041483 1219 AEAEAEAKRTVEEG---KRELDVLVRRREDINAEISRVQ 1254
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
164-269 |
8.55e-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: 8.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 164 MTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLD 243
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1072265250 244 PEDVDVPQPDEKSIITYVSSLYDAMP 269
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
152-267 |
1.34e-38 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 141.35 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 152 ISDIQVtgqsEDMTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTV 231
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1072265250 232 AERELGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 267
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
40-152 |
2.07e-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: 140.74 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 40 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhVNDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKLR 119
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSV---VSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNK 77
|
90 100 110
....*....|....*....|....*....|...
gi 1072265250 120 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 152
Cdd:cd21242 78 SIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
38-148 |
3.36e-38 |
|
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: 140.96 E-value: 3.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 38 EDERDRVQKKTFTKWVNKHLikhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFL 116
Cdd:cd21317 25 ADEREAVQKKTFTKWVNSHL-----ARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFL 99
|
90 100 110
....*....|....*....|....*....|..
gi 1072265250 117 KLRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 148
Cdd:cd21317 100 KEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1684-2563 |
2.12e-37 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 156.84 E-value: 2.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1684 RQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEedlFRLKNEVNEAIQRRRGLEEELAKVRAEM 1763
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEE---ARKAEDARKAEEARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1764 EILLKAK-SKAEEDSRSTSEKSKQMLEVEASKLRElAEEAARLravsEEAKRQRQLAEEDATRQRAEAERIlkEKLTAIN 1842
Cdd:PTZ00121 1161 EDARKAEeARKAEDAKKAEAARKAEEVRKAEELRK-AEDARKA----EAARKAEEERKAEEARKAEDAKKA--EAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1843 EATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQ-HKQDIEEKIHQLKQSSENELERQKTIVDETLKH--- 1918
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEaRKADELKKAEEKKKADEAKKAEEKKKADEAKKKaee 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1919 -------RRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDaEKQRQLALVEEARRKEAEEKVKK 1991
Cdd:PTZ00121 1314 akkadeaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA-EKKKEEAKKKADAAKKKAEEKKK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1992 IIAAEQEAGRQRKVA--LEEVERLKIKADEAKKQKDLAEK--EAEKQIQLAQDAARLKIDAEEKayyaavqqKEQEMLQT 2067
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKAdeLKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEAKKADEAKKKAEEA--------KKAEEAKK 1464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2068 RIQEQSIYDKLKEEAEKAKRAAE---EAERAKIKAEHeaalSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELE 2144
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEakkKAEEAKKKADE----AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2145 AAKRGQAEQAALKLKQMADAEmEKHKqfAEKTVRQKEQVEGELTKVKlqlEETDHQKAILDDELGRLKEEVTESLRQKKL 2224
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAE-EKKK--AEEAKKAEEDKNMALRKAE---EAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2225 VEEElfkvKIQMEELVKlklriEQENKmlilKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKiaeddlnEQR 2304
Cdd:PTZ00121 1615 AEEA----KIKAEELKK-----AEEEK----KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE-------EDK 1674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2305 ALAEKILKEKMQAVQEASRLKAEAEmlqkQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRrqldisAEAERL 2384
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAE----EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE------AEEDKK 1744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2385 KLQvvemsksQAKAEEDAKKfrKQAEDISEKLHQTELSTKEKMTVVhtleiqRQHSDKEAEELRKAIADLENEKEKLKKE 2464
Cdd:PTZ00121 1745 KAE-------EAKKDEEEKK--KIAHLKKEEEKKAEEIRKEKEAVI------EEELDEEDEKRRMEVDKKIKDIFDNFAN 1809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2465 AELLQKKSEEMQKAQKEQLRQETqtlqstflteKQILIQKEKYIEEEKAKLEKLF--DNEVGKAQKLKSEKERQLAQLEE 2542
Cdd:PTZ00121 1810 IIEGGKEGNLVINDSKEMEDSAI----------KEVADSKNMQLEEADAFEKHKFnkNNENGEDGNKEADFNKEKDLKED 1879
|
890 900
....*....|....*....|..
gi 1072265250 2543 -EKRLLQTSMDdamkKQLDAED 2563
Cdd:PTZ00121 1880 dEEEIEEADEI----EKIDKDD 1897
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1366-2416 |
2.69e-37 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 156.14 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1366 DQL--EKQRQLAEAHAQAKAVAEKEAlELRMNMQEEVtrrevvAVDAEQQKKTIQQELHQMKNNSETEIKAKVKLieeAE 1443
Cdd:NF041483 86 DQLraDAERELRDARAQTQRILQEHA-EHQARLQAEL------HTEAVQRRQQLDQELAERRQTVESHVNENVAW---AE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1444 YNRKKVEEEIRIIriqLETSQKQksgAEDELRALRARAE-------------------EAERQKKLAQEEAERLRKQVKD 1504
Cdd:NF041483 156 QLRARTESQARRL---LDESRAE---AEQALAAARAEAErlaeearqrlgseaesaraEAEAILRRARKDAERLLNAAST 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1505 EAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQaeEAERRMKQAELEKERQIKQAHDVAqqsadaelqSKRMSF 1584
Cdd:NF041483 230 QAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAA---------AKQLAS 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1585 LEKTTQLEMSLKQEHIT--VTHLQEEAERLKKQQLEAETAKEEaekelekwrqkanEALRLRLQAEEIAhkKTLAQEEAE 1662
Cdd:NF041483 299 AESANEQRTRTAKEEIArlVGEATKEAEALKAEAEQALADARA-------------EAEKLVAEAAEKA--RTVAAEDTA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1663 KQKEDAERETRK-RTKAEESALRQKDLAEEELEKQRKLAEETAShKLSAEQELI--RLK-AEVDSGEQHR---IVLEEDL 1735
Cdd:NF041483 364 AQLAKAARTAEEvLTKASEDAKATTRAAAEEAERIRREAEAEAD-RLRGEAADQaeQLKgAAKDDTKEYRaktVELQEEA 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1736 FRLKNEvneAIQRRRGLEEELAKVRAEM----------------EILLKAKSKAEE---DSRSTSEKSKQMLEVEASKLR 1796
Cdd:NF041483 443 RRLRGE---AEQLRAEAVAEGERIRGEArreavqqieeaartaeELLTKAKADADElrsTATAESERVRTEAIERATTLR 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1797 ELAE--------EAARLRAVSEE-AKRQRQLAEEDATRQRAEAER-ILKEKLTAINEATRMRTEAE-------IALKEKE 1859
Cdd:NF041483 520 RQAEetlertraEAERLRAEAEEqAEEVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAEerltaaeEALADAR 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1860 AENERLRRLAEDEAYQrklLEEQAAqhkqdieEKIHQLKQSSENELERQKTIVDETLKHRRVIEEEIrilkinfekASVG 1939
Cdd:NF041483 600 AEAERIRREAAEETER---LRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAARAEGENV---------AVRL 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1940 KSDLELELQKLKNIADETqKSKEKAEQDAEKQRQLAlveearrkeaeEKVKKIIAAEQEAGRQRKVALEEVERLKIKADE 2019
Cdd:NF041483 661 RSEAAAEAERLKSEAQES-ADRVRAEAAAAAERVGT-----------EAAEALAAAQEEAARRRREAEETLGSARAEADQ 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2020 ----AKKQKDLAEKEAEKQIQLAQ-DAARLKIDAEEKAYyAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEE-AE 2093
Cdd:NF041483 729 ererAREQSEELLASARKRVEEAQaEAQRLVEEADRRAT-ELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHaAE 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2094 RAKIKAEheaalsrqqaEEAERLKQKAEIEAQakgQAQEDAEKVRKEA--ELEAAKR------GQAEQAALKLKQMADAE 2165
Cdd:NF041483 808 RTRTEAQ----------EEADRVRSDAYAERE---RASEDANRLRREAqeETEAAKAlaertvSEAIAEAERLRSDASEY 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2166 MEKHKQFAEKTVRQKEQvegelTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELfkvkiqMEELVKLKLR 2245
Cdd:NF041483 875 AQRVRTEASDTLASAEQ-----DAARTRADAREDANRIRSDAAAQADRLIGEATSEAERLTAEA------RAEAERLRDE 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2246 IEQENKMLILKGKDNTQQFLAE---EAEKMKqvAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEkmqAVQEAS 2322
Cdd:NF041483 944 ARAEAERVRADAAAQAEQLIAEatgEAERLR--AEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTE---AREEAD 1018
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2323 RLKAEA-EMLQKQKEMAMEQAKKLQEDKEQMQQQLAEE--TEGFQKTLEAERRRQLDISA---EAERLKLQ-------VV 2389
Cdd:NF041483 1019 RTLDEArKDANKRRSEAAEQADTLITEAAAEADQLTAKaqEEALRTTTEAEAQADTMVGAarkEAERIVAEatvegnsLV 1098
|
1130 1140 1150
....*....|....*....|....*....|..
gi 1072265250 2390 EMSKSQAK-----AEEDAKKFRKQAEDISEKL 2416
Cdd:NF041483 1099 EKARTDADellvgARRDATAIRERAEELRDRI 1130
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
164-265 |
3.77e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 136.92 E-value: 3.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 164 MTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLD 243
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1072265250 244 PEDVDVPQPDEKSIITYVSSLY 265
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
161-265 |
3.83e-37 |
|
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: 137.06 E-value: 3.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 161 SEDMTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTR 240
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1072265250 241 LLDPEDVDVPQPDEKSIITYVSSLY 265
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
161-265 |
5.80e-36 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 134.03 E-value: 5.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 161 SEDMTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTR 240
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1072265250 241 LLDPEDVDVPQPDEKSIITYVSSLY 265
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
42-148 |
8.90e-36 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 132.90 E-value: 8.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 42 DRVQKKTFTKWVNKHLIKhwraeAQRHVNDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKLRQ 120
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRK-----AGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKG 77
|
90 100
....*....|....*....|....*...
gi 1072265250 121 VKLVNIRNDDIADGNPKLTLGLIWTIIL 148
Cdd:cd21214 78 VKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
44-150 |
1.14e-35 |
|
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: 132.52 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 44 VQKKTFTKWVNKHLikhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKLRQV 121
Cdd:cd21215 4 VQKKTFTKWLNTKL-----SSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGV 78
|
90 100
....*....|....*....|....*....
gi 1072265250 122 KLVNIRNDDIADGNPKLTLGLIWTIILHF 150
Cdd:cd21215 79 KLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1858-2624 |
3.77e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 149.52 E-value: 3.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1858 KEAENERLRRLAEDEAYQ--RKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKTIVDETLKHRRVIE----EEIRILKI 1931
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEeaFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEarkaEDAKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1932 NFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEagrQRKVALEEVE 2011
Cdd:PTZ00121 1157 ARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA---KKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2012 RLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYA--------------------AVQQKEQEMLQTRIQE 2071
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEArkadelkkaeekkkadeakkAEEKKKADEAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2072 QSIYDKLKEEAEKAKRAAEE----AERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAElEAAK 2147
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAakkkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2148 RGQAEQAALKLKQMADaEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAildDELGRLKEEVTESLRQKKLVEE 2227
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKAD-ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA---DEAKKKAEEAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2228 elfkvKIQMEELVKlklRIEQENKMLILKGKDNTQQFLAEEAEKmkqvAEEAARLSVEAQEAARLRKIAEDDLNEQRALA 2307
Cdd:PTZ00121 1469 -----AKKADEAKK---KAEEAKKADEAKKKAEEAKKKADEAKK----AAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2308 EKIlkEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKeQMQQQLAEETEgfqktlEAERRRQLDISAEAERLKLQ 2387
Cdd:PTZ00121 1537 DEA--KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK-NMALRKAEEAK------KAEEARIEEVMKLYEEEKKM 1607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2388 VVEMSKSQAKAEEDAKKFRKqAEDISEKLHQTELSTKEKMtvvhtleiqrqhsdKEAEELRKAIADLENEKEKLKKEAEL 2467
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEK--------------KKAEELKKAEEENKIKAAEEAKKAEE 1672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2468 LQKKSEEMQKAQKEQLRQETQTLQStfltekqiliqkekyiEEEKAKLE---KLFDNEVGKAQKLKSEKERQLAQLEEEK 2544
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKE----------------AEEAKKAEelkKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2545 RLLQTSMDDAMKKQLDAEDRirqkqEELQQLDKKRQEQERLLEEENRK-LRERLEQLEQEHRIALEKTREVIITKETVIT 2623
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEK-----KKIAHLKKEEEKKAEEIRKEKEAvIEEELDEEDEKRRMEVDKKIKDIFDNFANII 1811
|
.
gi 1072265250 2624 Q 2624
Cdd:PTZ00121 1812 E 1812
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1398-2231 |
7.39e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 148.37 E-value: 7.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1398 EEVTrrEVVAVDAEQQKKTIQQELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRAL 1477
Cdd:PTZ00121 1030 EELT--EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTE 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1478 RARAEEaERQKKLAQEEAERLRKqvkdeAQKKREAED--ELHRKVQAEKDAAREKQKALEDLEKFRL-----QAEEAERR 1550
Cdd:PTZ00121 1108 TGKAEE-ARKAEEAKKKAEDARK-----AEEARKAEDarKAEEARKAEDAKRVEIARKAEDARKAEEarkaeDAKKAEAA 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1551 MKQAELEKERQIKQAHDVAQQSADAELQSKRMsfLEKTTQLEMSLKQEHIT----VTHLQEEAERLKKQQLEAETAKEEA 1626
Cdd:PTZ00121 1182 RKAEEVRKAEELRKAEDARKAEAARKAEEERK--AEEARKAEDAKKAEAVKkaeeAKKDAEEAKKAEEERNNEEIRKFEE 1259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1627 EKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESalRQKDLAEEELEKQRKLAEETash 1706
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADAA--- 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1707 KLSAEQElirlkaevdsgeqhrivleedlfRLKNEVNEAiqrrrglEEELAKVRAEmeillKAKSKAEEDSRSTSEKSKQ 1786
Cdd:PTZ00121 1335 KKKAEEA-----------------------KKAAEAAKA-------EAEAAADEAE-----AAEEKAEAAEKKKEEAKKK 1379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1787 mleveASKLRELAEEAARlravSEEAKRQrqlAEEDatRQRAEAeriLKEKLTAINEATRMRTEAEIALKEKEAENERLR 1866
Cdd:PTZ00121 1380 -----ADAAKKKAEEKKK----ADEAKKK---AEED--KKKADE---LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE 1442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1867 RLAEDEAYQRKLLEEQAAQHKQDIEE--KIHQLKQSSEnelerQKTIVDETLKHRRVIEEEIRILKinfEKASVGKSDLE 1944
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEakKADEAKKKAE-----EAKKADEAKKKAEEAKKKADEAK---KAAEAKKKADE 1514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1945 LELQKLKNIADETQKSKEKAEQD----AEKQRQLALVEEARRKEAEEKVKKIIAAEQEAGRqRKVALEEVERLKiKADEA 2020
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADeakkAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED-KNMALRKAEEAK-KAEEA 1592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2021 KKQKDLAEKEAEKQIQlaqdAARLKIDAEEKAYYAAVQQKEQEmlqtRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAE 2100
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMK----AEEAKKAEEAKIKAEELKKAEEE----KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA 1664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2101 HEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAEL---EAAKRGQAEQAAlKLKQMADAEMEKHKQFAEKTV 2177
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELkkkEAEEKKKAEELK-KAEEENKIKAEEAKKEAEEDK 1743
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1072265250 2178 RQKEQV---EGELTKV-KLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELFK 2231
Cdd:PTZ00121 1744 KKAEEAkkdEEEKKKIaHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1855-2636 |
1.82e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 147.21 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1855 LKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENE-LERQKTIVDETLKHRRVIEEEIRILKINF 1933
Cdd:PTZ00121 1042 LKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEaTEEAFGKAEEAKKTETGKAEEARKAEEAK 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1934 EKASVGKSDLELELQKLKNIADETQKSKEkaEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVAL---EEV 2010
Cdd:PTZ00121 1122 KKAEDARKAEEARKAEDARKAEEARKAED--AKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELrkaEDA 1199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2011 ERLKI--KADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAyyAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKA--K 2086
Cdd:PTZ00121 1200 RKAEAarKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK--KAEEERNNEEIRKFEEARMAHFARRQAAIKAeeA 1277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2087 RAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEiEAQAKGQAQEDAEKVRKEAEleAAKRgQAEQAAlKLKQMADAEM 2166
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKAEEKKKADEAKKKAE-EAKKADEAKKKAEEAKKKAD--AAKK-KAEEAK-KAAEAAKAEA 1352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2167 EKHKQFAEKTVRQKEQVEGELTKVKLQLEETDhQKAilddELGRLKEEVTESLRQKKLVEEELFKVKIQMEELVKLKLRI 2246
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAK-KKA----EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA 1427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2247 EQENKMLILKGKdntqqflAEEAEKmkqvAEEAARLSVEAQEAARLRKIAEddlnEQRALAEkiLKEKMQAVQEASRLKA 2326
Cdd:PTZ00121 1428 EEKKKADEAKKK-------AEEAKK----ADEAKKKAEEAKKAEEAKKKAE----EAKKADE--AKKKAEEAKKADEAKK 1490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2327 EAEMLQKQKEmamEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKlQVVEMSKSQA--KAEE--DA 2402
Cdd:PTZ00121 1491 KAEEAKKKAD---EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK-KADELKKAEElkKAEEkkKA 1566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2403 KKFRKQAEDISEKLHQTELSTK-EKMTVVHTLEIQRQHSDKEAEELRKAiaDLENEKEKLKKEAELLQKKSEEMQKAQKE 2481
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2482 QLRQETQTLQStfltEKQILIQKEKyiEEEKAKLEKLFDNEVGKAQKLKSEKERQLAQLEEEKRllqtSMDDAMKKQLDA 2561
Cdd:PTZ00121 1645 EKKKAEELKKA----EEENKIKAAE--EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK----KAEELKKKEAEE 1714
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072265250 2562 EDRIRQKQEELQQLDKKRQEQERLLEEENRKLRERLEQLEQEHRIALEKTREVIITKETVITQTKTMPNGRDAAD 2636
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
39-152 |
2.59e-34 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 128.89 E-value: 2.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 39 DERDRVQKKTFTKWVNKHLIKHWRaeaqRHVNDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKL 118
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGK----PPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQK 76
|
90 100 110
....*....|....*....|....*....|....
gi 1072265250 119 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 152
Cdd:cd21231 77 NNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1355-1892 |
4.31e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 145.08 E-value: 4.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1355 EQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQQKKTIQQELHQMKNNSETEIKA 1434
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1435 KVKLIEEAEyNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAED 1514
Cdd:COG1196 315 EERLEELEE-ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1515 ELHRKVQAEKDAAREKQKALEDLEkfRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQSKRMSFLEKTTQLEMS 1594
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLE--RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1595 LKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRK 1674
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1675 RTKAEESALRQKDLAEEE---------LEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNE- 1744
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAr 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1745 ---AIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKskqmLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEE 1821
Cdd:COG1196 632 leaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA----LLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072265250 1822 DATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEE 1892
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1368-2142 |
5.60e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 145.67 E-value: 5.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1368 LEKQRQLAEAHAQAKAVAEKEALELRM--NMQEEVTRREVVAVDAEQQKKTIQQELHQMKNNSETEIKAKV-KLIEEAEY 1444
Cdd:PTZ00121 1026 IEKIEELTEYGNNDDVLKEKDIIDEDIdgNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAfGKAEEAKK 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1445 NRKKVEEEIRiiriqleTSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAED----ELHRKV 1520
Cdd:PTZ00121 1106 TETGKAEEAR-------KAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEarkaEDAKKA 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1521 QAEKDA-----AREKQKALEDLEKFRLQAEEAERRMKQA-ELEKERQIKQAHDVAQQSADAElQSKRMsflEKTTQLEMS 1594
Cdd:PTZ00121 1179 EAARKAeevrkAEELRKAEDARKAEAARKAEEERKAEEArKAEDAKKAEAVKKAEEAKKDAE-EAKKA---EEERNNEEI 1254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1595 LKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRlrlQAEEiAHKKTLAQEEAEKQKEDAERETRK 1674
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK---KADE-AKKKAEEAKKADEAKKKAEEAKKK 1330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1675 RTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDlfRLKNEVNEAIQRRRGLEE 1754
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK--KKADEAKKKAEEDKKKAD 1408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1755 ELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAAR---LRAVSEEAKRQRQLAEEDATRQRA-EA 1830
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaeeAKKKAEEAKKADEAKKKAEEAKKAdEA 1488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1831 ERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEE--KIHQLKQSSENELERQ 1908
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkKAEELKKAEEKKKAEE 1568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1909 KTIVDEtlkHRRVIEEEIRILKINFEKASVGKSDLELELQKLKniADETQKSKE---KAEQ--DAEKQRQLALVEEARRK 1983
Cdd:PTZ00121 1569 AKKAEE---DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK--AEEAKKAEEakiKAEElkKAEEEKKKVEQLKKKEA 1643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1984 EAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAE---KQIQLAQDAARLKIDAEEKAYYAAVQQK 2060
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEalkKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2061 EQEMLQTRIQEqsiydkLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQkaEIEAQAKGQAQEDAEKVRKE 2140
Cdd:PTZ00121 1724 AEEENKIKAEE------AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK--EKEAVIEEELDEEDEKRRME 1795
|
..
gi 1072265250 2141 AE 2142
Cdd:PTZ00121 1796 VD 1797
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
168-269 |
1.89e-33 |
|
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: 126.39 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 168 EKLLL-WSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDPED 246
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1072265250 247 VDVPQPDEKSIITYVSSLYDAMP 269
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
149-265 |
2.49e-33 |
|
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: 127.09 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 149 HFQISDIQVTGQSEDMTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQA 228
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1072265250 229 FTVAERELGVTRLLDPEDVDVPQPDEKSIITYVSSLY 265
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1662-2239 |
6.68e-32 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 137.76 E-value: 6.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1662 EKQKEDAER----ETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFR 1737
Cdd:COG1196 206 ERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1738 LKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAvSEEAKRQRQ 1817
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1818 LAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQL 1897
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1898 KQSSENELERQKTIVDETLKHRRVIEEEIRILK-INFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLAL 1976
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAaLAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1977 VEEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAY-YA 2055
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVdLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2056 AVQQKEQEMLQTRIQEQSIydklkeEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAE 2135
Cdd:COG1196 605 ASDLREADARYYVLGDTLL------GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2136 KVRKEAELEAAKRGQAEQAALKLKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEV 2215
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570 580
....*....|....*....|....
gi 1072265250 2216 TESLRQkklVEEELFKVKIQMEEL 2239
Cdd:COG1196 759 PPDLEE---LERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1437-2071 |
1.10e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 136.99 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1437 KLIEEA----EYNRKKVE------------EEIRIIRIQLEtsqKQksgaedeLRALRARAEEAERQKKLaQEEAERLRK 1500
Cdd:COG1196 159 AIIEEAagisKYKERKEEaerkleateenlERLEDILGELE---RQ-------LEPLERQAEKAERYREL-KEELKELEA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1501 QVKdeAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKfrLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQSK 1580
Cdd:COG1196 228 ELL--LLKLRELEAELEELEAELEELEAELEELEAELAE--LEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1581 RMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEE 1660
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1661 AEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKN 1740
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1741 EVNEAIQRRRGLEEELAKVRAEmeillKAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAE 1820
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEE-----LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1821 EDATRQRAEAERILKEkltaineatRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQS 1900
Cdd:COG1196 539 ALEAALAAALQNIVVE---------DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1901 SENELER--QKTIVDETLKHRRVIEEEIRILKINFEKASVgksdlELELQKLKNIADETQKSKEKAEQDAEKQRQLALVE 1978
Cdd:COG1196 610 EADARYYvlGDTLLGRTLVAARLEAALRRAVTLAGRLREV-----TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1979 EARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKD-LAEKEAEKQIQLAQDAARLKIDAEEKAYYAAV 2057
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEaEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
650
....*....|....
gi 1072265250 2058 QQKEQEMLQTRIQE 2071
Cdd:COG1196 765 LERELERLEREIEA 778
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
164-262 |
2.45e-31 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 120.22 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 164 MTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLD 243
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1072265250 244 PEDVDVPQPDEKSIITYVS 262
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
893-969 |
9.53e-31 |
|
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: 117.70 E-value: 9.53e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 893 LSYQYLLRDFQLIQSWTLVTFRSMISEEYSLALRNLEIHYQDFLKDSQDSQNFQPDDRMNIEREYSSCTQKYDMLLR 969
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLV 77
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
152-267 |
1.01e-30 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 118.78 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 152 ISDIQvtgqSEDMTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTV 231
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1072265250 232 AERELGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 267
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1398-1959 |
1.01e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 133.91 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1398 EEVTRR-EVVAVDAEQQKK--TIQQELHqmknnsETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDEL 1474
Cdd:COG1196 196 GELERQlEPLERQAEKAERyrELKEELK------ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1475 RALRARAEEAERQKKLAQE-------EAERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEA 1547
Cdd:COG1196 270 EELRLELEELELELEEAQAeeyellaELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1548 ERRMKQAELEKERQIKQAHDVAQQSADAE-----LQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETA 1622
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEeeleeLAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1623 KEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEE 1702
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1703 TASHKLSAEQELIR--LKAEVDSGEQHRIVLEEDLF-RLKNEVNEAIQRRRGLEEELAKV---RAEMEILLKAKSKAEED 1776
Cdd:COG1196 510 VKAALLLAGLRGLAgaVAVLIGVEAAYEAALEAALAaALQNIVVEDDEVAAAAIEYLKAAkagRATFLPLDKIRARAALA 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1777 SRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKL--TAINEATRMRTEAEIA 1854
Cdd:COG1196 590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLegEGGSAGGSLTGGSRRE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1855 LKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKTIVDETLKHRRVIEEEIRILKINFE 1934
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
570 580
....*....|....*....|....*
gi 1072265250 1935 KASVGKSDLELELQKLKNIADETQK 1959
Cdd:COG1196 750 EEALEELPEPPDLEELERELERLER 774
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
165-265 |
1.04e-30 |
|
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: 118.66 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDP 244
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1072265250 245 EDVDVPQPDEKSIITYVSSLY 265
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
170-265 |
1.12e-30 |
|
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: 118.60 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 170 LLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDPED-VD 248
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1072265250 249 VPQPDEKSIITYVSSLY 265
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
39-148 |
1.35e-30 |
|
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: 120.15 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 39 DERDRVQKKTFTKWVNKHLikhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLK 117
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHL-----ARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLK 122
|
90 100 110
....*....|....*....|....*....|.
gi 1072265250 118 LRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 148
Cdd:cd21316 123 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
44-152 |
1.86e-30 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 117.80 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 44 VQKKTFTKWVNKHLIKhwraEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKLRQVKL 123
Cdd:cd21232 2 VQKKTFTKWINARFSK----SGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVEL 77
|
90 100
....*....|....*....|....*....
gi 1072265250 124 VNIRNDDIADGNPKLTLGLIWTIILHFQI 152
Cdd:cd21232 78 VNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
164-262 |
2.69e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 117.63 E-value: 2.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 164 MTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLD 243
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1072265250 244 PEDVDVPQPDEKSIITYVS 262
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
40-154 |
4.30e-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: 116.91 E-value: 4.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 40 ERDRVQKKTFTKWVNKHLIKhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLK 117
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEK---CNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLE 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1072265250 118 LRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 154
Cdd:cd21191 78 DSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
37-153 |
5.71e-30 |
|
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: 117.17 E-value: 5.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 37 AED-ERDRVQKKTFTKWVNKHLIKhwraeAQRHVNDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIAL 113
Cdd:cd21311 7 AEDaQWKRIQQNTFTRWANEHLKT-----ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVAL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1072265250 114 DFLKLRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 153
Cdd:cd21311 82 KFLEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
168-269 |
1.64e-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: 115.05 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 168 EKLLL-WSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDPED 246
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1072265250 247 VDVPQPDEKSIITYVSSLYDAMP 269
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1365-2195 |
1.79e-29 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 130.33 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1365 EDQLEKQRQLAEAHAQA---KAVAEKEALELR---MNMQEEVTRrevVAVDAEQQKKTIQQELHQMKNNSETEikaKVKL 1438
Cdd:NF041483 401 EAEAEADRLRGEAADQAeqlKGAAKDDTKEYRaktVELQEEARR---LRGEAEQLRAEAVAEGERIRGEARRE---AVQQ 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1439 IEEAEYNRKKVEEEIRIIRIQLET-----SQKQKSGAEDELRALRARAEEA-ERqkklAQEEAERLRKQVKDEAQKKREA 1512
Cdd:NF041483 475 IEEAARTAEELLTKAKADADELRStataeSERVRTEAIERATTLRRQAEETlER----TRAEAERLRAEAEEQAEEVRAA 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1513 EDELHRKVQAEKDAAREKQKALEDLEKFRLQAeEAERRMKQAElekerqikqahdVAQQSADAELQSKRMSFLEKTTQLE 1592
Cdd:NF041483 551 AERAARELREETERAIAARQAEAAEELTRLHT-EAEERLTAAE------------EALADARAEAERIRREAAEETERLR 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1593 MSLKQEHITV-THLQEEAERLKKQQLEAETAKEEaekelekwrQKANEALRLRLQAEEIAHK-KTLAQEEAEKQKED--- 1667
Cdd:NF041483 618 TEAAERIRTLqAQAEQEAERLRTEAAADASAARA---------EGENVAVRLRSEAAAEAERlKSEAQESADRVRAEaaa 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1668 -AER----ETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELI---RLKAEVDSGEQHRIVLEEDlFRLK 1739
Cdd:NF041483 689 aAERvgteAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasaRKRVEEAQAEAQRLVEEAD-RRAT 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1740 NEVNEAIQRRRGLEEELAKV--RAEMEI--LLKAKSKAEEDSRSTSEKSKQMLEVEASKLRELA-EEAARLRAVS-EEAK 1813
Cdd:NF041483 768 ELVSAAEQTAQQVRDSVAGLqeQAEEEIagLRSAAEHAAERTRTEAQEEADRVRSDAYAERERAsEDANRLRREAqEETE 847
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1814 RQRQLAEEDATRQRAEAERILKEkltAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKllEEQAAQHKQDIEEK 1893
Cdd:NF041483 848 AAKALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIR--SDAAAQADRLIGEA 922
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1894 IHQLKQSSENELERQKTIVDETLKhrrvieEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSkekAEQDAEKQRQ 1973
Cdd:NF041483 923 TSEAERLTAEARAEAERLRDEARA------EAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGS---AQQHAERIRT 993
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1974 LAlveearrkeaeEKVKKiiAAEQEAGRQRKVALEEVERL--KIKADEAKKQKDLAEK----------EAEKQIQLAQDA 2041
Cdd:NF041483 994 EA-----------ERVKA--EAAAEAERLRTEAREEADRTldEARKDANKRRSEAAEQadtliteaaaEADQLTAKAQEE 1060
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2042 A-RLKIDAEEKA---YYAAVQQKEQEMLQTRIQEQSIYDKLKEEAEK----AKRAA----EEAE--RAKIKAEHEAALSR 2107
Cdd:NF041483 1061 AlRTTTEAEAQAdtmVGAARKEAERIVAEATVEGNSLVEKARTDADEllvgARRDAtairERAEelRDRITGEIEELHER 1140
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2108 QQAEEAERLK---------------QKAEIEAQAK---GQAQEDAEKVR-----------KEAELeaaKRGQAEQAALKL 2158
Cdd:NF041483 1141 ARRESAEQMKsagercdalvkaaeeQLAEAEAKAKelvSDANSEASKVRiaavkkaegllKEAEQ---KKAELVREAEKI 1217
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 1072265250 2159 KQMADAE----MEKHKQFAEKTVRQKEQVEGELTKVKLQLE 2195
Cdd:NF041483 1218 KAEAEAEakrtVEEGKRELDVLVRRREDINAEISRVQDVLE 1258
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
44-152 |
1.90e-29 |
|
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: 115.08 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 44 VQKKTFTKWVNKHLikhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKLRQV 121
Cdd:cd21227 4 IQKNTFTNWVNEQL-----KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGI 78
|
90 100 110
....*....|....*....|....*....|.
gi 1072265250 122 KLVNIRNDDIADGNPKLTLGLIWTIILHFQI 152
Cdd:cd21227 79 KLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1347-1966 |
6.05e-29 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 129.11 E-value: 6.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1347 ERTAEKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQQKKTIQQELHQMKN 1426
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1427 NSETEIKAKVKLIEEAEYNRKKVEEEiriiRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVK--- 1503
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEA----KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekk 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1504 --DEAQKKREAE----DELHRKVQAEKDAAREKQKAlEDLEKFRLQAEEAERRMKQAELEKE----RQIKQAHDVAQQSA 1573
Cdd:PTZ00121 1392 kaDEAKKKAEEDkkkaDELKKAAAAKKKADEAKKKA-EEKKKADEAKKKAEEAKKADEAKKKaeeaKKAEEAKKKAEEAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1574 DAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKK--QQLEAETAKEEAEKELEKWRQKANEALRL--RLQAEE 1649
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEAKKADEAKKAeeKKKADE 1550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1650 IAHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEEtaSHKLSAEQ----ELIRLKAE-VDSG 1724
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE--EKKMKAEEakkaEEAKIKAEeLKKA 1628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1725 EQHRIVLEEDLFRLKNEVNEAIQRRRglEEELAKVRAEMEillkaKSKAEEDSRSTSEKSKQmlEVEASKlrelAEEAAR 1804
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAEE-----AKKAEEDKKKAEEAKKA--EEDEKK----AAEALK 1695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1805 LRAvsEEAKRQRQLAEEDATRQRaEAERILKEkltainEATRmRTEAEIALKEKEAENERLRRLAEDEAYQRKLleeqaA 1884
Cdd:PTZ00121 1696 KEA--EEAKKAEELKKKEAEEKK-KAEELKKA------EEEN-KIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI-----A 1760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1885 QHKQDIEEKIHQLKQSSENELERQktIVDETLKHRRVIEEEIRILKINFEKASVGKSD--------LELELQKLKNIADE 1956
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEE--LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEgnlvindsKEMEDSAIKEVADS 1838
|
650
....*....|
gi 1072265250 1957 TQKSKEKAEQ 1966
Cdd:PTZ00121 1839 KNMQLEEADA 1848
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
168-270 |
6.18e-29 |
|
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: 113.48 E-value: 6.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 168 EKLLL-WSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTN-LENLDQAFTVAERELGVTRLLDPE 245
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1072265250 246 DVDVPQPDEKSIITYVSSLYDAMPR 270
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
43-150 |
2.82e-28 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 111.80 E-value: 2.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 43 RVQKKTFTKWVNKHLikhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKLR 119
Cdd:cd21183 3 RIQANTFTRWCNEHL-----KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEAD 77
|
90 100 110
....*....|....*....|....*....|.
gi 1072265250 120 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 150
Cdd:cd21183 78 HIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
168-267 |
4.39e-28 |
|
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: 110.84 E-value: 4.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 168 EKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDPED- 246
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1072265250 247 VDVPQPDEKSIITYVSSLYDA 267
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1782-2618 |
5.06e-28 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 125.47 E-value: 5.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1782 EKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAE 1861
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1862 NERLRRLAEDEAYQRKLLEEQAA------QHKQDIEEKIHQLKQSSENELERQKTIVDETLKHRRVIEEEIRILKINFEK 1935
Cdd:pfam02463 225 YLLYLDYLKLNEERIDLLQELLRdeqeeiESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1936 ASVGKSDLELELQ----KLKNIADETQKSKEKAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVE 2011
Cdd:pfam02463 305 LERRKVDDEEKLKesekEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2012 RLK---IKADEAKKQKDLAEKEAEKQIQLAQDAA-RLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKR 2087
Cdd:pfam02463 385 RLSsaaKLKEEELELKSEEEKEAQLLLELARQLEdLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2088 AAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQaqedaekvrkeaeleaakrgqaEQAALKLKQMADAEME 2167
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKAR----------------------SGLKVLLALIKDGVGG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2168 KHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELFKVKIQ----MEELVKLK 2243
Cdd:pfam02463 523 RIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPlksiAVLEIDPI 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2244 LRIEQENKMLILKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEASR 2323
Cdd:pfam02463 603 LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQ 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2324 LKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEEtegfQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAK 2403
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE----AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2404 KFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQL 2483
Cdd:pfam02463 759 KEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2484 RQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLFDNEVGKAQKLKSEKE-RQLAQLEEEKRLLQTSMDDAMKKQLDAE 2562
Cdd:pfam02463 839 ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELEsKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1072265250 2563 DRIRQKQEELQQLDKKRQEQERLLEEENRKLRERLEQLEQEHRIALEKTREVIITK 2618
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGK 974
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1352-2253 |
2.02e-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: 123.54 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1352 KLKEQERKKLAEVEDQLEKQR---QLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQQ-KKTIQQELHQMKNN 1427
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIidlEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKlNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1428 SETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKdeaq 1507
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK---- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1508 kkreaedELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQaELEKERQIKQAHDVAQQSADAELQSKrmsfLEK 1587
Cdd:pfam02463 325 -------KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK-LQEKLEQLEEELLAKKKLESERLSSA----AKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1588 TTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKED 1667
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1668 AERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQ 1747
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1748 R---RRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDAT 1824
Cdd:pfam02463 553 VsatADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1825 RQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIhqLKQSSENE 1904
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIK--KKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1905 LERQKTIVDETLKHRRVIEEEIRIlKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDaEKQRQLALVEEARRKE 1984
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKI-NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLK-EKELAEEREKTEKLKV 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1985 AEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEM 2064
Cdd:pfam02463 789 EEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2065 LQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKI---KAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEA 2141
Cdd:pfam02463 869 LQELLLKEEELEEQKLKDELESKEEKEKEEKKEleeESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEK 948
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2142 ELEAAKRGQAEQAALKLKQMADAEMEKH-KQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLR 2220
Cdd:pfam02463 949 EKEENNKEEEEERNKRLLLAKEELGKVNlMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVS 1028
|
890 900 910
....*....|....*....|....*....|...
gi 1072265250 2221 QKKlveeELFKVKIQMEELVKLKLRIEQENKML 2253
Cdd:pfam02463 1029 INK----GWNKVFFYLELGGSAELRLEDPDDPF 1057
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
150-267 |
4.47e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 109.02 E-value: 4.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 150 FQISDIQVtgqsEDMTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAF 229
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1072265250 230 TVAERELGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 267
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1507-2373 |
7.77e-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: 121.62 E-value: 7.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1507 QKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAER---RMKQAELEKERQIKQAHDVAQQSADAELQSKRMS 1583
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1584 ---FLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKAnEALRLRLQAEEIAHKKTLAQEE 1660
Cdd:pfam02463 249 eqeEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL-ERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1661 AEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQEliRLKAEVDSGEQHRIVLEEDLFRLKN 1740
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK--LESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1741 EVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLREL-----AEEAARLRAVSEEAKRQ 1815
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDelelkKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1816 RQLAEEDATRQRAEAERILKEKLTAINEAtRMRTEAEIALKEKEAENERLRRLAEDEAYQrKLLEEQAAQHKQDIEEKIH 1895
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLA-LIKDGVGGRIISAHGRLGDLGVAVENYKVA-ISTAVIVEVSATADEVEER 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1896 QLKQSSENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLA 1975
Cdd:pfam02463 564 QKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1976 LVEEARRKEAEEKvkkiiaAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKayya 2055
Cdd:pfam02463 644 KESGLRKGVSLEE------GLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELK---- 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2056 AVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAE 2135
Cdd:pfam02463 714 KLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2136 KVRKEAELEAAKRGQAEQAALKLKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEEtdhqkailddelgrLKEEV 2215
Cdd:pfam02463 794 EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE--------------ELERL 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2216 TESLRQKKLVEEELFKVKIQMEELVKLKLRIEQENKMLILKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARL-RK 2294
Cdd:pfam02463 860 EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEpEE 939
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072265250 2295 IAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRR 2373
Cdd:pfam02463 940 LLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
152-267 |
1.09e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 107.86 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 152 ISDIQVtgqsEDMTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTV 231
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1072265250 232 AERELGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 267
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
152-267 |
6.26e-26 |
|
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: 105.58 E-value: 6.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 152 ISDIQVtgqsEDMTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTV 231
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1072265250 232 AERELGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 267
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
170-265 |
9.35e-26 |
|
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: 104.54 E-value: 9.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 170 LLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDPED-VD 248
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1072265250 249 VPQPDEKSIITYVSSLY 265
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2076-2603 |
1.62e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 116.96 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2076 DKLKEEAEKAKRAAEEAERAKIK------AEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAA-KR 2148
Cdd:COG1196 203 EPLERQAEKAERYRELKEELKELeaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELeLE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2149 GQAEQAALKLKQMADAEMEKHKQFAEKtvrQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEE 2228
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEE---RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2229 LFKVKIQMEELVKLKLRIEQEnkmlILKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAE 2308
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEE----LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2309 KILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQ----------------MQQQLAEETEGFQKTLEA--- 2369
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAlaelleelaeaaarllLLLEAEADYEGFLEGVKAall 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2370 ------------------ERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDI--SEKLHQTELSTKEKM-T 2428
Cdd:COG1196 516 laglrglagavavligveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpLDKIRARAALAAALArG 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2429 VVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQLRQETQTLQSTFLT-----EKQILIQ 2503
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTggsrrELLAALL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2504 KEKYIEEEKAKLEKLFDNEVGKAQKLKSEKERQLAQLEEEKRLLQTSMDDAMKKQLDAEDRIRQKQEELQQLDKKRQEQE 2583
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
570 580
....*....|....*....|
gi 1072265250 2584 RLLEEENRKLRERLEQLEQE 2603
Cdd:COG1196 756 LPEPPDLEELERELERLERE 775
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
38-152 |
4.37e-25 |
|
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: 103.30 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 38 EDERDRVQKKTFTKWVNKHLIKHwraEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFL 116
Cdd:cd21247 14 QEQRMTMQKKTFTKWMNNVFSKN---GAKIEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFL 90
|
90 100 110
....*....|....*....|....*....|....*..
gi 1072265250 117 KLR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 152
Cdd:cd21247 91 KTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
43-150 |
4.73e-25 |
|
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: 102.57 E-value: 4.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 43 RVQKKTFTKWVNKHLikhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKLR 119
Cdd:cd21228 3 KIQQNTFTRWCNEHL-----KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERE 77
|
90 100 110
....*....|....*....|....*....|.
gi 1072265250 120 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 150
Cdd:cd21228 78 SIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1876-2559 |
1.00e-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: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1876 RKLLEEQA--AQHKQDIEEKIHQLKQSSENeLERQKTIVDEtlkhrrvieeeirilkinfekasvgksdLELELQKLKNI 1953
Cdd:COG1196 158 RAIIEEAAgiSKYKERKEEAERKLEATEEN-LERLEDILGE----------------------------LERQLEPLERQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1954 ADETQKSKEKAEQDAEKQRQLALveearrkeaeekvkkiiAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEk 2033
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLL-----------------LKLRELEAELEELEAELEELEAELEELEAELAELEAELE- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2034 QIQLAQDAARLKIDAEEKAYYAAVQQKEQ-------------EMLQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAE 2100
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARleqdiarleerrrELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2101 HEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMADAEMEKHKQFAEKTVRQK 2180
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2181 EQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELFKVKIQMEELVKLKLRIEQENKML------I 2254
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegflegV 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2255 LKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQ 2334
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2335 KEMAMEQAkKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDI---SAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAED 2411
Cdd:COG1196 591 ALARGAIG-AAVDLVASDLREADARYYVLGDTLLGRTLVAARLeaaLRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2412 ISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQLRQETQTLQ 2491
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2492 STFLTEKQILI---QKEKYIEEEKAKLEKLfdnevGK-----AQKLKSEKER------QLAQLEEEKRLLQT---SMDDA 2554
Cdd:COG1196 750 EEALEELPEPPdleELERELERLEREIEAL-----GPvnllaIEEYEELEERydflseQREDLEEARETLEEaieEIDRE 824
|
....*
gi 1072265250 2555 MKKQL 2559
Cdd:COG1196 825 TRERF 829
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1604-2416 |
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 1072265250 1604 HLQEEAERLKK-QQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHK-KTLAQEEAEKQKEDAERETRKRTKAEES 1681
Cdd:TIGR02168 204 SLERQAEKAERyKELKAELRELELALLVLRLEELREELEELQEELKEAEEElEELTAELQELEEKLEELRLEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1682 ALRQKDLAE-----EELEKQRKLAEETASHklsAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEEL 1756
Cdd:TIGR02168 284 EELQKELYAlaneiSRLEQQKQILRERLAN---LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1757 AKVRAEMEILLKAKSKAEEDsrstsekskqmLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKE 1836
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQ-----------LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1837 KLTAINEATRMR-TEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLK--QSSENELERQKTIVD 1913
Cdd:TIGR02168 430 LEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDslERLQENLEGFSEGVK 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1914 ETLKHRRVIEEEIRIL--KINFEKasvgKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLALVEEARRKEAEEKVKK 1991
Cdd:TIGR02168 510 ALLKNQSGLSGILGVLseLISVDE----GYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1992 IIAAEQEAGRQRKVALEEVERLKIKADEAKKQ-----------KDLAEKeAEKQIQLAQDAARLKIDAE----EKAYYAA 2056
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvDDLDNA-LELAKKLRPGYRIVTLDGDlvrpGGVITGG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2057 VQQKEQEMLQTRiqeQSIyDKLKEEAEKAKRAAEEAERAKIKAEHEaalsRQQAEEAERLKQKAEIEAQAK-GQAQEDAE 2135
Cdd:TIGR02168 665 SAKTNSSILERR---REI-EELEEKIEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELSRQiSALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2136 KVRKEAELEAAKRGQAEQAALKLKQmadaemekhkqfaektvrQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEV 2215
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEA------------------EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2216 TESLRQKKLVEEELFKVKIqmeELVKLKLRIEQEnkmlilkgkdntQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKI 2295
Cdd:TIGR02168 799 KALREALDELRAELTLLNE---EAANLRERLESL------------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2296 AEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKtLEAERRRQL 2375
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQ 942
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 1072265250 2376 DISAEAERLKLQVVEmsKSQAKAEEDAKKFRKQAEDISEKL 2416
Cdd:TIGR02168 943 ERLSEEYSLTLEEAE--ALENKIEDDEEEARRRLKRLENKI 981
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
152-267 |
1.88e-24 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 101.30 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 152 ISDIQVtgqsEDMTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTV 231
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1072265250 232 AERELGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 267
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
43-153 |
2.94e-24 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 100.88 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 43 RVQKKTFTKWVNKHLikhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLKLR 119
Cdd:cd21310 15 KIQQNTFTRWCNEHL-----KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDRE 89
|
90 100 110
....*....|....*....|....*....|....
gi 1072265250 120 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 153
Cdd:cd21310 90 HIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
166-265 |
3.01e-24 |
|
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: 99.94 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 166 AKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDPE 245
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1072265250 246 D-VDVPQPDEKSIITYVSSLY 265
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
168-268 |
1.66e-23 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 97.92 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 168 EKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDPEDV 247
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1072265250 248 DVPQPDEKSIITYVSSLYDAM 268
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
165-269 |
2.03e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 97.55 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQRMSEGYqGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDP 244
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1072265250 245 EDVDVPQPDEKSIITYVSSLYDAMP 269
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
165-265 |
2.97e-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: 97.11 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAErELGVTRLLDP 244
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 1072265250 245 EDVDVPQ-PDEKSIITYVSSLY 265
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
792-858 |
5.57e-23 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 95.02 E-value: 5.57e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 792 QLKPRSpsNPAKGKQPVQAVCDYKQMEITVHKGDECLLVNNSQLSKWKVLNSAGNDATVPSVCFIVP 858
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1354-2115 |
7.14e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.61 E-value: 7.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1354 KEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEevtrrevvavdAEQQKKTIQQELHQMKNnsetEIK 1433
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIEELQKELYALAN----EIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1434 AKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAerqkklaQEEAERLRKQVKDEAQKKREAE 1513
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL-------KEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1514 DELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQSKRMSFLEKTTQLEM 1593
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1594 SLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEkwRQKANEALRLRLQ------AEEIAHKKTLA---------- 1657
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQA--RLDSLERLQENLEgfsegvKALLKNQSGLSgilgvlseli 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1658 --QEEAEKQKEDAERE------TRKRTKAEE--SALRQKDL-----AEEELEKQRKLAEETASHKLSAEQELIRLKAEVD 1722
Cdd:TIGR02168 530 svDEGYEAAIEAALGGrlqavvVENLNAAKKaiAFLKQNELgrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVK 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1723 SGEQHRIVLEEDLFRLK--NEVNEAIQRRRGLEEELAKVRAEMEILLKAKS---KAEEDSRSTSEKSKQMLEVEAsKLRE 1797
Cdd:TIGR02168 610 FDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVitgGSAKTNSSILERRREIEELEE-KIEE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1798 LAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRK 1877
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1878 LLEEqAAQHKQDIEEKIHQLKQS---SENELERQKTIVDETlkhrrviEEEIRILKINFEKASVGKSDLELELQKLKNIA 1954
Cdd:TIGR02168 769 RLEE-AEEELAEAEAEIEELEAQieqLKEELKALREALDEL-------RAELTLLNEEAANLRERLESLERRIAATERRL 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1955 DETQKSKEKAEQDAEKqrqlalveearrkeAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQ 2034
Cdd:TIGR02168 841 EDLEEQIEELSEDIES--------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2035 IQLAQDAARLKIDAEEKAyyAAVQQKEQEMlqtRIQEQSIYDKLkeeAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAE 2114
Cdd:TIGR02168 907 ESKRSELRRELEELREKL--AQLELRLEGL---EVRIDNLQERL---SEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
.
gi 1072265250 2115 R 2115
Cdd:TIGR02168 979 N 979
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
165-263 |
8.18e-23 |
|
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: 95.77 E-value: 8.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQRMSEGYqglRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVY-RQTNLENLDQAFTVAERELGVTRLLD 243
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1072265250 244 PEDVDVPQPDEKSIITYVSS 263
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1354-2368 |
9.12e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.22 E-value: 9.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1354 KEQERKKLAEVEDQLEK--------QRQLAEAHAQAKAvAEKeALELRMnmQEEVTRREVVAVDAEQQKKTIQQelhqmk 1425
Cdd:TIGR02168 174 RKETERKLERTRENLDRledilnelERQLKSLERQAEK-AER-YKELKA--ELRELELALLVLRLEELREELEE------ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1426 nnSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQvkdE 1505
Cdd:TIGR02168 244 --LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ---L 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1506 AQKKREAEDELHRKVQAEKDAAREKQKALEDLEKF-RLQAEEAERRMKQAELEKERQIKQAHdvaqqsadaelqskrmsf 1584
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELeSLEAELEELEAELEELESRLEELEEQ------------------ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1585 lekttqlemslkqehitvthlqeeaerlkkqqleaetakeeaekelekWRQKANEALRLRLQAEEIAHKktlaQEEAEKQ 1664
Cdd:TIGR02168 381 ------------------------------------------------LETLRSKVAQLELQIASLNNE----IERLEAR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1665 KEDAEREtRKRTKAEESALRQKDLAEEELEKQRKLAEetashklsaeqelirLKAEVDSGEQHRIVLEEDLFRLKNEVNE 1744
Cdd:TIGR02168 409 LERLEDR-RERLQQEIEELLKKLEEAELKELQAELEE---------------LEEELEELQEELERLEEALEELREELEE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1745 AIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSE--KSKQMLEVEASKLRELAEEAARLRAVSEEAKRQR--QLAE 1820
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRlqAVVV 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1821 EDATRQRAEAErILKEkltaiNEATRMRTEAEIALKEKEAENERLRRLAEDEAYQR--KLLEEQAAQHK----------- 1887
Cdd:TIGR02168 553 ENLNAAKKAIA-FLKQ-----NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRkalsyllggvl 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1888 --QDIEEKIHQLKQSSENElerqkTIV--DETLKHRRVIeeeirilkINFEKASVGKSDLELElqklKNIADETQKSKEK 1963
Cdd:TIGR02168 627 vvDDLDNALELAKKLRPGY-----RIVtlDGDLVRPGGV--------ITGGSAKTNSSILERR----REIEELEEKIEEL 689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1964 AEQDAEKQRQLAlveearrkeaeeKVKKIIAAEQEAGRQRKVALEEVERlkiKADEAKKQKDLAEKEAEkqiQLAQDAAR 2043
Cdd:TIGR02168 690 EEKIAELEKALA------------ELRKELEELEEELEQLRKELEELSR---QISALRKDLARLEAEVE---QLEERIAQ 751
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2044 LKIDAEEKAYYAAVQQKEQEMLQTRIQEQsiydklkeeaeKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIE 2123
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEA-----------EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2124 AQAKGQAQEDAEKVRKEAELEAAKRgQAEQAALKLKQMAdAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAI 2203
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEE-QIEELSEDIESLA-AEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2204 LDDELGRLKEEVTESLRQKKLVEEELFKVKIQMEelvKLKLRIeqenkmlilkgkDNTQQFLAEEAekmkqvaeeaarlS 2283
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLE---GLEVRI------------DNLQERLSEEY-------------S 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2284 VEAQEAARLRKIAEDDLNEQRALAEKILKEK-------MQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQqql 2356
Cdd:TIGR02168 951 LTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID--- 1027
|
1050
....*....|..
gi 1072265250 2357 AEETEGFQKTLE 2368
Cdd:TIGR02168 1028 REARERFKDTFD 1039
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
47-149 |
1.17e-22 |
|
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: 95.46 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 47 KTFTKWVNKHLIKhwraEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPREK---GRMRFHKLQNVQIALDFLKLRQVKL 123
Cdd:smart00033 1 KTLLRWVNSLLAE----YDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKV 76
|
90 100
....*....|....*....|....*.
gi 1072265250 124 VNIRNDDIADGnPKLTLGLIWTIILH 149
Cdd:smart00033 77 VLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
44-152 |
3.35e-22 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 94.28 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 44 VQKKTFTKWVNKHLIKhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLP-REKGRMRFHKLQNVQIALDFLKLRQ-V 121
Cdd:pfam00307 2 ELEKELLRWINSHLAE---YGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgV 78
|
90 100 110
....*....|....*....|....*....|.
gi 1072265250 122 KLVNIRNDDIADGNPKLTLGLIWTIILHFQI 152
Cdd:pfam00307 79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1744-2416 |
6.63e-22 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 105.29 E-value: 6.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1744 EAIQRRRGLEEELAKVRAEMEILlkakskaeedsRSTSEKSKQMLEveasklrELAEEAARLRAVSEEAKrqRQLAEE-- 1821
Cdd:NF041483 5 ERQESHRADDDHLSRFEAEMDRL-----------KTEREKAVQHAE-------DLGYQVEVLRAKLHEAR--RSLASRpa 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1822 -DATRQRAEAERILKeklTAINEATRMRTEAEIALKEKEAENER-LRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQ 1899
Cdd:NF041483 65 yDGADIGYQAEQLLR---NAQIQADQLRADAERELRDARAQTQRiLQEHAEHQARLQAELHTEAVQRRQQLDQELAERRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1900 SSENELErQKTIVDETLKhRRVIEEEIRILKINFEKASVGKSDLELELQKL-----KNIADETQKSKEKAEQ-------D 1967
Cdd:NF041483 142 TVESHVN-ENVAWAEQLR-ARTESQARRLLDESRAEAEQALAAARAEAERLaeearQRLGSEAESARAEAEAilrrarkD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1968 AEKQRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVAL---------EEVERLKIKADEAKKQKDLAEKEAEKQIQLA 2038
Cdd:NF041483 220 AERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELsraaeqrmqEAEEALREARAEAEKVVAEAKEAAAKQLASA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2039 QDA--ARLKIDAEEKAYYAAVQQKEQEMLQTRiQEQSIYDKlKEEAEKAKRAAEEAERAkIKAEHEAALSRQQAEEAERL 2116
Cdd:NF041483 300 ESAneQRTRTAKEEIARLVGEATKEAEALKAE-AEQALADA-RAEAEKLVAEAAEKART-VAAEDTAAQLAKAARTAEEV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2117 KQKAEIEAQAKGQ-AQEDAEKVRKEAELEAAK-RGQAEQAALKLKQMADAEMekhKQFAEKTVRQKEQVEgeltkvKLQL 2194
Cdd:NF041483 377 LTKASEDAKATTRaAAEEAERIRREAEAEADRlRGEAADQAEQLKGAAKDDT---KEYRAKTVELQEEAR------RLRG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2195 E-ETDHQKAILDDELGR---LKEEVTESLRQKKLVEEELFKVKIQMEELvKLKLRIEQENKMLILKGKDNTQQFLAEEAe 2270
Cdd:NF041483 448 EaEQLRAEAVAEGERIRgeaRREAVQQIEEAARTAEELLTKAKADADEL-RSTATAESERVRTEAIERATTLRRQAEET- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2271 kMKQVAEEAARLSVEAQE-AARLRKIAEDDLNEQRALAEK-ILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKklqED 2348
Cdd:NF041483 526 -LERTRAEAERLRAEAEEqAEEVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAEERLTAAEEALADAR---AE 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072265250 2349 KEQMQQQLAEETEGfQKTLEAERRRQLDISA--EAERLKLQVV-EMSKSQAKAEEDAKKFRKQAEDISEKL 2416
Cdd:NF041483 602 AERIRREAAEETER-LRTEAAERIRTLQAQAeqEAERLRTEAAaDASAARAEGENVAVRLRSEAAAEAERL 671
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1747-2578 |
1.27e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 104.37 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1747 QRRRGLEEELAKVRAEMEILlkakskaeEDSRSTSEKSKQMLEVEASKlrelAEEAARLRAVSEEAKRQRQLAE-EDATR 1825
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRL--------EDILNELERQLKSLERQAEK----AERYKELKAELRELELALLVLRlEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1826 QRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDeaYQRKLLEEQAAQHKQDIEEKIHQLK-QSSENE 1904
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE--LQKELYALANEISRLEQQKQILRERlANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1905 LERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLALVEEARRKE 1984
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1985 AEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEM 2064
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2065 LQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAE----IEAQAKGQAQ----EDAEK 2136
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeaaIEAALGGRLQavvvENLNA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2137 VRKEAE-LEAAKRGQAeqAALKLKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEetdhqkAILDDELGRLK--E 2213
Cdd:TIGR02168 558 AKKAIAfLKQNELGRV--TFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR------KALSYLLGGVLvvD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2214 EVTESLRQKKLVEEELFKVKIQmEELVKLKLRI-----EQENKMLilkgkdNTQQFLAEEAEKMKQVAEEAARLSVEAQE 2288
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRIVTLD-GDLVRPGGVItggsaKTNSSIL------ERRREIEELEEKIEELEEKIAELEKALAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2289 AARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEmamEQAKKLQEDKEQMQQQLAEETEGFQKTLE 2368
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA---QLSKELTELEAEIEELEERLEEAEEELAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2369 AERRRQlDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAEELR 2448
Cdd:TIGR02168 780 AEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2449 KAIADLENEKEKLKKEAELLQKKSEEMQkAQKEQLRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLfdneVGKAQK 2528
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLE-EALALLRSELEELSEELRELESKRSELRRELEELREKLAQL----ELRLEG 933
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2529 LKSEKERQLAQLEEEkrlLQTSMDDAMKKQLDAEDRIRQKQEELQQLDKK 2578
Cdd:TIGR02168 934 LEVRIDNLQERLSEE---YSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
164-270 |
1.98e-21 |
|
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: 91.96 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 164 MTAKEKLLLWSQRMSEGY-QGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVY--RQTNLENLDQAFTVAERELGVTR 240
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1072265250 241 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 270
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
169-266 |
2.12e-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: 89.33 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 169 KLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLD-PEDV 247
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1072265250 248 DVPQPDEKSIITYVSSLYD 266
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
43-153 |
6.34e-20 |
|
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: 88.60 E-value: 6.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 43 RVQKKTFTKWVNKHLikhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKLR 119
Cdd:cd21309 16 KIQQNTFTRWCNEHL-----KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRE 90
|
90 100 110
....*....|....*....|....*....|....
gi 1072265250 120 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 153
Cdd:cd21309 91 SIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1354-2145 |
9.17e-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: 98.22 E-value: 9.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1354 KEQERKKLAEVEDQLEKQRQLAEahaqakavaekealELRMNMQEEVTRREvvavDAEQQKKtIQQELHqmknnsETEIK 1433
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIID--------------EKRQQLERLRRERE----KAERYQA-LLKEKR------EYEGY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1434 AKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQ-KKLAQEEAERLRKQVKDEAQKKREA 1512
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1513 EDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEKErqikqahdvAQQSADAELQSKRMSFLEKTTQLE 1592
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD---------KLTEEYAELKEELEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1593 MSLKQEHITVTHLQEEAERLKKQ----QLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDA 1668
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREinelKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1669 ERETRKRTKAEESALRQK----DLAEEELEKQRKLAEETASHKLSAEQELIR------LKAEVDS-----------GEQH 1727
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKeeydRVEKELSKLQRELAEAEAQARASEERVRGGraveevLKASIQGvhgtvaqlgsvGERY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1728 RIVLEEDL-FRLKNEV-------NEAIQ--RRRGLEE----ELAKVRAEMEILLKAKSKAEEDS---------------- 1777
Cdd:TIGR02169 538 ATAIEVAAgNRLNNVVveddavaKEAIEllKRRKAGRatflPLNKMRDERRDLSILSEDGVIGFavdlvefdpkyepafk 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1778 ---RSTS-------------------------EKSKQM------LEVEASKLRELAEEAARLRAVSEEAKRQRqlaeEDA 1823
Cdd:TIGR02169 618 yvfGDTLvvedieaarrlmgkyrmvtlegelfEKSGAMtggsraPRGGILFSRSEPAELQRLRERLEGLKREL----SSL 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1824 TRQRAEAERILKEKLTAINEATRM----RTEAEIALKEKEAENERLRRLAED-EAYQRKLLEEQA-----AQHKQDIEEK 1893
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEELEEDlSSLEQEIENVKSelkelEARIEELEED 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1894 IHQLKQsSENELERQ--KTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKL-KNIADETQKSKEKAEQDAEK 1970
Cdd:TIGR02169 774 LHKLEE-ALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLeKEIQELQEQRIDLKEQIKSI 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1971 QRQLALVeEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAE-KQIQLAQDAARLKIDAE 2049
Cdd:TIGR02169 853 EKEIENL-NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEkKRKRLSELKAKLEALEE 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2050 EKAYYAAVQQKEQEMlqtrIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQ 2129
Cdd:TIGR02169 932 ELSEIEDPKGEDEEI----PEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
890
....*....|....*.
gi 1072265250 2130 AQEDAEKVRKEAELEA 2145
Cdd:TIGR02169 1008 RIEEYEKKKREVFMEA 1023
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1173-1764 |
1.03e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.09 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1173 LERYREKvqllLERWQAivLQIEVRQRELEQLGKQLRYYRESYEWLIRWITEAKKRQEKIQnvpitdsktVKEQLMEEKK 1252
Cdd:COG1196 205 LERQAEK----AERYRE--LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELE---------AELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1253 LLEESEKNRGKVDecqkyakqyIEAIKDFEVQLVTYKAQVEPVVSPLKKpKVHSASDNIIQEYVELRTKYSELTTLTSQy 1332
Cdd:COG1196 270 EELRLELEELELE---------LEEAQAEEYELLAELARLEQDIARLEE-RRRELEERLEELEEELAELEEELEELEEE- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1333 IKFITETLRRLEEEERTAEKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQ 1412
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1413 QKKTIQQELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQ 1492
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1493 EEAERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQA---EEAERRMKQAELEKERQIKQA---- 1565
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivvEDDEVAAAAIEYLKAAKAGRAtflp 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1566 HDVAQQSADAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRL 1645
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1646 QAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGE 1725
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
570 580 590
....*....|....*....|....*....|....*....
gi 1072265250 1726 QHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEME 1764
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
43-153 |
2.14e-19 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 87.06 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 43 RVQKKTFTKWVNKHLikhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKLR 119
Cdd:cd21308 19 KIQQNTFTRWCNEHL-----KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRE 93
|
90 100 110
....*....|....*....|....*....|....
gi 1072265250 120 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 153
Cdd:cd21308 94 SIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
161-266 |
4.69e-19 |
|
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: 85.38 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 161 SEDMTAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTR 240
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1072265250 241 LLDPEDV-DVPQPDEKSIITYVSSLYD 266
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
165-264 |
4.84e-19 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 85.22 E-value: 4.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAErELGVTRLLDP 244
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1072265250 245 ED-VDVPQPDEKSIITYVSSL 264
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
165-265 |
7.71e-19 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 84.70 E-value: 7.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDP 244
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1072265250 245 EDVDV--PQPDEKSIITYVSSLY 265
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
45-150 |
9.68e-19 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 84.17 E-value: 9.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 45 QKKTFTKWVNKHLIKHwraEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKLRQVK 122
Cdd:cd21212 1 EIEIYTDWANHYLEKG---GHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVD 77
|
90 100
....*....|....*....|....*...
gi 1072265250 123 LVNIRNDDIADGNPKLTLGLIWTIILHF 150
Cdd:cd21212 78 VQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1351-2361 |
1.33e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 94.47 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1351 EKLKEQERKKLAEVEDQL-EKQRQLAEAHAQAkAVAEKEALELRMNMQEEVTRREvvavDAEQQKKTIQQELHQMKNNSE 1429
Cdd:pfam01576 207 EKAKRKLEGESTDLQEQIaELQAQIAELRAQL-AKKEEELQAALARLEEETAQKN----NALKKIRELEAQISELQEDLE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1430 TEIKAKVKlieeAEYNRKKVEEEIRIIRIQLETSQkQKSGAEDELRALRARaeEAERQKKLAQEEAERLRKQVKDEAQKK 1509
Cdd:pfam01576 282 SERAARNK----AEKQRRDLGEELEALKTELEDTL-DTTAAQQELRSKREQ--EVTELKKALEEETRSHEAQLQEMRQKH 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1510 REAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQqsadaELQSkrmsflektt 1589
Cdd:pfam01576 355 TQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQ-----ELQA---------- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1590 qlemslkqehitvthlqeeaerlkkqqleaetakeeaekelekwrqKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAE 1669
Cdd:pfam01576 420 ----------------------------------------------RLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1670 RETRKRTKAEESALRQKDLAEEEL--EKQRKLAEETASHKLSAEQEliRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAiq 1747
Cdd:pfam01576 454 GKNIKLSKDVSSLESQLQDTQELLqeETRQKLNLSTRLRQLEDERN--SLQEQLEEEEEAKRNVERQLSTLQAQLSDM-- 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1748 rRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLReLAEEaarLRAVSEEAKRQRQLAEEDATRQR 1827
Cdd:pfam01576 530 -KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR-LQQE---LDDLLVDLDHQRQLVSNLEKKQK 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1828 aEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSEN--EL 1905
Cdd:pfam01576 605 -KFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNvhEL 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1906 ERQKTIVDETLKHRRVIEEEiriLKINFEKASVGKSDLELELQKLKNIADETQKSKEkaEQDAEKQRQLalveearrkea 1985
Cdd:pfam01576 684 ERSKRALEQQVEEMKTQLEE---LEDELQATEDAKLRLEVNMQALKAQFERDLQARD--EQGEEKRRQL----------- 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1986 eekVKKIIAAEQEagrqrkvaLEEVERLKIKADEAKKQKDLAEKEAEKQIqlaQDAARLKIDAEEKAYYAAVQQKE--QE 2063
Cdd:pfam01576 748 ---VKQVRELEAE--------LEDERKQRAQAVAAKKKLELDLKELEAQI---DAANKGREEAVKQLKKLQAQMKDlqRE 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2064 MLQTRIQEQSIYDKLKEEAEKAKraAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAEL 2143
Cdd:pfam01576 814 LEEARASRDEILAQSKESEKKLK--NLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARI 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2144 EAAKRGQAEQAalklkqmADAEMEKHKQfaEKTVRQKEQVEGELTKvklqlEETDHQKailddelgrlkeevTESLRQKK 2223
Cdd:pfam01576 892 AQLEEELEEEQ-------SNTELLNDRL--RKSTLQVEQLTTELAA-----ERSTSQK--------------SESARQQL 943
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2224 LVEEELFKVKIQ-MEELVKLKLrieqenKMLIlkgkdntqqfLAEEAeKMKQVAEEAARLSVEAQEAARLRKIAEDDLNE 2302
Cdd:pfam01576 944 ERQNKELKAKLQeMEGTVKSKF------KSSI----------AALEA-KIAQLEEQLEQESRERQAANKLVRRTEKKLKE 1006
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*....
gi 1072265250 2303 QRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETE 2361
Cdd:pfam01576 1007 VLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATE 1065
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1154-1932 |
1.56e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.44 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1154 KAREVSERMLKVHSERDVDLERYREKVQLL-LERWQAIVLQIEVRQREleqlgkQLRYYREsyewlIRWITEAKKRQEKI 1232
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAhFARRQAAIKAEEARKAD------ELKKAEE-----KKKADEAKKAEEKK 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1233 QnvpITDSKTVKEQLMEEKKLLEESEKNRGKVDECQKYAKqyiEAIKDFEVQlvtyKAQVEPVVSPLKKPKVHSASDNII 1312
Cdd:PTZ00121 1303 K---ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE---EAKKAAEAA----KAEAEAAADEAEAAEEKAEAAEKK 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1313 QEyvELRTKYSELTTlTSQYIKFITETLRRLEEEERTAEKLK--EQERKKLAEVEDQLEKQRQLAEAhaQAKAVAEKEAL 1390
Cdd:PTZ00121 1373 KE--EAKKKADAAKK-KAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKAD 1447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1391 ELRMNmQEEVTRREVVAVDAEQQKKTiqqelHQMKNNSETEIKAKvKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKsgA 1470
Cdd:PTZ00121 1448 EAKKK-AEEAKKAEEAKKKAEEAKKA-----DEAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKKADEAKK--A 1518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1471 EDELRALRAR-AEEAER--------QKKLAQE--EAERLRK--QVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDL 1537
Cdd:PTZ00121 1519 EEAKKADEAKkAEEAKKadeakkaeEKKKADElkKAEELKKaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1538 EKFrlqaeEAERRMKQAELEKERQIKQAhdvAQQSADAELQSKRMSFLEKTTQLEmslkqehitvthlQEEAERLKKQQL 1617
Cdd:PTZ00121 1599 KLY-----EEEKKMKAEEAKKAEEAKIK---AEELKKAEEEKKKVEQLKKKEAEE-------------KKKAEELKKAEE 1657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1618 EAETAKEEAEKELEKWRQKANEALRlrlqaeeiahkktlAQEEAEKQKEDAERETRKRTKAEEsaLRQKDlaEEELEKQR 1697
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKK--------------AEEDEKKAAEALKKEAEEAKKAEE--LKKKE--AEEKKKAE 1719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1698 KLAEETASHKLSAEQelIRLKAEVDSGEQHRIVLEEDlfrlknEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAE-ED 1776
Cdd:PTZ00121 1720 ELKKAEEENKIKAEE--AKKEAEEDKKKAEEAKKDEE------EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEdEK 1791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1777 SRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEakrqrqlAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALK 1856
Cdd:PTZ00121 1792 RRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKE-------MEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDG 1864
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 1857 EKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSEN-ELERQKTIVDETLKhRRVIEEEIRILKIN 1932
Cdd:PTZ00121 1865 NKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNnDIIDDKLDKDEYIK-RDAEETREEIIKIS 1940
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1534-2267 |
2.98e-18 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 93.11 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1534 LEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSAD-AELQSKRMSFLEKT-TQLEMSLKQEHITVTHL------ 1605
Cdd:TIGR00618 172 LFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCmPDTYHERKQVLEKElKHLREALQQTQQSHAYLtqkrea 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1606 QEEAERlKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIA-HKKTLAQEEAEKQKEDAERETRKRTKAEESALR 1684
Cdd:TIGR00618 252 QEEQLK-KQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1685 QKDLAEE-ELEKQRKLAEEtashkLSAEQELIRLKAEVDSG----EQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKV 1759
Cdd:TIGR00618 331 AAHVKQQsSIEEQRRLLQT-----LHSQEIHIRDAHEVATSireiSCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1760 RAEmeillkaksKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLt 1839
Cdd:TIGR00618 406 QRE---------QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQL- 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1840 aineatrmRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEE--QAAQHKQDIE---------EKIHQLKQSSENELERQ 1908
Cdd:TIGR00618 476 --------QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSciHPNPARQDIDnpgpltrrmQRGEQTYAQLETSEEDV 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1909 KTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKaEQDAEKQRQLALVEEARRKEAEEK 1988
Cdd:TIGR00618 548 YHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK-LSEAEDMLACEQHALLRKLQPEQD 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1989 VKKIIAAEQEAGRQRKVALEEVERLKIK-ADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQT 2067
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTALHALQLTlTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2068 RIQEQSI--YDKLKEEAEKAKRAAeeaeRAKIKAEHEAA---LSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAE 2142
Cdd:TIGR00618 707 RELETHIeeYDREFNEIENASSSL----GSDLAAREDALnqsLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSH 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2143 LEAAKRGQAEQAALKLKQMADAEmEKHKQFA-----EKTVRQkEQVEGELTKVKLQLEEtDHQKAIlddELGRLKEEVTE 2217
Cdd:TIGR00618 783 LAAEIQFFNRLREEDTHLLKTLE-AEIGQEIpsdedILNLQC-ETLVQEEEQFLSRLEE-KSATLG---EITHQLLKYEE 856
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2218 SLRQKKLVEEELFKVKIQMEELvklklriEQENKMLILKGKDNTQQFLAE 2267
Cdd:TIGR00618 857 CSKQLAQLTQEQAKIIQLSDKL-------NGINQIKIQFDGDALIKFLHE 899
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1571-2607 |
3.15e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 93.32 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1571 QSADAELQSKRmsflEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAekelekwrqkanEALRLRLQA--- 1647
Cdd:pfam01576 8 QAKEEELQKVK----ERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEA------------EEMRARLAArkq 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1648 --EEIAHKKTLAQEEAEKQKEDAEREtRKRTKAEESALRQKdLAEEELEKQR-KLAEETASHKL-SAEQELIRLKAEVDS 1723
Cdd:pfam01576 72 elEEILHELESRLEEEEERSQQLQNE-KKKMQQHIQDLEEQ-LDEEEAARQKlQLEKVTTEAKIkKLEEDILLLEDQNSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1724 GEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAeMEILLKAKSKAEEDSRSTSEKSKQMLEVEASklrELAEEAA 1803
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA-MISDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1804 RLRAVSEEAKRQRQLAEEDatrqraeaeriLKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRklleEQA 1883
Cdd:pfam01576 226 ELQAQIAELRAQLAKKEEE-----------LQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAAR----NKA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1884 AQHKQDIEEKIHQLKQSSENELErqKTIVDETLKHRR---------VIEEEIRILKINFEKASVGKSDLELELQKLKNIA 1954
Cdd:pfam01576 291 EKQRRDLGEELEALKTELEDTLD--TTAAQQELRSKReqevtelkkALEEETRSHEAQLQEMRQKHTQALEELTEQLEQA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1955 DETQKSKEKAEQDAEKQRQlalveearrkEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQK-DLAEKEAEK 2033
Cdd:pfam01576 369 KRNKANLEKAKQALESENA----------ELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRaELAEKLSKL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2034 QIQLAQDAARLKiDAEEKAYYAAvqqKEQEMLQTRIQEQSiydKLKEEAEKAKRAAEEAERAkikAEHEAALSRQQAEEA 2113
Cdd:pfam01576 439 QSELESVSSLLN-EAEGKNIKLS---KDVSSLESQLQDTQ---ELLQEETRQKLNLSTRLRQ---LEDERNSLQEQLEEE 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2114 ERLKQKAEIEAQAKGQAQEDaekVRKEAELEAAKRGQAEQAALKLKQMADA---EMEKHKQFAEKTVRQKEQVEGELTKV 2190
Cdd:pfam01576 509 EEAKRNVERQLSTLQAQLSD---MKKKLEEDAGTLEALEEGKKRLQRELEAltqQLEEKAAAYDKLEKTKNRLQQELDDL 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2191 KLQLeetDHQKAILDdelgrlkeevTESLRQKK----LVEEELFKVKIQMEELVKLKLRIEQENKMLILKGKDNTQQFLA 2266
Cdd:pfam01576 586 LVDL---DHQRQLVS----------NLEKKQKKfdqmLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAK 652
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2267 EEAEK-MKQVAEEAARL-------SVEAQEAARLRKIAEDDLNEQRALAEKiLKEKMQAVQEAsRLKAEAEM-------- 2330
Cdd:pfam01576 653 EELERtNKQLRAEMEDLvsskddvGKNVHELERSKRALEQQVEEMKTQLEE-LEDELQATEDA-KLRLEVNMqalkaqfe 730
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2331 --LQKQKEMAMEQAKKLQEDKEQMQQQLAEETEgfQKTLEAERRRQLDIsaEAERLKLQVVEMSKSQAKAEEDAKKFRKQ 2408
Cdd:pfam01576 731 rdLQARDEQGEEKRRQLVKQVRELEAELEDERK--QRAQAVAAKKKLEL--DLKELEAQIDAANKGREEAVKQLKKLQAQ 806
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2409 AEDISEKLHQTELSTKEkmtvvhtLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQLRQETQ 2488
Cdd:pfam01576 807 MKDLQRELEEARASRDE-------ILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSA 879
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2489 TLQSTFLTEKQIlIQKEKYIEEEKAKLEKLFDN-----------------EVGKAQKLKSEKERQLAQLEEEKRLLQtSM 2551
Cdd:pfam01576 880 LQDEKRRLEARI-AQLEEELEEEQSNTELLNDRlrkstlqveqlttelaaERSTSQKSESARQQLERQNKELKAKLQ-EM 957
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072265250 2552 DDAMKKQLDA-----EDRIRQKQEELQQLDKKRQEQERLLEEENRKLRERLEQLEQEHRIA 2607
Cdd:pfam01576 958 EGTVKSKFKSsiaalEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHA 1018
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1361-2381 |
3.96e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 92.93 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1361 LAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQQKK---TIQQELHQMKNNSETE------ 1431
Cdd:pfam01576 143 LEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGEstdlqe 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1432 -IKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAER---QKKLAQEEAERLRKQVKDEAQ 1507
Cdd:pfam01576 223 qIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEdleSERAARNKAEKQRRDLGEELE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1508 K-KREAEDELHR-KVQAEKDAAREKQkaLEDLEKfrlqAEEAERRMKQAELEkerQIKQAHDVAQQSADAEL-QSKRM-S 1583
Cdd:pfam01576 303 AlKTELEDTLDTtAAQQELRSKREQE--VTELKK----ALEEETRSHEAQLQ---EMRQKHTQALEELTEQLeQAKRNkA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1584 FLEKTTQlemSLKQEhitVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEK 1663
Cdd:pfam01576 374 NLEKAKQ---ALESE---NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSS 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1664 QKEDAERETRKRTKAEESALRQKDLAEEEL--EKQRKLAEETASHKLSAEQEliRLKAEVDSGEQHRIVLEEDLFRLKNE 1741
Cdd:pfam01576 448 LLNEAEGKNIKLSKDVSSLESQLQDTQELLqeETRQKLNLSTRLRQLEDERN--SLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1742 VNEAiqrRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLReLAEEaarLRAVSEEAKRQRQLAEE 1821
Cdd:pfam01576 526 LSDM---KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR-LQQE---LDDLLVDLDHQRQLVSN 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1822 DATRQRaEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSS 1901
Cdd:pfam01576 599 LEKKQK-KFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVG 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1902 EN--ELERQKTIVDETLKHRRVIEEEiriLKINFEKASVGKSDLELELQKLKNIADETQKSKEkaEQDAEKQRQLalvee 1979
Cdd:pfam01576 678 KNvhELERSKRALEQQVEEMKTQLEE---LEDELQATEDAKLRLEVNMQALKAQFERDLQARD--EQGEEKRRQL----- 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1980 arrkeaeekVKKIIAAEQEagrqrkvaLEEVERLKIKADEAKKQKDLAEKEAEKQIQlaqDAARLKIDAEEKAYYAAVQQ 2059
Cdd:pfam01576 748 ---------VKQVRELEAE--------LEDERKQRAQAVAAKKKLELDLKELEAQID---AANKGREEAVKQLKKLQAQM 807
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2060 KE--QEMLQTRIQEQSIYDKLKEEAEKAKraAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKV 2137
Cdd:pfam01576 808 KDlqRELEEARASRDEILAQSKESEKKLK--NLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKR 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2138 RKEAELEAAKRGQAEQAAlklkqmaDAEMEKHKQfaEKTVRQKEQVEGELTKvklqlEETDHQKailddelgrlkeevTE 2217
Cdd:pfam01576 886 RLEARIAQLEEELEEEQS-------NTELLNDRL--RKSTLQVEQLTTELAA-----ERSTSQK--------------SE 937
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2218 SLRQKKLVEEELFKVKIQ-MEELVKLKLrieqenKMLILkgkdntqqflAEEAeKMKQVAEEAARLSVEAQEAARLRKia 2296
Cdd:pfam01576 938 SARQQLERQNKELKAKLQeMEGTVKSKF------KSSIA----------ALEA-KIAQLEEQLEQESRERQAANKLVR-- 998
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2297 eddlneqraLAEKILKEKMQAVQEASRlkaeaemlqkQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERR--RQ 2374
Cdd:pfam01576 999 ---------RTEKKLKEVLLQVEDERR----------HADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKlqRE 1059
|
....*..
gi 1072265250 2375 LDISAEA 2381
Cdd:pfam01576 1060 LDDATES 1066
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1352-2135 |
5.06e-17 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 89.26 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1352 KLKEQERKKLAEVEDQLEKQRQLAeahaqakAVAEKEALELRMNMQEEVTRREVVAVDAEQQkktiQQELHQMKNNSETE 1431
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLA-------LMEFAKKKSLHGKAELLTLRSQLLTLCTPCM----PDTYHERKQVLEKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1432 ikakVKLIEEAEYNRKKVEEEIRiiriQLETSQKQKSGAEDELRALRAR-----AEEAERQKklAQEEAERLRKQVKDEA 1506
Cdd:TIGR00618 228 ----LKHLREALQQTQQSHAYLT----QKREAQEEQLKKQQLLKQLRARieelrAQEAVLEE--TQERINRARKAAPLAA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1507 QKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEkerQIKQAHDVAQQSADAELQskRMSFLE 1586
Cdd:TIGR00618 298 HIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ---TLHSQEIHIRDAHEVATS--IREISC 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1587 KTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEkwRQKANEALRLRLQAEEIAHKKTLAQEEA----- 1661
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTS--AFRDLQGQLAHAKKQQELQQRYAELCAAaitct 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1662 ---EKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEetasHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRL 1738
Cdd:TIGR00618 451 aqcEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVL----ARLLELQEEPCPLCGSCIHPNPARQDIDNPGPL 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1739 KNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDsrstSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQl 1818
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQ----MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE- 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1819 AEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRklLEEQAAQHKQDIEEK--IHQ 1896
Cdd:TIGR00618 602 KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQER--VREHALSIRVLPKELlaSRQ 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1897 LKQSSENELERQKTIVDETLKHRRvieeeiriLKINFEKASVGKSDLELELQKLkniADETQKSKEKAEQDAEKQRQlal 1976
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKEMLAQCQ--------TLLRELETHIEEYDREFNEIEN---ASSSLGSDLAAREDALNQSL--- 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1977 veearrkeaeekvkkiiaaeQEAGRQRKVALEEVErlkiKADEAKKQKDLAEkeaekqIQLAQDAARLKIDAEEKAYYAA 2056
Cdd:TIGR00618 746 --------------------KELMHQARTVLKART----EAHFNNNEEVTAA------LQTGAELSHLAAEIQFFNRLRE 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2057 VQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEEAE---RAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQED 2133
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQflsRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
..
gi 1072265250 2134 AE 2135
Cdd:TIGR00618 876 DK 877
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1684-2615 |
5.18e-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: 89.36 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1684 RQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEdlfRLKNEVNEAIQRRRGLEEELAKVRAEM 1763
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE---KREYEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1764 EillkakSKAEEDSRSTSEKSKQMLEVEAsKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINE 1843
Cdd:TIGR02169 247 A------SLEEELEKLTEEISELEKRLEE-IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1844 ATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLkqssENELERQKTIVDETLKHRRVIE 1923
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL----EEVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1924 ---EEIRILKINFEKASVGKSDLELELQKLKN-IADETQKSKEKAEQDAEKQrqlalveearrkeaeekvKKIIAAEQEA 1999
Cdd:TIGR02169 396 klkREINELKRELDRLQEELQRLSEELADLNAaIAGIEAKINELEEEKEDKA------------------LEIKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2000 GR-QRKVALEEVERLKIKADEAKKQKDLAEKEAEkqiqLAQDAARLKIDAEEKAYYAAVQqkeqEMLQTRIQeqSIYDKL 2078
Cdd:TIGR02169 458 EQlAADLSKYEQELYDLKEEYDRVEKELSKLQRE----LAEAEAQARASEERVRGGRAVE----EVLKASIQ--GVHGTV 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2079 keeaekakraaeeAERAKIKAEHEAAlsrqqaeeaerlkqkaeIEAQAKGQAQE---DAEKVRKEAeLEAAKRGQAEQAA 2155
Cdd:TIGR02169 528 -------------AQLGSVGERYATA-----------------IEVAAGNRLNNvvvEDDAVAKEA-IELLKRRKAGRAT 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2156 -LKLKQMADAEMEKHK-------QFAEKTVRQKEQVEgelTKVKLQLEETdhqkAILDD-ELGRlkeevtESLRQKKLV- 2225
Cdd:TIGR02169 577 fLPLNKMRDERRDLSIlsedgviGFAVDLVEFDPKYE---PAFKYVFGDT----LVVEDiEAAR------RLMGKYRMVt 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2226 -EEELFK---------VKIQMEELVKLKLRIEQENKMLILKGKDNTQQFLAEEAEKMKQVAEEA-ARLSVEAQEAARLRK 2294
Cdd:TIGR02169 644 lEGELFEksgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELsQELSDASRKIGEIEK 723
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2295 IAEDDLNEQRALAEKI--LKEKMQAVQEA-SRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEEtegFQKTLEAER 2371
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLeeLEEDLSSLEQEiENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS---RIPEIQAEL 800
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2372 RrqlDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAEELRKAI 2451
Cdd:TIGR02169 801 S---KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2452 ADLENEKEKLKKEAELLQKKSEEMQKAQKEQ--LRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLFDNE--VGKAQ 2527
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELeaQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsLEDVQ 957
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2528 KLKSEKERQLAQLEEEKRLLQTSMDDAMKKQLDAEDrirqKQEELQqldkkrqeqerlleEENRKLRERLEQLEQEHRIA 2607
Cdd:TIGR02169 958 AELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE----KRAKLE--------------EERKAILERIEEYEKKKREV 1019
|
....*...
gi 1072265250 2608 LEKTREVI 2615
Cdd:TIGR02169 1020 FMEAFEAI 1027
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1940-2578 |
6.04e-17 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 88.87 E-value: 6.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1940 KSDLELELQKLKNIADETQKSKEKAEQDAEKQRQlalveearRKEAEEKVKKIIAAEQEAGRQRKV---ALEEVERLKIK 2016
Cdd:TIGR00618 221 KQVLEKELKHLREALQQTQQSHAYLTQKREAQEE--------QLKKQQLLKQLRARIEELRAQEAVleeTQERINRARKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2017 ADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIY---DKLKEEAEKAKRAAEEAE 2093
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHsqeIHIRDAHEVATSIREISC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2094 RAKIKAEH--------EAALSRQQAEEAERLKQKAE---IEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMA 2162
Cdd:TIGR00618 373 QQHTLTQHihtlqqqkTTLTQKLQSLCKELDILQREqatIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2163 DAEMEK-HKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQkklVEEELFKVKIqMEELVK 2241
Cdd:TIGR00618 453 CEKLEKiHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH---PNPARQDIDN-PGPLTR 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2242 LKLRIEQENKMLILKGKDNTQQfLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEkMQAVQEA 2321
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEEDVYHQ-LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL-TEKLSEA 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2322 SRLKAEA---EMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQ-LDISAEAERLKLQVVEMSKSQAK 2397
Cdd:TIGR00618 607 EDMLACEqhaLLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhALSIRVLPKELLASRQLALQKMQ 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2398 AE-EDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQR--------------QHSDKEAEELRkaiaDLENEKEKLK 2462
Cdd:TIGR00618 687 SEkEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASsslgsdlaaredalNQSLKELMHQA----RTVLKARTEA 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2463 KEAELLQKKSEEMQKAQKEQLRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLFDNEVGKAQKlksEKERQLAQLEE 2542
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ---EEEQFLSRLEE 839
|
650 660 670
....*....|....*....|....*....|....*.
gi 1072265250 2543 EKRLLQTsmddaMKKQLdaedriRQKQEELQQLDKK 2578
Cdd:TIGR00618 840 KSATLGE-----ITHQL------LKYEECSKQLAQL 864
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
169-266 |
6.85e-17 |
|
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: 79.15 E-value: 6.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 169 KLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLD-PEDV 247
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1072265250 248 DVPQPDEKSIITYVSSLYD 266
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1437-2369 |
7.32e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.97 E-value: 7.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1437 KLIEE----AEYNRK--KVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEeaerlrkqvkdeaqkKR 1510
Cdd:TIGR02169 157 KIIDEiagvAEFDRKkeKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE---------------KR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1511 EAEDELHrkvqaekdaAREKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQSKRMSFLE---- 1586
Cdd:TIGR02169 222 EYEGYEL---------LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrv 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1587 KTTQLEMSLKQEHItvthlqEEAERLKKQQLeaetakeeaekelekwrQKANEALRlrlQAEEIAHKKtlaQEEAEKQKE 1666
Cdd:TIGR02169 293 KEKIGELEAEIASL------ERSIAEKEREL-----------------EDAEERLA---KLEAEIDKL---LAEIEELER 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1667 DAERETRKRTKAEEsalRQKDLAEEELEKQRKLAEETASHK------LSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKN 1740
Cdd:TIGR02169 344 EIEEERKRRDKLTE---EYAELKEELEDLRAELEEVDKEFAetrdelKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1741 EVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTseksKQMLEVEASKLRELAEEAARLRavSEEAKRQRQLAE 1820
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL----AADLSKYEQELYDLKEEYDRVE--KELSKLQRELAE 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1821 EDATRQRAE--------AERILKEKL------------------TAINEATRMRTEAEIA------------LKEKEAEN 1862
Cdd:TIGR02169 495 AEAQARASEervrggraVEEVLKASIqgvhgtvaqlgsvgeryaTAIEVAAGNRLNNVVVeddavakeaielLKRRKAGR 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1863 ER---LRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENELerQKTIVDETLKHRRVIEEEIRILKIN---FEK- 1935
Cdd:TIGR02169 575 ATflpLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF--GDTLVVEDIEAARRLMGKYRMVTLEgelFEKs 652
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1936 -ASVGKSDLELELQklKNIADETQKSKEKAEQDAEKQRQLAlveearrkeaeekvkkIIAAEQEAGRQRkvaleeVERLK 2014
Cdd:TIGR02169 653 gAMTGGSRAPRGGI--LFSRSEPAELQRLRERLEGLKRELS----------------SLQSELRRIENR------LDELS 708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2015 IKADEAKKQKDLAEKEAEkqiQLAQDAARLKIDAEEKAYYaaVQQKEQEMLQTRiQEQSIYDKLKEEAEKAKRAAEEAEr 2094
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIE---QLEQEEEKLKERLEELEED--LSSLEQEIENVK-SELKELEARIEELEEDLHKLEEAL- 781
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2095 akikAEHEAALSRQQAEEAERLKQKAEIEAQakgqaqeDAEKVRKEAELEAAKRGQAEQAALKLKQMADAEMEKHKqfAE 2174
Cdd:TIGR02169 782 ----NDLEARLSHSRIPEIQAELSKLEEEVS-------RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK--EQ 848
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2175 KTVRQKEQVEGELTKVKLQLEETDHQKAI--LDDELGRLKEEVTESLRQKKLVEEELFKVKIQMEelvKLKLRIEQenkm 2252
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEELEAALrdLESRLGDLKKERDELEAQLRELERKIEELEAQIE---KKRKRLSE---- 921
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2253 lilkgkdnTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALaEKILKEKMQAVQEASRLKAEAEMLQ 2332
Cdd:TIGR02169 922 --------LKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELK 992
|
970 980 990
....*....|....*....|....*....|....*..
gi 1072265250 2333 KQKEMAMEQAKKLQEDKEQMQQQlaeETEGFQKTLEA 2369
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEEYEKK---KREVFMEAFEA 1026
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1224-2104 |
1.10e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.10 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1224 EAKKRQEKIQNvpitDSKTVKEQLMEEKKLLEESEKNRGKVDECQKYAKQYIEAIKDFEVQLVTYKAQVEpvvspLKKPK 1303
Cdd:pfam02463 205 QAKKALEYYQL----KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQV-----LKENK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1304 VHSASDNIIQEyvELRTKYSELTTLTSQYIKFITETLRRLEEEERTAEKLKEQERKKLAEVEDQLEKQRQLAEaHAQAKA 1383
Cdd:pfam02463 276 EEEKEKKLQEE--ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE-LEIKRE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1384 VAEKEALELRMNMQEEVTRREVVAV------DAEQQKKTIQQELHQMKNNSETEIKAKVKLIEEAEYNRK--------KV 1449
Cdd:pfam02463 353 AEEEEEEELEKLQEKLEQLEEELLAkkklesERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKeekkeeleIL 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1450 EEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEeaerlrkqvKDEAQKKREAEDELHRKVQAEKDAARE 1529
Cdd:pfam02463 433 EEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE---------TQLVKLQEQLELLLSRQKLEERSQKES 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1530 KQKALEDLeKFRLQAEEAERRMKQAELEKERQIKQAhdvaqqsadaelqskrmsflekttqlemsLKQEHITVTHLQEEA 1609
Cdd:pfam02463 504 KARSGLKV-LLALIKDGVGGRIISAHGRLGDLGVAV-----------------------------ENYKVAISTAVIVEV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1610 ERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTlAQEEAEKQKEDAERETRKRTKAEESALRQKDLA 1689
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEI-DPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1690 EEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQhrivleedLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKA 1769
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLS--------ELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1770 KSKAEEDSRStseKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINEATRMRT 1849
Cdd:pfam02463 705 EQREKEELKK---LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1850 EAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKTIVDETLKhRRVIEEEIRIL 1929
Cdd:pfam02463 782 KTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLE-KLAEEELERLE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1930 KINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQdaEKQRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEE 2009
Cdd:pfam02463 861 EEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE--EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2010 VERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEmlqtriqEQSIYDKLKEEAEKAKRAA 2089
Cdd:pfam02463 939 ELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNK-------DELEKERLEEEKKKLIRAI 1011
|
890
....*....|....*
gi 1072265250 2090 EEAERAKIKAEHEAA 2104
Cdd:pfam02463 1012 IEETCQRLKEFLELF 1026
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
165-264 |
1.15e-16 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 78.36 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAErELGVTRLLDP 244
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFA-SLGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1072265250 245 ED-VDVPQPDEKSIITYVSSL 264
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
46-148 |
1.19e-16 |
|
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: 78.15 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 46 KKTFTKWVNKHLIKhwraEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLK-LRQVK 122
Cdd:cd00014 1 EEELLKWINEVLGE----ELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKkLGLPE 76
|
90 100
....*....|....*....|....*..
gi 1072265250 123 LVNIRNDDI-ADGNPKLTLGLIWTIIL 148
Cdd:cd00014 77 LDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
167-278 |
3.00e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 77.34 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 167 KEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDPED 246
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 1072265250 247 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 278
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1722-2543 |
3.44e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 86.56 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1722 DSGEQHRIVLEEDLFRLK------NEVNEAIQRRRGLEEElakvRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEasKL 1795
Cdd:TIGR00618 102 KTEQPEQLYLEQKKGRGRilaakkSETEEVIHDLLKLDYK----TFTRVVLLPQGEFAQFLKAKSKEKKELLMNLF--PL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1796 RELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRlaEDEAYQ 1875
Cdd:TIGR00618 176 DQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQ--KREAQE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1876 RKLLEEQAAQHKQDIEEKIhqlkQSSENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKsdlelELQKLKN-IA 1954
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEEL----RAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHT-----ELQSKMRsRA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1955 DETQKSKEKAEQDAEKQRQLALVEEARRKEAEEKvkkiIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQ 2034
Cdd:TIGR00618 325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR----DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2035 IQLAQDAARLKIDAEEKAYYAAVQQKEQemLQTRIQEQSIYDKLKEEAekakrAAEEAERAKIKAEHEAALSRQQAEEAE 2114
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAH--AKKQQELQQRYAELCAAA-----ITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2115 RLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMADAEMekhkqfaekTVRQKEQVEGELTKVKLQL 2194
Cdd:TIGR00618 474 QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGP---------LTRRMQRGEQTYAQLETSE 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2195 EETDHQKAILDDELGRLKEEVTESLRQKKLVEEELFKVKIQMEELVKLKLRIeqenkmlilkgkdntQQFLAEEAEKMKQ 2274
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL---------------QDLTEKLSEAEDM 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2275 VAEEAARLSVEAQ-EAARLRKIAEDDLNEQR---------ALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKK 2344
Cdd:TIGR00618 610 LACEQHALLRKLQpEQDLQDVRLHLQQCSQElalkltalhALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEK 689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2345 LQ--EDKEQMQQQLAEETEGFQKTLEAERRRQ---LDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQT 2419
Cdd:TIGR00618 690 EQltYWKEMLAQCQTLLRELETHIEEYDREFNeieNASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEE 769
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2420 ELSTKEKMTvvhtleiQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQLRQETQTLqstflteKQ 2499
Cdd:TIGR00618 770 VTAALQTGA-------ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQF-------LS 835
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1072265250 2500 ILIQKEKYIEEEKAKLEKLFDNEVGKAQKLKseKERQLAQLEEE 2543
Cdd:TIGR00618 836 RLEEKSATLGEITHQLLKYEECSKQLAQLTQ--EQAKIIQLSDK 877
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
167-266 |
6.47e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 76.54 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 167 KEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDPED 246
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1072265250 247 VDV--PQPDEKSIITYVSSLYD 266
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1575-2388 |
8.88e-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: 85.12 E-value: 8.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1575 AELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQqleaetakeeaekelekwRQKANEALRLRLQAEEIAHKK 1654
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE------------------REKAERYQALLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1655 TLAQ-EEAEKQKE--DAERETRKRTKAEESALRQkDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVL 1731
Cdd:TIGR02169 228 LLKEkEALERQKEaiERQLASLEEELEKLTEEIS-ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1732 EEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEIL---------LKAKSKAE-EDSRSTSEKSKQMLEVEASKLRELAEE 1801
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELereieeerkRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1802 AARLRAVSEEAKRQRQLAEEDATRQRAEAERI------LKEKLTAINEA-TRMRTEAEIALKEKEAENERLRRLAED-EA 1873
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLseeladLNAAIAGIEAKiNELEEEKEDKALEIKKQEWKLEQLAADlSK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1874 YQRKLLEEQAAQhkQDIEEKIHQLKQSSEnELERQKTIVDETLKHRRVIEEEI--------------------------- 1926
Cdd:TIGR02169 467 YEQELYDLKEEY--DRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVLkasiqgvhgtvaqlgsvgeryataiev 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1927 ----RILKINFEKASVGKSDLE------------LELQKLKNIADETQKSKEKAEQDA-------EKQRQLALVEEARRK 1983
Cdd:TIGR02169 544 aagnRLNNVVVEDDAVAKEAIEllkrrkagratfLPLNKMRDERRDLSILSEDGVIGFavdlvefDPKYEPAFKYVFGDT 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1984 EAeekVKKIIAAEQEAGRQRKVALEE--VERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARL-KIDAEEKAYYAAVQQK 2060
Cdd:TIGR02169 624 LV---VEDIEAARRLMGKYRMVTLEGelFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLeGLKRELSSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2061 EQEMLQTRiqeQSIYDKLKEEAEKAKRAAE-EAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAK--GQAQEDAEKV 2137
Cdd:TIGR02169 701 ENRLDELS---QELSDASRKIGEIEKEIEQlEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAriEELEEDLHKL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2138 RKE-AELEAAKRGQAEQaalklkqmadaEMEKHKQFAEKTVRqkeQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVT 2216
Cdd:TIGR02169 778 EEAlNDLEARLSHSRIP-----------EIQAELSKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2217 ESLRQKKLVEEELFKVKIQMEELVKLKLRIEQENKMLILKGKDntqqfLAEEAEKMKQVAEEAARLSVEAQEAARLRKIA 2296
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD-----LKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2297 EDDLNEQRALAEKILKE---KMQAVQEASRLKAEAEMLQKQKE------MAMEQAKKLQEDKEQMQQQLAEETEGFQKTL 2367
Cdd:TIGR02169 919 LSELKAKLEALEEELSEiedPKGEDEEIPEEELSLEDVQAELQrveeeiRALEPVNMLAIQEYEEVLKRLDELKEKRAKL 998
|
890 900
....*....|....*....|.
gi 1072265250 2368 EAERRRQLDISAEAERLKLQV 2388
Cdd:TIGR02169 999 EEERKAILERIEEYEKKKREV 1019
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
168-264 |
1.21e-15 |
|
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: 75.43 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 168 EKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTN----LENLDQAFTVAERELGVTRLLD 243
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1072265250 244 PEDVDVPQPDEKSIITYVSSL 264
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1408-2304 |
1.34e-15 |
|
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: 84.71 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1408 VDAEQQKKTIQQELHQMKNNSETEIKakvkLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRaraeeaERQ 1487
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELK----YLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLK------NRL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1488 KKLAQEEAERLRKQVKDEAQKKREAEDElhrKVQAEKDAAREK-----QKALEDLEKFR-LQAEEAERRMKQAELEKERQ 1561
Cdd:TIGR00606 255 KEIEHNLSKIMKLDNEIKALKSRKKQME---KDNSELELKMEKvfqgtDEQLNDLYHNHqRTVREKERELVDCQRELEKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1562 IKQAHDVAQQSADAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEAL 1641
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1642 RLrlqAEEIAHKKTLAQEEAEKQKEdaERETRKRTKAEESALRQKDLAE-EELEKQRKLAEETASHKLSAEQELIRLKAE 1720
Cdd:TIGR00606 412 QL---CADLQSKERLKQEQADEIRD--EKKGLGRTIELKKEILEKKQEElKFVIKELQQLEGSSDRILELDQELRKAERE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1721 VDSGEQHRIV--LEEDLFRLKNEVNEAIQRRRGLEEELAKV------RAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEA 1792
Cdd:TIGR00606 487 LSKAEKNSLTetLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1793 SKLRELAEEAARLRAVSEEAKRQRQ-LAEEDATRQRAEAERilkeklTAINEATRMRTEAEIALKEK----------EAE 1861
Cdd:TIGR00606 567 GYFPNKKQLEDWLHSKSKEINQTRDrLAKLNKELASLEQNK------NHINNELESKEEQLSSYEDKlfdvcgsqdeESD 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1862 NERLRRLAEDEAYQRKLLEEQAAQHKQDIEE--------------------KIHQLKQSSENELERQKTIVDETLKHRRV 1921
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATAVYSQFITQltdenqsccpvcqrvfqteaELQEFISDLQSKLRLAPDKLKSTESELKK 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1922 IEEEIRILKInfeKASVGKSDLELELQKLKNIADETQK-SKEKAEQDAEKQRQLALVEEarrkeaeekvkkiIAAEQEAG 2000
Cdd:TIGR00606 721 KEKRRDEMLG---LAPGRQSIIDLKEKEIPELRNKLQKvNRDIQRLKNDIEEQETLLGT-------------IMPEEESA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2001 RQRKVALEEVERLKIKADEAKKQkdLAEKEAEKQ-IQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQS-----I 2074
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKDVERK--IAQQAAKLQgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQeqiqhL 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2075 YDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAE----IEAQAKGQAQEDAEKVRKEAELEAAKRGQ 2150
Cdd:TIGR00606 863 KSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEqdspLETFLEKDQQEKEELISSKETSNKKAQDK 942
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2151 AEQAALKLKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELF 2230
Cdd:TIGR00606 943 VNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLT 1022
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 2231 KVKI--QMEELVK-LKLRIEQENKMLILKGKDNTQQFlaeeAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQR 2304
Cdd:TIGR00606 1023 LRKRenELKEVEEeLKQHLKEMGQMQVLQMKQEHQKL----EENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1658-2602 |
2.23e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 83.69 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1658 QEEAEKQKED-----AERETRKRTKAEESALRQKDLAEEELEKQRKLAEETashKLSAEQELIRLKAEVDSGEqhrivLE 1732
Cdd:pfam01576 3 QEEEMQAKEEelqkvKERQQKAESELKELEKKHQQLCEEKNALQEQLQAET---ELCAEAEEMRARLAARKQE-----LE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1733 EDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEiLLKAKSKAEEDSRSTSEKSKQMLEveaSKLRELAEEAARLRAVSEEA 1812
Cdd:pfam01576 75 EILHELESRLEEEEERSQQLQNEKKKMQQHIQ-DLEEQLDEEEAARQKLQLEKVTTE---AKIKKLEEDILLLEDQNSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1813 KRQRQLAEE---DATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEA---ENERLRRLAEDEAYQrklLEEQAAQH 1886
Cdd:pfam01576 151 SKERKLLEErisEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKgrqELEKAKRKLEGESTD---LQEQIAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1887 KQDIEEKIHQLKQSsenelerqktivdetlkhrrviEEEIRILKINFEKASVGKSDLELELQKLKNIADETQkskekaeQ 1966
Cdd:pfam01576 228 QAQIAELRAQLAKK----------------------EEELQAALARLEEETAQKNNALKKIRELEAQISELQ-------E 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1967 DAEKQRqlalveearrkeaeekvkkiiAAEQEAGRQRKVALEEVERLKIkadEAKKQKDLAEKEAEKQIQLAQDAARLKI 2046
Cdd:pfam01576 279 DLESER---------------------AARNKAEKQRRDLGEELEALKT---ELEDTLDTTAAQQELRSKREQEVTELKK 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2047 DAEEKAyyaavQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEHEAA-------LSRQQAEEAERLKQK 2119
Cdd:pfam01576 335 ALEEET-----RSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAelqaelrTLQQAKQDSEHKRKK 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2120 AEIEAQ--------AKGQAQEDAEKVRK-EAELEAAKR--GQAEQAALKL-KQMADAEMEKH---KQFAEKTvRQK---- 2180
Cdd:pfam01576 410 LEGQLQelqarlseSERQRAELAEKLSKlQSELESVSSllNEAEGKNIKLsKDVSSLESQLQdtqELLQEET-RQKlnls 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2181 ---EQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQ--------------KKLVEEELFKVKIQMEE----- 2238
Cdd:pfam01576 489 trlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKleedagtlealeegKKRLQRELEALTQQLEEkaaay 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2239 --LVKLKLRIEQENKMLILKgKDNTQQFLAEEAEKMKQ----VAEEAARLSVEAQEaaRLRKIAEDDLNEQRALA-EKIL 2311
Cdd:pfam01576 569 dkLEKTKNRLQQELDDLLVD-LDHQRQLVSNLEKKQKKfdqmLAEEKAISARYAEE--RDRAEAEAREKETRALSlARAL 645
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2312 KEKMQAVQEASR----LKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAE---ETEGFQKTLEAERRRQLDISAEAERL 2384
Cdd:pfam01576 646 EEALEAKEELERtnkqLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEmktQLEELEDELQATEDAKLRLEVNMQAL 725
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2385 KLQV-VEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKK 2463
Cdd:pfam01576 726 KAQFeRDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQA 805
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2464 EAELLQKKSEEMQKAQKEQLRQETQTLQSTFLTEKQILIQKE---------KYIEEEKAKLEKLFDNEVGKAQKLKSEKE 2534
Cdd:pfam01576 806 QMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEdlaaserarRQAQQERDELADEIASGASGKSALQDEKR 885
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2535 R---QLAQLEEEKRLLQTSMD-------------DAMKKQLDAEDRIRQKQEEL-QQLDKKrqeqerlleeeNRKLRERL 2597
Cdd:pfam01576 886 RleaRIAQLEEELEEEQSNTEllndrlrkstlqvEQLTTELAAERSTSQKSESArQQLERQ-----------NKELKAKL 954
|
....*
gi 1072265250 2598 EQLEQ 2602
Cdd:pfam01576 955 QEMEG 959
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1680-2247 |
2.23e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.55 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1680 ESALRQKDLAEEELEKQRKLAEETASHKL--SAEQELIRLKAEVDSGEQHRIVLEEDlfrlKNEVNEAIQRRRGLEEELA 1757
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKDLHERlnGLESELAELDEEIERYEEQREQARET----RDEADEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1758 KVRAEMEILLKAKSKAEedsrstsekskqmleveaSKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERIL--K 1835
Cdd:PRK02224 255 TLEAEIEDLRETIAETE------------------REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEarR 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1836 EKLTAINEATRMR-TEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAqhkqDIEEKIhqlkQSSENELERQKTIVDE 1914
Cdd:PRK02224 317 EELEDRDEELRDRlEECRVAAQAHNEEAESLREDADDLEERAEELREEAA----ELESEL----EEAREAVEDRREEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1915 TLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLaLVEEARRKEAEEKVKKIIA 1994
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-LEAGKCPECGQPVEGSPHV 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1995 AEQEAGRQRKVALEEvERLKIKADEAKKQKDLAE----KEAEKQIQLAQDAARlkiDAEEKayyaaVQQKEQEMLQTRIQ 2070
Cdd:PRK02224 468 ETIEEDRERVEELEA-ELEDLEEEVEEVEERLERaedlVEAEDRIERLEERRE---DLEEL-----IAERRETIEEKRER 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2071 EQSiydkLKEEAEKAKRAAEEAERAkikaeheAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQ 2150
Cdd:PRK02224 539 AEE----LRERAAELEAEAEEKREA-------AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDE 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2151 AEQAALKLKQMADAEMEKHKQFAEKTVRqKEQVEGELTKVKLQLEETDHQKAI-----LDDELGRLKEEVTESLRQKKLV 2225
Cdd:PRK02224 608 IERLREKREALAELNDERRERLAEKRER-KRELEAEFDEARIEEAREDKERAEeyleqVEEKLDELREERDDLQAEIGAV 686
|
570 580
....*....|....*....|..
gi 1072265250 2226 EEELFKVKIQMEELVKLKLRIE 2247
Cdd:PRK02224 687 ENELEELEELRERREALENRVE 708
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4041-4079 |
3.15e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.98 E-value: 3.15e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1072265250 4041 LLEAQIATGGIIDPEESHRLPVEMAYKRGLFDEEMNEIL 4079
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1958-2184 |
3.32e-15 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 81.01 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1958 QKSKEKAEQDAEKQRQlalveeARRKEAEEKVKKIIAAEQEagRQRKVALEEVERLKIK------ADEAKKQKDLAEKEA 2031
Cdd:PRK09510 67 QQQQQKSAKRAEEQRK------KKEQQQAEELQQKQAAEQE--RLKQLEKERLAAQEQKkqaeeaAKQAALKQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2032 EKQIQlaqdAARLKIDAEEKAYYAAVQQKEQEMlqtriqeqsiydKLKEEAEKAKRAAEEAerakiKAEHEAALSRQQAE 2111
Cdd:PRK09510 139 AKAAA----AAKAKAEAEAKRAAAAAKKAAAEA------------KKKAEAEAAKKAAAEA-----KKKAEAEAAAKAAA 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 2112 EAerlKQKAEIEAQAKgqAQEDAEkvrKEAELEAAKRgqAEQAALKLKqmADAEMEKHKQFAEKTVRQKEQVE 2184
Cdd:PRK09510 198 EA---KKKAEAEAKKK--AAAEAK---KKAAAEAKAA--AAKAAAEAK--AAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
167-270 |
3.34e-15 |
|
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: 74.31 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 167 KEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDPED 246
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1072265250 247 VDV--PQPDEKSIITYVSSLYDAMPR 270
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1351-1597 |
4.13e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 82.48 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1351 EKLKEQERK-KLAEVED--QLEKQRQLAEAHAQAKAVAEKEALELRMNMQE-----EVTRREVVAVDAEQQKKTIQQELH 1422
Cdd:pfam17380 307 EKAREVERRrKLEEAEKarQAEMDRQAAIYAEQERMAMERERELERIRQEErkrelERIRQEEIAMEISRMRELERLQME 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1423 QMKNN----SETEIKAKVKLIEEaEYNRKKVEE--EIRIIRIQLETSQKQKSGAEDELRAL---RARAEEAERQKK---L 1490
Cdd:pfam17380 387 RQQKNervrQELEAARKVKILEE-ERQRKIQQQkvEMEQIRAEQEEARQREVRRLEEERARemeRVRLEEQERQQQverL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1491 AQEEAERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQ-----------AEEAERRMKQAELEKE 1559
Cdd:pfam17380 466 RQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLekemeerqkaiYEEERRREAEEERRKQ 545
|
250 260 270
....*....|....*....|....*....|....*...
gi 1072265250 1560 RQIKQAHDVAQQSADAELQSKRMSFLEKTTQLEMSLKQ 1597
Cdd:pfam17380 546 QEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVE 583
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
170-265 |
5.07e-15 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 73.93 E-value: 5.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 170 LLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAErELGVTRLLDPED-VD 248
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1072265250 249 VPQPDEKSIITYVSSLY 265
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2807-2845 |
5.83e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.20 E-value: 5.83e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1072265250 2807 LLEAQIATGGIVDPVNSHRLPLDVAYKRGYFDEEMNKTL 2845
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1314-2073 |
8.10e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 81.94 E-value: 8.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1314 EYVELRTKYSELTTLTSQYIKFITETLRRLEEEERTAEKLKEQER-------KKLAEVEDQLEKQRQLAEAHAQAKavaE 1386
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQqshayltQKREAQEEQLKKQQLLKQLRARIE---E 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1387 KEALELRM-NMQEEVTRREVVAVDAEQQKKTIQQElhQMKNNSETEIKAKVKLIEEaeynrkkveeeiriIRIQLETSQK 1465
Cdd:TIGR00618 272 LRAQEAVLeETQERINRARKAAPLAAHIKAVTQIE--QQAQRIHTELQSKMRSRAK--------------LLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1466 QKSGAEDELRALRARAEEAERQKKLAQEEAERLrkqvkdeAQKKREAEDELH-RKVQAEKDAAREKQKALEDlEKFRLQA 1544
Cdd:TIGR00618 336 QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR-------EISCQQHTLTQHiHTLQQQKTTLTQKLQSLCK-ELDILQR 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1545 EEAERRMKQAElEKERQIKQAHDVAQQSADAELQSKRMSFLEKTTQlemSLKQEHItvtHLQEEAERLKKQQleaetake 1624
Cdd:TIGR00618 408 EQATIDTRTSA-FRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ---CEKLEKI---HLQESAQSLKERE-------- 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1625 eaekelekwrqkanealrlrlqaEEIAHKKTLAQEEAEKQKEDAERetRKRTKAEESALRQKDLAEEELEKQRKLAEETA 1704
Cdd:TIGR00618 473 -----------------------QQLQTKEQIHLQETRKKAVVLAR--LLELQEEPCPLCGSCIHPNPARQDIDNPGPLT 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1705 SHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKS 1784
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1785 KQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRaeaerilkekltaineatrmrtEAEIALKEKEAENER 1864
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA----------------------LQLTLTQERVREHAL 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1865 LRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKTIVDETLKHRRVIEEEI--RILKINFEKASVGKSd 1942
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASssLGSDLAAREDALNQS- 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1943 leleLQKLKNIADETQKSKEKAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERlKIKADEAKK 2022
Cdd:TIGR00618 745 ----LKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQ-EIPSDEDIL 819
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1072265250 2023 ---QKDLAEKEAEKQIQLAQDAARL-KIDAEEKAYYAAVQQKEQEML-QTRIQEQS 2073
Cdd:TIGR00618 820 nlqCETLVQEEEQFLSRLEEKSATLgEITHQLLKYEECSKQLAQLTQeQAKIIQLS 875
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
165-262 |
8.50e-15 |
|
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: 73.19 E-value: 8.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQRMSEGyqgLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTN-LENLDQAFTVAERELGVTRLLD 243
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1072265250 244 PEDVDVPQPDEKSIITYVS 262
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3465-3503 |
1.25e-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: 1.25e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1072265250 3465 LLEAQVATGGIIDPVHSHRVPIDVAYKRGYFDEAMNKIL 3503
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1312-2208 |
1.46e-14 |
|
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: 81.25 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1312 IQEYVELRTKYSELTTLTS-----QYIKFITETLRRLEEEERTAEKLKEQERKKLAEVEDQLEKQrqlaeahaQAKAVAE 1386
Cdd:TIGR00606 165 LSEGKALKQKFDEIFSATRyikalETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSK--------EAQLESS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1387 KEALELRMNMQEEVTRRevvavdaeqqkktiQQELHQMKnNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRiqletsQKQ 1466
Cdd:TIGR00606 237 REIVKSYENELDPLKNR--------------LKEIEHNL-SKIMKLDNEIKALKSRKKQMEKDNSELELKM------EKV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1467 KSGAEDELRAL----RARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDELHR-KVQAE--------KDAAREKQKA 1533
Cdd:TIGR00606 296 FQGTDEQLNDLyhnhQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRlQLQADrhqehiraRDSLIQSLAT 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1534 LEDLEKFRLQAeEAERRMKQA-ELEKERQIKQAHDVAQQSADaeLQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERl 1612
Cdd:TIGR00606 376 RLELDGFERGP-FSERQIKNFhTLVIERQEDEAKTAAQLCAD--LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEK- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1613 KKQQLEAETAKEEAEKELEKWRQKANEALRLRLQ----AEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESAlrQKDL 1688
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRILELDQELRKAERelskAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEME--QLNH 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1689 AEEELEKQRKLAEETAS-------HKLSAEQELIRLKAEVDSGEQhrivLEEDLFRLKNEVNEAIQRRRGLEEELAKVRA 1761
Cdd:TIGR00606 530 HTTTRTQMEMLTKDKMDkdeqirkIKSRHSDELTSLLGYFPNKKQ----LEDWLHSKSKEINQTRDRLAKLNKELASLEQ 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1762 EMEILLKAKSKAEEDSRSTSEK-----SKQMLEVEASKLRELAEEAARLRAVSEEAKRQ-----RQLAEEDAT------- 1824
Cdd:TIGR00606 606 NKNHINNELESKEEQLSSYEDKlfdvcGSQDEESDLERLKEEIEKSSKQRAMLAGATAVysqfiTQLTDENQSccpvcqr 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1825 --RQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQ--------------AAQHKQ 1888
Cdd:TIGR00606 686 vfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEipelrnklqkvnrdIQRLKN 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1889 DIEEKIHQLKQSSENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDA 1968
Cdd:TIGR00606 766 DIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKI 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1969 EKQRQLALVEEARRKEAEEKVKKIIAAEQEAGR--QRKVALEE--VERLK-----IKADEAKKQKDLAEKEAEKQIQLAQ 2039
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTnlQRRQQFEEqlVELSTevqslIREIKDAKEQDSPLETFLEKDQQEK 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2040 DAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRaAEEAERAKIKAEHEAALSRQQA--EEAERLK 2117
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLK-QKETELNTVNAQLEECEKHQEKinEDMRLMR 1004
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2118 QKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQaalkLKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEET 2197
Cdd:TIGR00606 1005 QDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQH----LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGY 1080
|
970
....*....|.
gi 1072265250 2198 DHQKAILDDEL 2208
Cdd:TIGR00606 1081 EKEIKHFKKEL 1091
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1350-2031 |
2.24e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.50 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1350 AEKLKEQERKKLAEVEDQLEKQRQ-LAEAHAQAKAVAEKEALELRMNMQEevtrrevVAVDAEQQKKTIQQELHQMKNNS 1428
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQlLEELNKKIKDLGEEEQLRVKEKIGE-------LEAEIASLERSIAEKERELEDAE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1429 ETEIKAKVKlieeaeynRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQK 1508
Cdd:TIGR02169 322 ERLAKLEAE--------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1509 KREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERrmKQAELEKERQIKQAHDVAQQSADAELQSKRMSFLEKT 1588
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA--KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1589 TQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAE------ 1662
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAgnrlnn 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1663 ---KQKEDAER--ETRKRTKA----------------EESALRQK-------DLAE-------------------EELEK 1695
Cdd:TIGR02169 552 vvvEDDAVAKEaiELLKRRKAgratflplnkmrderrDLSILSEDgvigfavDLVEfdpkyepafkyvfgdtlvvEDIEA 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1696 QRKL--------------------------AEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRR 1749
Cdd:TIGR02169 632 ARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1750 RGLEEELAKVRAEMEILLK--AKSKAE-EDSRSTSEKSKQMLEVEASKLRELAEEAARLRAV-----SEEAKRQRQLAEE 1821
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQeeEKLKERlEELEEDLSSLEQEIENVKSELKELEARIEELEEDlhkleEALNDLEARLSHS 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1822 DATRQRAEAERIlKEKLTAINEATRmrtEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQlKQSS 1901
Cdd:TIGR02169 792 RIPEIQAELSKL-EEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK-KEEL 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1902 ENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQdaEKQRQLALVEEAR 1981
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE--ELSEIEDPKGEDE 944
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 1982 RKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIK--ADEAKKQKDLAEKEA 2031
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQeyEEVLKRLDELKEKRA 996
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1410-2036 |
3.06e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.11 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1410 AEQQKKTIQQELHQMKNNSETEIKAKV---KLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAE---E 1483
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTEnieELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1484 AERQKKLAQEEAERLR---KQVKDEAQKKREAEDELHRKVqAEKDAAREKQKALEDLEKFRLQAEEAERRMkqaELEKER 1560
Cdd:PRK03918 243 LEKELESLEGSKRKLEekiRELEERIEELKKEIEELEEKV-KELKELKEKAEEYIKLSEFYEEYLDELREI---EKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1561 QIKQAHDVAQQSADAELQSKRMSFLEKttqlemsLKQEhitvthLQEEAERLKKqqleaetakeeaekelekWRQKANEA 1640
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKK-------KLKE------LEKRLEELEE------------------RHELYEEA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1641 LRLRLQAEEIAHKKT-LAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETAshklSAEQELIRLKA 1719
Cdd:PRK03918 368 KAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK----KAKGKCPVCGR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1720 EVDSGEQHRIVLE--EDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEI---LLKAKSKAEEdSRSTSEKSKqmlEVEASK 1794
Cdd:PRK03918 444 ELTEEHRKELLEEytAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseLIKLKELAEQ-LKELEEKLK---KYNLEE 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1795 LRELAEEAARLRAVSEEAKRQRQLAEEDATRQrAEAERILKEKLTAINEATRMRTEAEIALKEK--EAENERLRRLAEDE 1872
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-EELKKKLAELEKKLDELEEELAELLKELEELgfESVEELEERLKELE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1873 AYQRKLLEEQAAqhKQDIEEKIHQLKqSSENELERQKTIVDETLKHRRVIEEEIRILKINF-----EKASVGKSDLELEL 1947
Cdd:PRK03918 599 PFYNEYLELKDA--EKELEREEKELK-KLEEELDKAFEELAETEKRLEELRKELEELEKKYseeeyEELREEYLELSREL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1948 QKLKNIADETQKSKEKAEQDAEKQRQlalveearrkeaeeKVKKIIAAEQEAGRQRKvALEEVERLKIKadeAKKQKDLA 2027
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKE--------------ELEEREKAKKELEKLEK-ALERVEELREK---VKKYKALL 737
|
....*....
gi 1072265250 2028 EKEAEKQIQ 2036
Cdd:PRK03918 738 KERALSKVG 746
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2073-2797 |
3.85e-14 |
|
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: 80.02 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2073 SIYDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQ-----AEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAK 2147
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKlkeqaKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2148 RGQAEQAAL-KLKQMADAEMEKHKQfaektvRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVE 2226
Cdd:pfam02463 245 LLRDEQEEIeSSKQEIEKEEEKLAQ------VLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2227 EELFKVKIQmEELVKLKLRIEQENKMLILKGKDNTQQFLAEEAEKMKQVAEEAAR--LSVEAQEAARLRKIAEDDLNEQR 2304
Cdd:pfam02463 319 SEKEKKKAE-KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEeeLLAKKKLESERLSSAAKLKEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2305 ALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERL 2384
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2385 KLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAEELRK-AIADLENEKEKLKK 2463
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKvAISTAVIVEVSATA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2464 EAELLQKKSEEMQKAQKEQLRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLFD-NEVGKAQKLKSEKERQLAQLEE 2542
Cdd:pfam02463 558 DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEaDEDDKRAKVVEGILKDTELTKL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2543 EKRLLQTSMDDAMKKQLDAEDRIRQKQEELQQLDKKRQEQERLLEEENRKLRERLEQLEQEHRIALEKTREVIITKEtVI 2622
Cdd:pfam02463 638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK-LK 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2623 TQTKTMPNGRDAADGSAQNGELLNAFDGLRQKISpdklfEAGILTKEQLDKLASGQLTVDDLSKREEIRRYLQGKSSIAG 2702
Cdd:pfam02463 717 LEAEELLADRVQEAQDKINEELKLLKQKIDEEEE-----EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2703 LLLKPSNEKMSIYNAMKKKLVTPGTALILLEAQAASGFITDPVGNKRLTVSEAVKENVIGPEVHNKLLSAERAITGYKDP 2782
Cdd:pfam02463 792 KEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
730
....*....|....*
gi 1072265250 2783 YTGEKISLFQAMNKD 2797
Cdd:pfam02463 872 LLLKEEELEEQKLKD 886
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
45-150 |
4.61e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 71.17 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 45 QKKTFTKWVNKHLIKHwraEAQRHVNDLYEDLRDGHNLISLLEVLSGETL------PREKGRMRfhklQNVQIALDFLKL 118
Cdd:cd21213 1 QLQAYVAWVNSQLKKR---PGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMAS 73
|
90 100 110
....*....|....*....|....*....|..
gi 1072265250 119 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 150
Cdd:cd21213 74 KRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
167-268 |
5.91e-14 |
|
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: 71.27 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 167 KEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDPED 246
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1072265250 247 -VDVPQPDEKSIITYVSSLYDAM 268
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1948-2180 |
6.93e-14 |
|
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: 76.42 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1948 QKLKNIADETQKSKEKAEQDAEKQrqlalveearrkeaeekvKKIIAAEQEAGRQRKVALEEVERLKiKADEAKKQKDLA 2027
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEA------------------EKQRAAEQARQKELEQRAAAEKAAK-QAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2028 EKEAE--KQIQLAQDAARLKIDAEEKAYYAAVQQKEQEML-----QTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAE 2100
Cdd:TIGR02794 118 QKQAEeaKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKakaaaEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2101 HEAALSRQQAEEAErlKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMADAEMEKHKQFAEKTVRQK 2180
Cdd:TIGR02794 198 AEAAKAKAAAEAAA--KAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
165-265 |
7.57e-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: 70.87 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAErELGVTRLLDP 244
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1072265250 245 ED-VDVPQPDEKSIITYVSSLY 265
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1381-2127 |
1.10e-13 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 78.34 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1381 AKAVAEKEAL--ELRMNMQEEVTRREVVAVDAEQQKKTIQQELHQMKNNSETE-IKAKVKLIEEAEYNRKKVEEEIRIIR 1457
Cdd:pfam12128 185 AKAMHSKEGKfrDVKSMIVAILEDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMkIRPEFTKLQQEFNTLESAELRLSHLH 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1458 IQLETSQKQKSGAEDELRALRARAEEAERQ--KKLAQEEAE-RLRKQVKDEAQKKREAEDEL--HRKVQAEKDAAREKQK 1532
Cdd:pfam12128 265 FGYKSDETLIASRQEERQETSAELNQLLRTldDQWKEKRDElNGELSAADAAVAKDRSELEAleDQHGAFLDADIETAAA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1533 ALEDLEKFRLQAEEAERRMKqAELEKERQIKQAHDVAQQSADAELQSKRMSFLEKT-TQLEMSLKQEHITVTHLQEEAER 1611
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLK-ALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLaKIREARDRQLAVAEDDLQALESE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1612 LKKQQLEAETAKEEAEKELEKwrqkANEALRLRLqAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESALrqkdlaEE 1691
Cdd:pfam12128 424 LREQLEAGKLEFNEEEYRLKS----RLGELKLRL-NQATATPELLLQLENFDERIERAREEQEAANAEVERL------QS 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1692 ELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFR-LKNEVNeaiqrrrGLEEELAKVrAEMEILLKAk 1770
Cdd:pfam12128 493 ELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHfLRKEAP-------DWEQSIGKV-ISPELLHRT- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1771 skaEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTA---INEATRM 1847
Cdd:pfam12128 564 ---DLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQAngeLEKASRE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1848 RTEAEIALKEKEaenERLRRLA-EDEAYQRKlLEEQAAQHKQDIEEKIHQL-KQSSENELERQktivdETLKHRRVIEEE 1925
Cdd:pfam12128 641 ETFARTALKNAR---LDLRRLFdEKQSEKDK-KNKALAERKDSANERLNSLeAQLKQLDKKHQ-----AWLEEQKEQKRE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1926 IRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLAL--VEEARRKEAEEKVKKIIAA-EQEAGRQ 2002
Cdd:pfam12128 712 ARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASlgVDPDVIAKLKREIRTLERKiERIAVRR 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2003 RKVALEEV---ERLKIKADEAKKQKDLAEKEAEkqiQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQsiYDKLK 2079
Cdd:pfam12128 792 QEVLRYFDwyqETWLQRRPRLATQLSNIERAIS---ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSEN--LRGLR 866
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1072265250 2080 EEAEKAKRAAEEAERAkiKAEHEAALSRQQAEEAeRLKQKAEIEAQAK 2127
Cdd:pfam12128 867 CEMSKLATLKEDANSE--QAQGSIGERLAQLEDL-KLKRDYLSESVKK 911
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
38-149 |
1.11e-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: 70.00 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 38 EDERDrvqKKTFTKWVNKHLIKHwraeaqrHVNDLYEDLRDGhnlISLLEVL--------SGETLPREKGRMRFHKLQNV 109
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDP-------LINNLYEDLRDG---LVLLQVLdkiqpgcvNWKKVNKPKPLNKFKKVENC 67
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1072265250 110 QIALDFLKLRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 149
Cdd:cd21219 68 NYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1355-1914 |
1.22e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1355 EQERKKLAEVEDQLEKQRQLA-----------EAHAQAK---AVAEKEALELRMNMQEEVTRREVVA---VDAEQQKKTI 1417
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQAretrdeadevlEEHEERReelETLEAEIEDLRETIAETEREREELAeevRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1418 QQELHQMKNNSE---TEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEaerqkklaqee 1494
Cdd:PRK02224 292 EEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE----------- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1495 aerlrkqvkdeaqkKREAEDELHRKVQAEKDAAREKQKALEDLEKfrlQAEEAERRMKQAELEKERqikqahdvaQQSAD 1574
Cdd:PRK02224 361 --------------LREEAAELESELEEAREAVEDRREEIEELEE---EIEELRERFGDAPVDLGN---------AEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1575 AELQSKRMSFLEKTTQLEMSLKQEHITVthlqEEAERLkkqqleaetakeeaekelekwrQKANEALRLRLQAEEIAHKK 1654
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERV----EEAEAL----------------------LEAGKCPECGQPVEGSPHVE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1655 TLAQEEAEKQKEDAERETRKrtkaeesalrqkdLAEEELEKqrklaeetashKLSAEQELIRLKAEVDSGEQHRIVLEED 1734
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLE-------------EEVEEVEE-----------RLERAEDLVEAEDRIERLEERREDLEEL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1735 LFRLKNEVNEAIQRRRGLEEELAKVRAEMEillkAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEeakr 1814
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAE----EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRT---- 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1815 qrQLAEEDATRQRAEAeriLKEKLTAINEATRMRTEaeiALKEKeaeNERLRRLAE-------DEAYQRKlleEQAAQHK 1887
Cdd:PRK02224 597 --LLAAIADAEDEIER---LREKREALAELNDERRE---RLAEK---RERKRELEAefdeariEEAREDK---ERAEEYL 662
|
570 580 590
....*....|....*....|....*....|....*..
gi 1072265250 1888 QDIEEKIHQLKQ----------SSENELERQKTIVDE 1914
Cdd:PRK02224 663 EQVEEKLDELREerddlqaeigAVENELEELEELRER 699
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
42-146 |
2.14e-13 |
|
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: 69.48 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 42 DRVQKKTFTKWVNKHLIKhwraEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFL-K 117
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEK----RGIPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIeE 77
|
90 100
....*....|....*....|....*....
gi 1072265250 118 LRQVKLVNIRNDDIADGNPKLTLGLIWTI 146
Cdd:cd21225 78 DLKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
165-265 |
4.23e-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: 68.52 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAErELGVTRLLDP 244
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1072265250 245 ED-VDVPQPDEKSIITYVSSLY 265
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3058-3096 |
4.75e-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: 4.75e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1072265250 3058 LLEAQAGTGFIIDPVTKELLPVDEAVKAGIVGPEYHEKL 3096
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3722-3760 |
4.80e-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: 4.80e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1072265250 3722 LLDAQAATGFIIDPVKNELLTVDEAVRKGVVGPEIHDRL 3760
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
167-262 |
4.94e-13 |
|
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: 68.18 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 167 KEKLLLWSQRMsegYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLI-DMNRVYRQTNLENLDQAFTVAERELGVTRLLDPE 245
Cdd:cd21229 5 KKLMLAWLQAV---LPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1072265250 246 DVDVPQPDEKSIITYVS 262
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
64-147 |
5.75e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 68.00 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 64 EAQRHVNDLYEDLRDGHNLISLLEVLSGETLPREKGRM----RFHKLQNVQIALDFLKLRQV----KLVNIRNDDIADGN 135
Cdd:cd21223 21 EFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGH 100
|
90
....*....|..
gi 1072265250 136 PKLTLGLIWTII 147
Cdd:cd21223 101 REKTLALLWRII 112
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2258-2578 |
6.26e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 75.55 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2258 KDNTQQFLAEEAEKMKQVAEEAARlsveaqEAARLRKIAEDD------LNEQRALAEKILKEKMQAVQEASRLKAEA--- 2328
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAR------EVERRRKLEEAEkarqaeMDRQAAIYAEQERMAMERERELERIRQEErkr 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2329 EMLQ-KQKEMAMEQAKKLQEDKEQMQQQlaEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKkfrk 2407
Cdd:pfam17380 361 ELERiRQEEIAMEISRMRELERLQMERQ--QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ---- 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2408 qaedisEKLHQTELSTKEKMTVVHTLEIQRQHsdkEAEELRKAIADLenekeklkkeaellQKKSEEMQKAQKEQLRQET 2487
Cdd:pfam17380 435 ------REVRRLEEERAREMERVRLEEQERQQ---QVERLRQQEEER--------------KRKKLELEKEKRDRKRAEE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2488 QTLQstfLTEKQILIQKEKYIEEEKAKleKLFDNEVGKAQKL--------KSEKERQLAQLEEEKRLLQTSMDDAM--KK 2557
Cdd:pfam17380 492 QRRK---ILEKELEERKQAMIEEERKR--KLLEKEMEERQKAiyeeerrrEAEEERRKQQEMEERRRIQEQMRKATeeRS 566
|
330 340
....*....|....*....|.
gi 1072265250 2558 QLDAEDRIRQKQEELQQLDKK 2578
Cdd:pfam17380 567 RLEAMEREREMMRQIVESEKA 587
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1440-2052 |
6.84e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1440 EEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVkdEAQKKREAEDELHRK 1519
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--EKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1520 VQAEKDaaREKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQSKRMSFLEKTTQLEMSLKQEh 1599
Cdd:PRK03918 239 EIEELE--KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1600 itVTHLQEEAERLKKQqleaetakeeaekelekwrqkANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAE 1679
Cdd:PRK03918 316 --LSRLEEEINGIEER---------------------IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1680 ESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEE---- 1755
Cdd:PRK03918 373 ELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrke 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1756 -LAKVRAEMEILLKAKSKAEEDSRStsekskqmLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERIL 1834
Cdd:PRK03918 453 lLEEYTAELKRIEKELKEIEEKERK--------LRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKA 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1835 KEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQdIEEKIHQLKQSSENELERQKTIVDE 1914
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE-LEELGFESVEELEERLKELEPFYNE 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1915 TLKHR------RVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQksKEKAEQDAEKQRQLALVEEARRKEAEEK 1988
Cdd:PRK03918 604 YLELKdaekelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREEYLELSRELAGLRAE 681
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 1989 VKKIIAAEQEAgrqrKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKA 2052
Cdd:PRK03918 682 LEELEKRREEI----KKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERA 741
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2116-2604 |
8.39e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.10 E-value: 8.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2116 LKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMAdaEMEKHKQFAEKTVRQKEQVEGELTKVKLQLE 2195
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK--ELEELKEEIEELEKELESLEGSKRKLEEKIR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2196 ETDHQKAILDDELGRLKEEVTEsLRQKKLVEEELFKVKIQMEELVKLKLRIEQEnkMLILKGKDNTQQFLAEEAEKMKQV 2275
Cdd:PRK03918 263 ELEERIEELKKEIEELEEKVKE-LKELKEKAEEYIKLSEFYEEYLDELREIEKR--LSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2276 AEEAARLSVEAQEaaRLRKIAEDDLNEQRALAEKILKEKMQ---AVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQM 2352
Cdd:PRK03918 340 LEELKKKLKELEK--RLEELEERHELYEEAKAKKEELERLKkrlTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2353 QQQLAEETEGFQKTLEAERR-----RQLDISAEAE---RLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTK 2424
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKElleEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2425 EKMTVVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQ-----KEQLRQETQTLQSTFLT-EK 2498
Cdd:PRK03918 498 LKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelkkkLAELEKKLDELEEELAElLK 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2499 QILIQKEKYIEEEKAKLEKL--FDNEVGKAQKLKSEKERqlaqLEEEKRLLQTSMDDAMKKQLDAEDRIRQKQEELQQLD 2576
Cdd:PRK03918 578 ELEELGFESVEELEERLKELepFYNEYLELKDAEKELER----EEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
490 500
....*....|....*....|....*...
gi 1072265250 2577 KKrqeqerLLEEENRKLRERLEQLEQEH 2604
Cdd:PRK03918 654 KK------YSEEEYEELREEYLELSREL 675
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1354-2165 |
1.01e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 75.15 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1354 KEQERKKLAEVEDQLEK-QRQLAEA---HAQAKAVAEKEALELRMNMQEEVTRREVVAvDAEQQKKTIQQELHQMKNNSE 1429
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDlQRRLNESnelHEKQKFYLRQSVIDLQTKLQEMQMERDAMA-DIRRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1430 TEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLEtsqkqksGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKK 1509
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTQIEQLRKMMLSHE-------GVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1510 reaedeLHRKVQAEKDAAREKQKALED-LEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQSKRMSFLEKT 1588
Cdd:pfam15921 225 ------ILRELDTEISYLKGRIFPVEDqLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1589 TQLEMslkqehitvthLQEEAerlKKQQLEAETAKEEAEKELEKWRQKANEALRL-RLQAEEIAHKKTLAQEEAEKQKed 1667
Cdd:pfam15921 299 SQLEI-----------IQEQA---RNQNSMYMRQLSDLESTVSQLRSELREAKRMyEDKIEELEKQLVLANSELTEAR-- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1668 AERETRKRTKAEESALRQKDLAeeELEKQRKlaeetashKLSAEQELIRLKAEVDSGEQHRIvleEDLFRLKNEVNEAIQ 1747
Cdd:pfam15921 363 TERDQFSQESGNLDDQLQKLLA--DLHKREK--------ELSLEKEQNKRLWDRDTGNSITI---DHLRRELDDRNMEVQ 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1748 RRRGLEEEL-AKVRAEMEILLKAKSKAEEDSRSTSEKSKQmLEVEASKLRELAEEAARLRAVSEEAKRqrqlAEEDATRQ 1826
Cdd:pfam15921 430 RLEALLKAMkSECQGQMERQMAAIQGKNESLEKVSSLTAQ-LESTKEMLRKVVEELTAKKMTLESSER----TVSDLTAS 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1827 RAEAERILKekltAIN-EATRMRTEAEIALKEKE---AENERLRRL-AEDEAYQRKLLEEQAAQH--KQDIEEKIHQLKQ 1899
Cdd:pfam15921 505 LQEKERAIE----ATNaEITKLRSRVDLKLQELQhlkNEGDHLRNVqTECEALKLQMAEKDKVIEilRQQIENMTQLVGQ 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1900 --SSENELERQKTIVDETLKHRRVIEEEIRIL------KINFEKASVgkSDLELELQKLKNIADEtqksKEKAEQDAEKQ 1971
Cdd:pfam15921 581 hgRTAGAMQVEKAQLEKEINDRRLELQEFKILkdkkdaKIRELEARV--SDLELEKVKLVNAGSE----RLRAVKDIKQE 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1972 RQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERlKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEK 2051
Cdd:pfam15921 655 RDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTN-KLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2052 AYYAAvQQKEQEMLQTRIQ--EQSIYDKLKE----EAEKAKRAAEEAERAKIKAEHEAALSRQQAEEaERLKQKAeieaq 2125
Cdd:pfam15921 734 KQITA-KRGQIDALQSKIQflEEAMTNANKEkhflKEEKNKLSQELSTVATEKNKMAGELEVLRSQE-RRLKEKV----- 806
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1072265250 2126 AKGQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMADAE 2165
Cdd:pfam15921 807 ANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVK 846
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3389-3427 |
1.25e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 64.66 E-value: 1.25e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1072265250 3389 LLEAQAATGFIIDPVKNQKFYVNEAVKAGIVGPELHEKL 3427
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
167-267 |
1.40e-12 |
|
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: 66.99 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 167 KEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTVAERELGVTRLLDPED 246
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1072265250 247 VdVPQPDEKSIITYVSSLYDA 267
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3134-3172 |
1.76e-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: 1.76e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1072265250 3134 LLSAQLATGGIIDPVNSHRLPLEIAYKRGHLDEETTKLL 3172
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
36-144 |
4.10e-12 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 65.91 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 36 DAEDERD-RVqkktFTKWVNKhlikhwrAEAQRHVNDLYEDLRDGHNLISLLE-VLSGE-------TLPREKGRMRFHKL 106
Cdd:cd21300 2 DAEGEREaRV----FTLWLNS-------LDVEPAVNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAV 70
|
90 100 110
....*....|....*....|....*....|....*...
gi 1072265250 107 QNVQIALDFLKLRQVKLVNIRNDDIADGNPKLTLGLIW 144
Cdd:cd21300 71 ENTNYAVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
47-153 |
4.26e-12 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 65.72 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 47 KTFTKWVNKhlikhwrAEAQRHVNDLYEDLRDGHNLISLLEVL-------SGETLPREKGRMRFHKLQNVQIALDFLKLR 119
Cdd:cd21298 9 KTYRNWMNS-------LGVNPFVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKL 81
|
90 100 110
....*....|....*....|....*....|....
gi 1072265250 120 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 153
Cdd:cd21298 82 KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1351-1611 |
5.35e-12 |
|
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: 72.78 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1351 EKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAV---AEKEALELRMNMQEEVTRREVVAVDAEQQKKTIQQELHQMKNN 1427
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKEleeLSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1428 SETEIKAKVKLiEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARA---------------------EEAER 1486
Cdd:TIGR02168 767 EERLEEAEEEL-AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlrerleslerriaaterrlEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1487 QKKLAQEEAERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAE--LEKERQIKQ 1564
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRreLEELREKLA 925
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1072265250 1565 AHDVAQQSADAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAER 1611
Cdd:TIGR02168 926 QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1778-2613 |
6.35e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 72.77 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1778 RSTSEKSKQMLEVEASKLRELAEEAARLRavSEEAKRQRQLAEEDATRQRAEAE-RILKEKLTAI--NEATRMRTEAEI- 1853
Cdd:TIGR00606 195 RQTQGQKVQEHQMELKYLKQYKEKACEIR--DQITSKEAQLESSREIVKSYENElDPLKNRLKEIehNLSKIMKLDNEIk 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1854 ALKEKEAENERLRrlaedeayqrKLLEEQAAQHKQDIEEKIHQLKQSSENElerqktiVDETLKHRRVIEEEIRILKINF 1933
Cdd:TIGR00606 273 ALKSRKKQMEKDN----------SELELKMEKVFQGTDEQLNDLYHNHQRT-------VREKERELVDCQRELEKLNKER 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1934 EKASVGKSDLELELQKLKNIADETQ-KSKEKAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEaGRQRKVALEever 2012
Cdd:TIGR00606 336 RLLNQEKTELLVEQGRLQLQADRHQeHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIE-RQEDEAKTA---- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2013 lkikadeAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEEA 2092
Cdd:TIGR00606 411 -------AQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKA 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2093 ERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEK-----VRKEAELEAAKRGQAEQAALKLKQMADAEME 2167
Cdd:TIGR00606 484 ERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhttTRTQMEMLTKDKMDKDEQIRKIKSRHSDELT 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2168 K------HKQFAEKTV----RQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTEslrqkklVEEELFKV-KIQM 2236
Cdd:TIGR00606 564 SllgyfpNKKQLEDWLhsksKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS-------YEDKLFDVcGSQD 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2237 EE--LVKLKLRIEQENKML-ILKGKDNT-QQFLAEEAEK--------------MKQVAEEAARLS-------VEAQEAAR 2291
Cdd:TIGR00606 637 EEsdLERLKEEIEKSSKQRaMLAGATAVySQFITQLTDEnqsccpvcqrvfqtEAELQEFISDLQsklrlapDKLKSTES 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2292 LRKIAEDDLNEQRALAE-------------KILKEKMQAV-QEASRLKAEAEMLQKQKEMAM---EQAKKLQED---KEQ 2351
Cdd:TIGR00606 717 ELKKKEKRRDEMLGLAPgrqsiidlkekeiPELRNKLQKVnRDIQRLKNDIEEQETLLGTIMpeeESAKVCLTDvtiMER 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2352 MQQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQ--------VVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELST 2423
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQekqheldtVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2424 KEKMTVVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQLRQETQTLQSTFLTEKQILIQ 2503
Cdd:TIGR00606 877 GTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGY 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2504 K---EKYIEEEKAKLEKLFDNEVGKAQKLKSEKERQLAQLEEEKRLLQTSMDDA------MKKQLD---AEDRIRQKQEE 2571
Cdd:TIGR00606 957 MkdiENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQkiqerwLQDNLTlrkRENELKEVEEE 1036
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1072265250 2572 LQQLDKKRQEQE-RLLEEENRKLRERLEQLEQEHRIALEKTRE 2613
Cdd:TIGR00606 1037 LKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGRQKG 1079
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1994-2202 |
8.93e-12 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 69.87 E-value: 8.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1994 AAEQEAGRQRKvaleevERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQS 2073
Cdd:TIGR02794 47 AVAQQANRIQQ------QKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2074 IYDKLKEEAEKAKRAAE-EAER-AKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRgqA 2151
Cdd:TIGR02794 121 AEEAKAKQAAEAKAKAEaEAERkAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK--A 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1072265250 2152 EQAALKLKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKA 2202
Cdd:TIGR02794 199 EAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1995-2450 |
1.13e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.61 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1995 AEQEAGRQRKVALEEV-----ERLK----IKADEAKKQKDLAEKEAEK-----QIQLAQDAA-RLKIDAEEKAYYAAVQQ 2059
Cdd:PRK02224 227 EQREQARETRDEADEVleeheERREeletLEAEIEDLRETIAETEREReelaeEVRDLRERLeELEEERDDLLAEAGLDD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2060 KEQEMLQTRI-----QEQSIYDKLKEEAEKAKRAAEEAERAKIKA---EHEAALSRQQAEEAERLKQKAEiEAQAKGQAQ 2131
Cdd:PRK02224 307 ADAEAVEARReeledRDEELRDRLEECRVAAQAHNEEAESLREDAddlEERAEELREEAAELESELEEAR-EAVEDRREE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2132 -----EDAEKVRKEAELEAAKRGQAEQAALKLKQMAD------AEMEKHKQFAEKTVRQKEQV--EGELTKVKLQLEETD 2198
Cdd:PRK02224 386 ieeleEEIEELRERFGDAPVDLGNAEDFLEELREERDelrereAELEATLRTARERVEEAEALleAGKCPECGQPVEGSP 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2199 HQKAILDDElgRLKEEVTESLRQKKLVEEELFKVKIQMEELVKLKLRIE--QENKMLILKGKDNTQQFLAEEAEKMKQVA 2276
Cdd:PRK02224 466 HVETIEEDR--ERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIErlEERREDLEELIAERRETIEEKRERAEELR 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2277 EEAARLSVEAQE----AARLRKIAEDDLNEQRALAEKI--LKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKE 2350
Cdd:PRK02224 544 ERAAELEAEAEEkreaAAEAEEEAEEAREEVAELNSKLaeLKERIESLERIRTLLAAIADAEDEIERLREKREALAELND 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2351 QMQQQLAEETEgfqktleaeRRRQLDISAEAERLklqvvemsksqAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVV 2430
Cdd:PRK02224 624 ERRERLAEKRE---------RKRELEAEFDEARI-----------EEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
490 500
....*....|....*....|
gi 1072265250 2431 HTLEiqrqHSDKEAEELRKA 2450
Cdd:PRK02224 684 GAVE----NELEELEELRER 699
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1998-2343 |
1.17e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 71.31 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1998 EAGRQRKVALEEVERLKI----KADEAKKQKDLAEKEAEKQIQLAQDAArlkIDAEEKAYyaaVQQKEQEMLQTRIQEQs 2073
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQekeeKAREVERRRKLEEAEKARQAEMDRQAA---IYAEQERM---AMERERELERIRQEER- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2074 iydklKEEAEKAKRAAEEAERAKIKAEHEAALSRQQaeEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQ 2153
Cdd:pfam17380 359 -----KRELERIRQEEIAMEISRMRELERLQMERQQ--KNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2154 AAlklkqmadaemekhkqfAEKTVRQKEQVEGELTKVKLQLEETDHQKAIL---DDELGRLKEEVTESLRQKKLVEEELF 2230
Cdd:pfam17380 432 AR-----------------QREVRRLEEERAREMERVRLEEQERQQQVERLrqqEEERKRKKLELEKEKRDRKRAEEQRR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2231 KVKIQMEELVKLKLrIEQENKMLILKgkdntqqflAEEAEKMKQVAEEAARLsvEAQEAARlrkiAEDDLNEQRALAEKI 2310
Cdd:pfam17380 495 KILEKELEERKQAM-IEEERKRKLLE---------KEMEERQKAIYEEERRR--EAEEERR----KQQEMEERRRIQEQM 558
|
330 340 350
....*....|....*....|....*....|....*.
gi 1072265250 2311 lkekMQAVQEASRLKA---EAEMLQKQKEMAMEQAK 2343
Cdd:pfam17380 559 ----RKATEERSRLEAmerEREMMRQIVESEKARAE 590
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1407-1831 |
1.43e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1407 AVDAEQQKKTIQQELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQkqksgAEDELRALRARAEEAER 1486
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-----LEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1487 QKKlAQEEAERLRKQVKDEAQKKREAEDELHRKVQAEKdaAREKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAH 1566
Cdd:COG4717 154 RLE-ELRELEEELEELEAELAELQEELEELLEQLSLAT--EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1567 DVAQQSADAELQskrmsflEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQ 1646
Cdd:COG4717 231 QLENELEAAALE-------ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1647 AEEI---AHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDS 1723
Cdd:COG4717 304 AEELqalPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1724 GEQHRIVLEEdlfrlKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSkaEEDSRSTSEKSKQMLEVEASKLRELAEEAA 1803
Cdd:COG4717 384 EEELRAALEQ-----AEEYQELKEELEELEEQLEELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELA 456
|
410 420
....*....|....*....|....*...
gi 1072265250 1804 RLRAVSEEAKRQRQLAEEDATRQRAEAE 1831
Cdd:COG4717 457 ELEAELEQLEEDGELAELLQELEELKAE 484
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1155-1956 |
1.61e-11 |
|
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: 71.15 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1155 AREVSERMLKVHSERDVDLERYREKVQLLLERWQAIVLQIEVRQRELEQLGKQLRYYRESYEWLIRWITEAKKRQEKIQN 1234
Cdd:TIGR00618 182 ALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1235 VpitdsKTVKEQLMEEKKLLEESEKNRGKVDECQKYAK--QYIEAIKDFEVQLVTYKAQVEPVVSPLKKPKVHSAsdNII 1312
Cdd:TIGR00618 262 L-----KQLRARIEELRAQEAVLEETQERINRARKAAPlaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA--AHV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1313 QEYVELRTKYSELTTLTSQYIKFitetlrrlEEEERTAEKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKealel 1392
Cdd:TIGR00618 335 KQQSSIEEQRRLLQTLHSQEIHI--------RDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKE----- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1393 rmnmqEEVTRREVVAVDAEQQKktiQQELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAED 1472
Cdd:TIGR00618 402 -----LDILQREQATIDTRTSA---FRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1473 ELRALRARAEEAERQKKLAQEEAERLRKQVKDeaQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMK 1552
Cdd:TIGR00618 474 QLQTKEQIHLQETRKKAVVLARLLELQEEPCP--LCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1553 QAELEKERQIKQAHDVAQQSadaelqskrmsfLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAEtakeeaekelek 1632
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQS------------FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE------------ 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1633 wRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEEsalrqkdLAEEELEKqrKLAEETASHKLSAEQ 1712
Cdd:TIGR00618 608 -DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT-------LTQERVRE--HALSIRVLPKELLAS 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1713 ELIRLKAEVDSGEQHRIVLEEdlfrlKNEVNEAIQRRRGLEEELAKVRAEMEILL---KAKSKAEEDSRSTSEKSKQMLE 1789
Cdd:TIGR00618 678 RQLALQKMQSEKEQLTYWKEM-----LAQCQTLLRELETHIEEYDREFNEIENASsslGSDLAAREDALNQSLKELMHQA 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1790 VEASKLRELAEEAARLRAVSEEAKRQR--QLAEEDATRQRAEAERILKEKLtaineatrmrTEAEIALKEKEAENErlrR 1867
Cdd:TIGR00618 753 RTVLKARTEAHFNNNEEVTAALQTGAElsHLAAEIQFFNRLREEDTHLLKT----------LEAEIGQEIPSDEDI---L 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1868 LAEDEAYQRKllEEQAAQHKQDIEEKIHQLKQSSENELERQKTIVDETLKHRRVIEEE-----IRILKINFEKASVGKSD 1942
Cdd:TIGR00618 820 NLQCETLVQE--EEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSdklngINQIKIQFDGDALIKFL 897
|
810
....*....|....
gi 1072265250 1943 LELELQKLKNIADE 1956
Cdd:TIGR00618 898 HEITLYANVRLANQ 911
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1669-2359 |
1.67e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 70.91 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1669 ERETRKRTKAE-ESALRQKdlaEEELEKQRKL--AEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFR-----LKN 1740
Cdd:pfam05483 86 EAEKIKKWKVSiEAELKQK---ENKLQENRKIieAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnlLKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1741 EVNEAIQRRRGLE---EELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEasklreLAEEAARLRAVSEEAKRQRQ 1817
Cdd:pfam05483 163 TCARSAEKTKKYEyerEETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFK------LKEDHEKIQHLEEEYKKEIN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1818 LAEEDATR---QRAEAERILKE----------KLTAINEATRMRTEAeiaLKEKEAENERLRRLAED--EAYQRKLLEEQ 1882
Cdd:pfam05483 237 DKEKQVSLlliQITEKENKMKDltflleesrdKANQLEEKTKLQDEN---LKELIEKKDHLTKELEDikMSLQRSMSTQK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1883 AAQHKQDIEEK-IHQLKQSSENELER-------QKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIA 1954
Cdd:pfam05483 314 ALEEDLQIATKtICQLTEEKEAQMEElnkakaaHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1955 DETQKSKEKAEQDAEKqrqlalveearrkeaeekVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEK- 2033
Cdd:pfam05483 394 EEMTKFKNNKEVELEE------------------LKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDl 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2034 QIQLAqdaarlKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEA 2113
Cdd:pfam05483 456 EIQLT------AIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQE 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2114 ERLKQKAEIEAQAKGQAQEDAEKVRKEAeleaakRGQAEQAALKLKQmADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQ 2193
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDELESVREEF------IQKGDEVKCKLDK-SEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2194 LEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELFKVKIQMEElVKLKLRIEQENKMLILKGKDNTQQFLAEEAEKMK 2273
Cdd:pfam05483 603 IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS-AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2274 QVAEEAARLSVEAQEAARlRKIAE------------DDLNEQRALAEKILKEKMQAVQ--------EASRLKAEAEMLQK 2333
Cdd:pfam05483 682 AIADEAVKLQKEIDKRCQ-HKIAEmvalmekhkhqyDKIIEERDSELGLYKNKEQEQSsakaaleiELSNIKAELLSLKK 760
|
730 740
....*....|....*....|....*.
gi 1072265250 2334 QKEMAMEQAKKLQEDKEQMQQQLAEE 2359
Cdd:pfam05483 761 QLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1472-2004 |
1.96e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.10 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1472 DELRALRARAEEAERQKKL---AQEEAERLRKQVKDEAQKkrEAEDELHRKVQAEKdAAREKQKALEDLEKFRLQAEEAE 1548
Cdd:COG4913 235 DDLERAHEALEDAREQIELlepIRELAERYAAARERLAEL--EYLRAALRLWFAQR-RLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1549 RRMKQAELEKERQIKQAHDVAQQSADAELQskrmsflekttQLEMSLKQEHITVTHLQEEAERLKKQqleAETAKEEAEK 1628
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGNGGDRLE-----------QLEREIERLERELEERERRRARLEAL---LAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1629 ELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAEREtRKRTKAEESAL--RQKDLAEEELEKQRKLAEETash 1706
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE-LRELEAEIASLerRKSNIPARLLALRDALAEAL--- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1707 KLSAEQ-----ELIrlkaEVDSGEQH--------------RIVLEEDLFRlknEVNEAIqRRRGLEEEL--AKVRAEmei 1765
Cdd:COG4913 454 GLDEAElpfvgELI----EVRPEEERwrgaiervlggfalTLLVPPEHYA---AALRWV-NRLHLRGRLvyERVRTG--- 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1766 lLKAKSKAEEDSRSTSEKskqmLEVEASKLR-----ELAEEAARLRAVSEEA-----------------------KRQRQ 1817
Cdd:COG4913 523 -LPDPERPRLDPDSLAGK----LDFKPHPFRawleaELGRRFDYVCVDSPEElrrhpraitragqvkgngtrhekDDRRR 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1818 LAEE-----DATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLleEQAAQHKQDIEE 1892
Cdd:COG4913 598 IRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1893 KIHQLKQSS------ENELERQKTIVDETLKHRRVIEEEIRILKINFEkasvgksDLELELQKLKNIADETQKSKEKA-E 1965
Cdd:COG4913 676 ELERLDASSddlaalEEQLEELEAELEELEEELDELKGEIGRLEKELE-------QAEEELDELQDRLEAAEDLARLElR 748
|
570 580 590
....*....|....*....|....*....|....*....
gi 1072265250 1966 QDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRK 2004
Cdd:COG4913 749 ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4309-4347 |
2.23e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.19 E-value: 2.23e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1072265250 4309 LLEAQACTGGIIDPITGEKFAVADAVNKGLVDKIMVDRI 4347
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1956-2160 |
2.28e-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: 68.72 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1956 ETQKSKEKAEQDAEKQRQlalveearrKEAEEK---VKKIIAAEQEAGRQRKVALEEVERLKiKADEAKKQKDLAEKEAE 2032
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQ---------KKLEQQaeeAEKQRAAEQARQKELEQRAAAEKAAK-QAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2033 --KQIQLAQDAARLKIDAEEKAYYAAVQQKEQEmlqtriqeqsiydKLKEEAEKAKRAAEEAER-----AKIKAEHEA-A 2104
Cdd:TIGR02794 123 eaKAKQAAEAKAKAEAEAERKAKEEAAKQAEEE-------------AKAKAAAEAKKKAEEAKKkaeaeAKAKAEAEAkA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2105 LSRQQAEEAERLKQKAEIEAQAKGQA----QEDAEKVRKEAELEAAKRGQAEQAALKLKQ 2160
Cdd:TIGR02794 190 KAEEAKAKAEAAKAKAAAEAAAKAEAeaaaAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1366-1822 |
2.28e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1366 DQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEevTRREVVAVDAEQQKKTIQQELHQMKNnsetEIKAKVKLIEEAEYN 1445
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEE--LEAELEELREELEKLEKLLQLLPLYQ----ELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1446 RKKVEEEIRiiriQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEA-ERLRKQVKDEAQKKREAEDELhRKVQAEK 1524
Cdd:COG4717 148 LEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEEL-EEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1525 DAAREKQKALEDlekfRLQAEEAERRMKQAE---------LEKERQIKQAHDVAQQSADA-------------ELQSKRM 1582
Cdd:COG4717 223 EELEEELEQLEN----ELEAAALEERLKEARlllliaaalLALLGLGGSLLSLILTIAGVlflvlgllallflLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1583 SFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAE 1662
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1663 KQKEDAEretrkrtkAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEvdsgeqhriVLEEDLFRLKNEV 1742
Cdd:COG4717 379 AGVEDEE--------ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE---------ELEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1743 NEAIQRRRGLEEELAKVRAEMEILlkakskaeEDSRSTSEKsKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEED 1822
Cdd:COG4717 442 EELEEELEELREELAELEAELEQL--------EEDGELAEL-LQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1778-2577 |
2.47e-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: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1778 RSTSEKSKQMLEVEASKLRELAeeaarlravseeakrqRQLAEEDATRQRAEAERILKeklTAINEATRMRT-EAEIALK 1856
Cdd:pfam12128 145 RSIIQNDRTLLGRERVELRSLA----------------RQFALCDSESPLRHIDKIAK---AMHSKEGKFRDvKSMIVAI 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1857 EKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSEnelERQKTIVDETLKHRRVIEEEIRILKINFEKA 1936
Cdd:pfam12128 206 LEDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFN---TLESAELRLSHLHFGYKSDETLIASRQEERQ 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1937 SvGKSDLELELQKL----KNIADETQKSKEKAEQD-AEKQRQLALVEEARRKEAEEKVKKIiAAEQEAGRQRKVALEEVE 2011
Cdd:pfam12128 283 E-TSAELNQLLRTLddqwKEKRDELNGELSAADAAvAKDRSELEALEDQHGAFLDADIETA-AADQEQLPSWQSELENLE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2012 RlKIKADEAKKQKDLAEKEAEKQI---QLAQDAARLKiDAEEKAYYAAVQQKEQEMLQTRIQEQSiydkLKEEAEKAKRA 2088
Cdd:pfam12128 361 E-RLKALTGKHQDVTAKYNRRRSKikeQNNRDIAGIK-DKLAKIREARDRQLAVAEDDLQALESE----LREQLEAGKLE 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2089 AEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAEleaakrgQAEQAALKLKQMADAEMEK 2168
Cdd:pfam12128 435 FNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVE-------RLQSELRQARKRRDQASEA 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2169 HKQFAektvRQKEQVEGELTKVKLQLEETDH--------QKAILDDELGRLKEevTESLRQKKLVEEELFKVKIQMEELV 2240
Cdd:pfam12128 508 LRQAS----RRLEERQSALDELELQLFPQAGtllhflrkEAPDWEQSIGKVIS--PELLHRTDLDPEVWDGSVGGELNLY 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2241 KLKLRIEQ-------------ENKMLILKGKDNTQQFLAEEAEK-MKQVAEEAARLSVEAQEAARLRKIAEDDL------ 2300
Cdd:pfam12128 582 GVKLDLKRidvpewaaseeelRERLDKAEEALQSAREKQAAAEEqLVQANGELEKASREETFARTALKNARLDLrrlfde 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2301 --NEQRALAEKILKEKMQAVQEASRLKAEAEML-QKQKEMAMEQAKKLQEDKEQMQQQLaeetegfqKTLEAERRRQLD- 2376
Cdd:pfam12128 662 kqSEKDKKNKALAERKDSANERLNSLEAQLKQLdKKHQAWLEEQKEQKREARTEKQAYW--------QVVEGALDAQLAl 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2377 ----ISAEAERLKLQV----VEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVV-------HTLEIQRQHSD 2441
Cdd:pfam12128 734 lkaaIAARRSGAKAELkaleTWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLryfdwyqETWLQRRPRLA 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2442 KEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQLRQETQTLQSTFLTEKQILIQKEKYIEEEkAKLEKLFDN 2521
Cdd:pfam12128 814 TQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQ-AQGSIGERL 892
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1072265250 2522 EVGkaQKLKSEKERQLAQLEEEKRLLQTSMDDAMKKQLDaEDRIRQKQEELQQLDK 2577
Cdd:pfam12128 893 AQL--EDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLA-ETWESLREEDHYQNDK 945
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1475-2453 |
2.99e-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: 70.37 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1475 RALRARAEEAERQKKLAqEEAERLrKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEdlekfrlQAEEAERRmkQA 1554
Cdd:COG3096 286 RALELRRELFGARRQLA-EEQYRL-VEMARELEELSARESDLEQDYQAASDHLNLVQTALR-------QQEKIERY--QE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1555 ELEkerqikqahdvaqqSADAELQSKRMSFLEKTTQLEMSLKQEHITvthlQEEAERLKKQQLEAETAKEEAEKELEKWR 1634
Cdd:COG3096 355 DLE--------------ELTERLEEQEEVVEEAAEQLAEAEARLEAA----EEEVDSLKSQLADYQQALDVQQTRAIQYQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1635 QkANEALRlrlQAEEIAHKKTLAQEEAEKQKEDAeretrkrtKAEESALRQKDLaeeELEKQRKLAEETASHKLSAEQEL 1714
Cdd:COG3096 417 Q-AVQALE---KARALCGLPDLTPENAEDYLAAF--------RAKEQQATEEVL---ELEQKLSVADAARRQFEKAYELV 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1715 IRLKAEVDSGEQHRIVLEedLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEK--SKQMLEVEA 1792
Cdd:COG3096 482 CKIAGEVERSQAWQTARE--LLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQldAAEELEELL 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1793 SKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDE 1872
Cdd:COG3096 560 AELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1873 AyQRKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKTIVD----ETLKHrrvIEEEIRILKINFEKASVGKS------- 1941
Cdd:COG3096 640 R-EATVERDELAARKQALESQIERLSQPGGAEDPRLLALAErlggVLLSE---IYDDVTLEDAPYFSALYGPArhaivvp 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1942 DLELELQKLKNIADETQ---------KSKEKAEQDAEKQRQLALVeearrkeaeekvkkiiaaeQEAGRQRKVA-LEEVE 2011
Cdd:COG3096 716 DLSAVKEQLAGLEDCPEdlyliegdpDSFDDSVFDAEELEDAVVV-------------------KLSDRQWRYSrFPEVP 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2012 RLKIKADEAKKQKDLAEKEAEkqiqlaqdaarlkidAEEKAYYAAVQQKEQEMLQTRiqEQSIYDKL--------KEEAE 2083
Cdd:COG3096 777 LFGRAAREKRLEELRAERDEL---------------AEQYAKASFDVQKLQRLHQAF--SQFVGGHLavafapdpEAELA 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2084 KAKRAAEEAERAKikAEHEAALS--RQQAEEA-ERLKQKAEIEAQAKGQAQEDAEKVRKEAEleaAKRGQAEQAALKLKQ 2160
Cdd:COG3096 840 ALRQRRSELEREL--AQHRAQEQqlRQQLDQLkEQLQLLNKLLPQANLLADETLADRLEELR---EELDAAQEAQAFIQQ 914
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2161 MADA--EMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAIL------------DDELGRLKE--EVTESLRQK-K 2223
Cdd:COG3096 915 HGKAlaQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALsevvqrrphfsyEDAVGLLGEnsDLNEKLRARlE 994
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2224 LVEEELFKVKIQMEELVKlklRIEQENKMLI-LKGK-DNTQQFLAEEAEKMKQVAeeaARLSVEAQEAARLRKiaeDDLN 2301
Cdd:COG3096 995 QAEEARREAREQLRQAQA---QYSQYNQVLAsLKSSrDAKQQTLQELEQELEELG---VQADAEAEERARIRR---DELH 1065
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2302 EQralaekilkekmqavqeASRLKAEAEMLQKQKEMameqakkLQEDKEQMQQQLAEETEGFQktleAERRrqldisaea 2381
Cdd:COG3096 1066 EE-----------------LSQNRSRRSQLEKQLTR-------CEAEMDSLQKRLRKAERDYK----QERE--------- 1108
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 2382 erlklQVVemsksQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKmtvvhtlEIQRQHSDKEAEELRKAIAD 2453
Cdd:COG3096 1109 -----QVV-----QAKAGWCAVLRLARDNDVERRLHRRELAYLSA-------DELRSMSDKALGALRLAVAD 1163
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1223-2133 |
3.48e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 70.08 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1223 TEAKKRQEKIQNVPITDSKTVKEQLMEEkklleeseknrgkvdecqKYAKQYIEAIKDFEVQLVTYKAQVEPVVSPLKKP 1302
Cdd:TIGR00606 182 TRYIKALETLRQVRQTQGQKVQEHQMEL------------------KYLKQYKEKACEIRDQITSKEAQLESSREIVKSY 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1303 KVHSAS-DNIIQEYVELRTKYSELTTLTSQYIKFITETLRRLEEEERTAEK--------LKEQER----------KKLAE 1363
Cdd:TIGR00606 244 ENELDPlKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvfqgtdeqLNDLYHnhqrtvrekeRELVD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1364 VEDQLEKQRQLAEAHAQAKavAEKEALELRMNMQEEVTRREVVAVDAEQQKKTIQQELHQMKNN--SETEIKAKVKL-IE 1440
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEK--TELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpfSERQIKNFHTLvIE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1441 EAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALrarAEEAERQKKLAQEEAERLrKQVKDEAQKKREAEDELHRKV 1520
Cdd:TIGR00606 402 RQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGL---GRTIELKKEILEKKQEEL-KFVIKELQQLEGSSDRILELD 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1521 QAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEKERQiKQAHDVAQQSADAELQSKRMSFLEKTTQLEMSLKQehI 1600
Cdd:TIGR00606 478 QELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLR-KLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRK--I 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1601 TVTHLQEEAERL----KKQQLEAETAKEEAEKELEKWRQKaneALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRT 1676
Cdd:TIGR00606 555 KSRHSDELTSLLgyfpNKKQLEDWLHSKSKEINQTRDRLA---KLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDV 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1677 KAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAE-------VDSGEQHRIVLEEDLFRLKNEVNEAIQRR 1749
Cdd:TIGR00606 632 CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDKL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1750 RGLEEELAKVRAEMEILLkakSKAEEDSRSTSEKSKQMLEVEaSKLRELAEEAARLRAVSEEAKRQRQ--LAEEDATR-- 1825
Cdd:TIGR00606 712 KSTESELKKKEKRRDEML---GLAPGRQSIIDLKEKEIPELR-NKLQKVNRDIQRLKNDIEEQETLLGtiMPEEESAKvc 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1826 ------------QRAEAERILKEKLTAINEATRMRTEAEIAlKEKEAENERLRRLAEDEAYQRKLLEEQaaqhkqdieEK 1893
Cdd:TIGR00606 788 ltdvtimerfqmELKDVERKIAQQAAKLQGSDLDRTVQQVN-QEKQEKQHELDTVVSKIELNRKLIQDQ---------QE 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1894 IHQLKQSSENELERQKTIVDETLKHRRVIEE-------EIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQ 1966
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEqlvelstEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1967 DAEKQRQLALVEEARRKEAEEKVKKIIAAEQEagRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQ---------- 2036
Cdd:TIGR00606 938 KAQDKVNDIKEKVKNIHGYMKDIENKIQDGKD--DYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQdidtqkiqer 1015
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2037 -LAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQ-SIYDKLKEEAEkakraaeeaeraKIKAEHEAALSRQQAEEAE 2114
Cdd:TIGR00606 1016 wLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMkQEHQKLEENID------------LIKRNHVLALGRQKGYEKE 1083
|
970
....*....|....*....
gi 1072265250 2115 RLKQKAEIEAQAKGQAQED 2133
Cdd:TIGR00606 1084 IKHFKKELREPQFRDAEEK 1102
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1191-1801 |
3.59e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1191 VLQIEVRQRELEQLGKQLRYYRESYEWLIRWIteakKRQEKIQNVPITDSKTVKEQLMEEKKLLEESEKNRGKVDECQKY 1270
Cdd:PRK03918 154 ILGLDDYENAYKNLGEVIKEIKRRIERLEKFI----KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1271 AKQYiEAIKDFEVQLVTYKAQVEPVVSPL--KKPKVHSASDNIIQEYVELRTKYSELTTLTSQYIKFITEtlrrleeeer 1348
Cdd:PRK03918 230 VKEL-EELKEEIEELEKELESLEGSKRKLeeKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKL---------- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1349 taEKLKEQERKKLAEVEDQLEKQRQLAeahaqakavaekEALELRMNMQEEVTRRevvAVDAEQQKKTIQQELHQMKNNS 1428
Cdd:PRK03918 299 --SEFYEEYLDELREIEKRLSRLEEEI------------NGIEERIKELEEKEER---LEELKKKLKELEKRLEELEERH 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1429 ETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQK 1508
Cdd:PRK03918 362 ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVC 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1509 KREAEDE----LHRKVQAE-KDAAREKQKALEDLEKFRLQAEEAERrmkqaELEKERQIKQAHDVAQQ--SADAELQSKR 1581
Cdd:PRK03918 442 GRELTEEhrkeLLEEYTAElKRIEKELKEIEEKERKLRKELRELEK-----VLKKESELIKLKELAEQlkELEEKLKKYN 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1582 MSFLEKTTQLEMSLKQEHITVT-HLQEEAERLKKQQLEAETAKEEAEKELEKWRQKAN-------------EALRLRLQA 1647
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKLKgEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEllkeleelgfesvEELEERLKE 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1648 EEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASH------------KLSAEQELI 1715
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeyeelreeYLELSRELA 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1716 RLKAEVDSGEQHRIVLEEDLFRLKNEVneaiqrrrgleEELAKVRAEMEILLKAKSKAEEdSRSTSEKSKQMLEVEA-SK 1794
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEEL-----------EEREKAKKELEKLEKALERVEE-LREKVKKYKALLKERAlSK 744
|
....*..
gi 1072265250 1795 LRELAEE 1801
Cdd:PRK03918 745 VGEIASE 751
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1892-2578 |
4.00e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 69.75 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1892 EKIHQLKQSSENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVgksDLELELQKLKNIADETQKS-------KEKA 1964
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSL---KLEEEIQENKDLIKENNATrhlcnllKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1965 EQDAEKQRQLALveearrkeaeekvkkiiaaEQEAGRQRKVALEE-VERLKIKADEAKKQKDLAEkeAEKQIQLAQDAAr 2043
Cdd:pfam05483 165 ARSAEKTKKYEY-------------------EREETRQVYMDLNNnIEKMILAFEELRVQAENAR--LEMHFKLKEDHE- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2044 lKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIYDKLKEEAekakraaeeaerakikaeheaALSRQQAEEAERLKQKAEIE 2123
Cdd:pfam05483 223 -KIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLT---------------------FLLEESRDKANQLEEKTKLQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2124 AQAKGQAQEDAEKVRKEAE--LEAAKRGQAEQAALklkqmadaemEKHKQFAEKTVRQ----KEQVEGELTKVK----LQ 2193
Cdd:pfam05483 281 DENLKELIEKKDHLTKELEdiKMSLQRSMSTQKAL----------EEDLQIATKTICQlteeKEAQMEELNKAKaahsFV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2194 LEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELFKVKIQMEELVKLKLRIEQEnkMLILKGKDNTQQFLAEEAEKMK 2273
Cdd:pfam05483 351 VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVE--LEELKKILAEDEKLLDEKKQFE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2274 QVAEEaarLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQ-KQKEMAMEQAKKLQEDKEqm 2352
Cdd:pfam05483 429 KIAEE---LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHCDKLLLENKE-- 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2353 qqqLAEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAEED----AKKFRKQAEDISEKLHQTELSTKEKMT 2428
Cdd:pfam05483 504 ---LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDElesvREEFIQKGDEVKCKLDKSEENARSIEY 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2429 VVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSeemqkaqkeqlrqetqTLQSTFLTEKQILIQK-EKY 2507
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKG----------------SAENKQLNAYEIKVNKlELE 644
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072265250 2508 IEEEKAKLEKLFDNEVGKAQKLKSEKERQLAQLEEEKrllqTSMDDAMKKQLDAEDRIRQKQEELQQLDKK 2578
Cdd:pfam05483 645 LASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK----AIADEAVKLQKEIDKRCQHKIAEMVALMEK 711
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1422-1793 |
4.17e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 69.38 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1422 HQmKNNSETEIKAKVKLIEEaEYNRKKVEEEIRII--RIQLETSQKQKSGAEDELRALRARAE----EAERQ-KKLAQEE 1494
Cdd:pfam17380 280 HQ-KAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQErmamERERElERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1495 AERLRKQVKD-----EAQKKREAEdelhrKVQAEKDAAREK-QKALEDLEKFRLQAEEAERRMKQAELEKErQIKQAHDV 1568
Cdd:pfam17380 358 RKRELERIRQeeiamEISRMRELE-----RLQMERQQKNERvRQELEAARKVKILEEERQRKIQQQKVEME-QIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1569 AQQSADAELQSKRMSFLEKTTQlemslkqehitvthlqEEAERlkKQQLeaetakeeaekelEKWRQKanealrlrlqae 1648
Cdd:pfam17380 432 ARQREVRRLEEERAREMERVRL----------------EEQER--QQQV-------------ERLRQQ------------ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1649 eiahkktlaQEEAEKQKEDAERETRKRTKAEEsaLRQKDLAEEELEKQRKLAEETASHKLsAEQELIRLKAEVDSGEQHR 1728
Cdd:pfam17380 469 ---------EEERKRKKLELEKEKRDRKRAEE--QRRKILEKELEERKQAMIEEERKRKL-LEKEMEERQKAIYEEERRR 536
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072265250 1729 IVLEEDlfRLKNEVNEaiqrRRGLEEELAKVRAEMEiLLKAKSKAEEDSRSTSEKSKQMLEVEAS 1793
Cdd:pfam17380 537 EAEEER--RKQQEMEE----RRRIQEQMRKATEERS-RLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
617-795 |
4.25e-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: 65.54 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 617 LNTFVAAATKELMWLNDKEEEEVNFDWSDRNTNMTSKKDNYSGLMRELELKEKKIKEIQNTGDRLLRDDHPGKSTIEAFQ 696
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 697 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFADVKDTEDHLKKINDTMRRKYICDrsiTVTRLEDLLQDSVDEKEQLTEY 776
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170
....*....|....*....
gi 1072265250 777 KGQVAGLAKRAKTIIQLKP 795
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH 177
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
1940-2369 |
5.64e-11 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 68.87 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1940 KSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLALVEEARRKEAEEKVkkIIAAEQEAGRQRKVALEEVERLKIKADE 2019
Cdd:COG5281 19 ASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAA--AAAAAAAAADALAAALAEDAAAAAAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2020 AKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKA 2099
Cdd:COG5281 97 AALAALAAAALALAAAALAEAALAAAAAAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAALAAAAAAAAAAAAAAAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2100 EHEAALSRqqAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMADAEMEKHKQFAEKTVRQ 2179
Cdd:COG5281 177 AALAAASA--AAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAASAAAQALAALAAAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2180 KEQVEGELTKVKLQLeetdhqkailddelgrlkeevteslrqkklvEEELFKVKIQMEELVKLKLRIEQENKMLILKGKD 2259
Cdd:COG5281 255 AAAALALAAAAELAL-------------------------------TAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2260 NTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAM 2339
Cdd:COG5281 304 AAAAAAAAQLAAAAAAAAQALRAAAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWAA 383
|
410 420 430
....*....|....*....|....*....|
gi 1072265250 2340 EQAKKLQEDKEQMQQQLAEETEGFQKTLEA 2369
Cdd:COG5281 384 GAKAALAEYADSATNVAAQVAQAATSAFSG 413
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1786-2620 |
6.03e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.33 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1786 QMLEVEASKLRELAEEAArlrAVSE-EAKRQRQLAEEDATRQR-AEAERILKEKLTAINEATRMRTEAE--IALKEKEAE 1861
Cdd:TIGR02169 146 DFISMSPVERRKIIDEIA---GVAEfDRKKEKALEELEEVEENiERLDLIIDEKRQQLERLRREREKAEryQALLKEKRE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1862 NERLRRLAEDEAY--QRKLLEEQAA---QHKQDIEEKIHQLKQSSEnelERQKTIVDETLKHRRVIEEEIRILKINFEka 1936
Cdd:TIGR02169 223 YEGYELLKEKEALerQKEAIERQLAsleEELEKLTEEISELEKRLE---EIEQLLEELNKKIKDLGEEEQLRVKEKIG-- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1937 svgksDLELELQKLKNIADEtqksKEKAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQeagrqrkvaleeVERLKIK 2016
Cdd:TIGR02169 298 -----ELEAEIASLERSIAE----KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER------------KRRDKLT 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2017 ADEAKKQKDLAEKEAEKQiQLAQDAARLKidAEEKAYyaavqQKEQEMLQTRIQE-QSIYDKLKEEAEKAkraaeEAERA 2095
Cdd:TIGR02169 357 EEYAELKEELEDLRAELE-EVDKEFAETR--DELKDY-----REKLEKLKREINElKRELDRLQEELQRL-----SEELA 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2096 KIKAEHEAALSRQQAEEAERLKQKAEIEAQAKG--QAQEDAEKVRKEAELEAAKRGQAEQAaLKLKQMADAEMEKHKQFA 2173
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKleQLAADLSKYEQELYDLKEEYDRVEKE-LSKLQRELAEAEAQARAS 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2174 EKTVRQKEQVE--------------GELTKVKLQleetdHQKAILDDELGRLKEEVTESLRQKKLVEEELFKVKIQMEEL 2239
Cdd:TIGR02169 503 EERVRGGRAVEevlkasiqgvhgtvAQLGSVGER-----YATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATF 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2240 VKLKlRIEQENKMLILKGKDNTQQF---LAEEAEKMKQVAEEAAR--LSVEAQEAARlrkiaeDDLNEQRALA-EKILKE 2313
Cdd:TIGR02169 578 LPLN-KMRDERRDLSILSEDGVIGFavdLVEFDPKYEPAFKYVFGdtLVVEDIEAAR------RLMGKYRMVTlEGELFE 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2314 KMQAVQEASRLKAEAEMLQKQKEmamEQAKKLQEDKEQMQQQLaeetEGFQKTLEAERRRQLDISAEAERLKLQVVEMSK 2393
Cdd:TIGR02169 651 KSGAMTGGSRAPRGGILFSRSEP---AELQRLRERLEGLKREL----SSLQSELRRIENRLDELSQELSDASRKIGEIEK 723
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2394 SQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKeaellQKKSE 2473
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI-----PEIQA 798
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2474 EMQKAQKEQLRQETQtlqstfltekqiliqkekyIEEEKAKLEKLfDNEVGKAQKLKSEKERQLAQLEEEKRLLQtsmdd 2553
Cdd:TIGR02169 799 ELSKLEEEVSRIEAR-------------------LREIEQKLNRL-TLEKEYLEKEIQELQEQRIDLKEQIKSIE----- 853
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 2554 amkkqlDAEDRIRQKQEELQQLDKKRQEQERLLEEENRKLRERLEQLEQEHRIALEKTREVIITKET 2620
Cdd:TIGR02169 854 ------KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2731-2769 |
6.46e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.65 E-value: 6.46e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1072265250 2731 LLEAQAASGFITDPVGNKRLTVSEAVKENVIGPEVHNKL 2769
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1766-2411 |
6.48e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 68.98 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1766 LLKAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLR----------AVSEEAKRQRQLAEEDATRQRAEAERILK 1835
Cdd:pfam05483 114 IIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnllketcARSAEKTKKYEYEREETRQVYMDLNNNIE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1836 EKLTAINE----ATRMRTEAEIALKEKEAE----NERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSE--NEL 1905
Cdd:pfam05483 194 KMILAFEElrvqAENARLEMHFKLKEDHEKiqhlEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDkaNQL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1906 ERQKTIVDETLKH----RRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLALVEEAR 1981
Cdd:pfam05483 274 EEKTKLQDENLKEliekKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1982 RKEAEEKVKKIIAAEQEA----GRQRKVALEEVERLKIKADEAKKQKDLAEKEAEK-QIQLAQDAARLKIDAEEKAYYAA 2056
Cdd:pfam05483 354 FEATTCSLEELLRTEQQRleknEDQLKIITMELQKKSSELEEMTKFKNNKEVELEElKKILAEDEKLLDEKKQFEKIAEE 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2057 VQQKEQEM---LQTRIQE------QSIYDKLKEE--AEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQ 2125
Cdd:pfam05483 434 LKGKEQELiflLQAREKEihdleiQLTAIKTSEEhyLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTL 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2126 AKGQAQEDAEKVRKeaeleaakrgQAEQAALKLKQMADAEMEKHKQFaeKTVRQKEQVEGELTKVKLQLEETDHQKaild 2205
Cdd:pfam05483 514 ELKKHQEDIINCKK----------QEERMLKQIENLEEKEMNLRDEL--ESVREEFIQKGDEVKCKLDKSEENARS---- 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2206 delgrLKEEVTESLRQKKLVEEELFKVKIQMEELVKLKLRIEQENKMLILKGKDNTQQFLAEEAEKMKQVAE-EAARLSV 2284
Cdd:pfam05483 578 -----IEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELElASAKQKF 652
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2285 EAQEAARLRKIAEDDLNEQRALAEkiLKEKMQAVQEASRLKAEAEMLQKQKEMAMeqaKKLQEDKEQMQQQLAEETE--- 2361
Cdd:pfam05483 653 EEIIDNYQKEIEDKKISEEKLLEE--VEKAKAIADEAVKLQKEIDKRCQHKIAEM---VALMEKHKHQYDKIIEERDsel 727
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1072265250 2362 GFQKTLEAERRR-QLDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAED 2411
Cdd:pfam05483 728 GLYKNKEQEQSSaKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1350-1908 |
7.25e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1350 AEKLKEQeRKKLAEVEDQLEKQRQLAEAHAQAKAVAEK-EALELRMNMQEEVtRREVVAVDAEQQKKTIQQELHQmknnS 1428
Cdd:COG4913 227 ADALVEH-FDDLERAHEALEDAREQIELLEPIRELAERyAAARERLAELEYL-RAALRLWFAQRRLELLEAELEE----L 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1429 ETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLetsqkQKSGAeDELRALRARAEEAERQKKLAQEEAERLRKQVKD---E 1505
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQI-----RGNGG-DRLEQLEREIERLERELEERERRRARLEALLAAlglP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1506 AQKKREAEDELHRKVQAEKDAAREKQKALEDlEKFRLQAEEAERRMKQAELEKERQIKQAHDVaqqSADAELQSKRMSFL 1585
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEE-ALAEAEAALRDLRRELRELEAEIASLERRKS---NIPARLLALRDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1586 EKTTQLEMSLK--QEHITVthlQEEAERlkkqqleaetakeeaekelekWRQKANEAL---RLRLQAEEIAHKKTLAQEE 1660
Cdd:COG4913 451 EALGLDEAELPfvGELIEV---RPEEER---------------------WRGAIERVLggfALTLLVPPEHYAAALRWVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1661 AEK-------QKEDAERETRKRTKAEESALRQK-DLAEEELEK--QRKLAEETASHKLSAEQELIRLKAEV-------DS 1723
Cdd:COG4913 507 RLHlrgrlvyERVRTGLPDPERPRLDPDSLAGKlDFKPHPFRAwlEAELGRRFDYVCVDSPEELRRHPRAItragqvkGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1724 GEQHRI---------------------VLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEIL--LKAKSKAEEDSRST 1780
Cdd:COG4913 587 GTRHEKddrrrirsryvlgfdnraklaALEAELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1781 ----SEKSKQMLEVEAS--KLRELAEEAARLRAVSEEAKRQRQLAEEDATR---QRAEAERILKEKLTAINEATRMRTEA 1851
Cdd:COG4913 667 ereiAELEAELERLDASsdDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEELDELQDRLEAAEDLARLE 746
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 1852 EIALKEkeaenERLRRLAEDEAYQRklLEEQAAQHKQDIEEKIHQLkqssENELERQ 1908
Cdd:COG4913 747 LRALLE-----ERFAAALGDAVERE--LRENLEERIDALRARLNRA----EEELERA 792
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2023-2195 |
7.59e-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: 67.18 E-value: 7.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2023 QKDLAEKEAEKQIQLAQDAARlkidAEEKAYYAAVQQKEQeMLQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEhe 2102
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPAAK----KEQERQKKLEQQAEE-AEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEE-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2103 aalSRQQAEEAerlKQKAEIEAQAKGQA---QEDAEKVRKEAELEAAKRGQAE--QAALKLKQMADAEMEKHKQFAEKTV 2177
Cdd:TIGR02794 117 ---KQKQAEEA---KAKQAAEAKAKAEAeaeRKAKEEAAKQAEEEAKAKAAAEakKKAEEAKKKAEAEAKAKAEAEAKAK 190
|
170
....*....|....*...
gi 1072265250 2178 RQKEQVEGELTKVKLQLE 2195
Cdd:TIGR02794 191 AEEAKAKAEAAKAKAAAE 208
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1474-2020 |
8.50e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.53 E-value: 8.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1474 LRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEdeLHRKVQAEKDAAREKQKALEDLEKFRLQAEEAeRRMKQ 1553
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKD--LHERLNGLESELAELDEEIERYEEQREQARET-RDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1554 AELEKERQIKQAHDVAQQSADAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKw 1633
Cdd:PRK02224 241 EVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1634 rQKANEALRLRLqaEEIAHKKTLAQEEAEKQKEDAER-ETRKRTKAEESALRQKDL--AEEELEKQRKLAEETASHKLSA 1710
Cdd:PRK02224 320 -EDRDEELRDRL--EECRVAAQAHNEEAESLREDADDlEERAEELREEAAELESELeeAREAVEDRREEIEELEEEIEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1711 EQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRA--------EMEILLKAKSKAE--EDSRST 1780
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpECGQPVEGSPHVEtiEEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1781 SEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAE--EDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEK 1858
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1859 EAENERLRRLAEDEAYQRKLLEEQAAQHKQDIE---------EKIHQLKQSSENELERQKTIVD------ETLKHRRvie 1923
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAElnderrERLAEKR--- 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1924 EEIRILKINFEKASV--GKSDLELELQKLKNIADETQkskEKAEQDAEKQRQLALVEEARrkeaeekvkkiiaAEQEAGR 2001
Cdd:PRK02224 634 ERKRELEAEFDEARIeeAREDKERAEEYLEQVEEKLD---ELREERDDLQAEIGAVENEL-------------EELEELR 697
|
570 580
....*....|....*....|
gi 1072265250 2002 QRKVALEE-VERLKIKADEA 2020
Cdd:PRK02224 698 ERREALENrVEALEALYDEA 717
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1744-2113 |
1.07e-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: 68.23 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1744 EAIQRRR---GLEEELAKVRAEMEILLKAKSKAEED-----------SRSTSEKSKQ--MLEVEASKLRELAEEAARlra 1807
Cdd:pfam17380 234 EKMERRKesfNLAEDVTTMTPEYTVRYNGQTMTENEflnqllhivqhQKAVSERQQQekFEKMEQERLRQEKEEKAR--- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1808 vseEAKRQRQLAEEDATRQrAEAERilKEKLTAINEATRMRTEAE---IALKEKEAENERLRR--LAEDEAYQRKLleEQ 1882
Cdd:pfam17380 311 ---EVERRRKLEEAEKARQ-AEMDR--QAAIYAEQERMAMERERElerIRQEERKRELERIRQeeIAMEISRMREL--ER 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1883 AAQHKQDIEEKIHQlkqssENELERQKTIVDETlKHRRVIEEEIRILKINFEKASVGKSDL-------ELELQKLKNIAD 1955
Cdd:pfam17380 383 LQMERQQKNERVRQ-----ELEAARKVKILEEE-RQRKIQQQKVEMEQIRAEQEEARQREVrrleeerAREMERVRLEEQ 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1956 ETQKSKEKAEQDAEKQRQlalveearrkEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQI 2035
Cdd:pfam17380 457 ERQQQVERLRQQEEERKR----------KKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072265250 2036 QLAQDAARLKIDAEEKayyaavqQKEQEMLQ-TRIQEQsiydKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEA 2113
Cdd:pfam17380 527 KAIYEEERRREAEEER-------RKQQEMEErRRIQEQ----MRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1650-2036 |
1.96e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 67.46 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1650 IAHKKTLAQEEAEKQKEDAEREtRKRTKAEESAlrqkdlaeEELEKQRKLAEETashklSAEQELIRLKAEVdSGEQHRI 1729
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQE-RLRQEKEEKA--------REVERRRKLEEAE-----KARQAEMDRQAAI-YAEQERM 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1730 VLEEdlfrlknevneaiqrrrglEEELAKVRAEmeillkakskaeEDSRSTSEKSKQMLEVEASKLREL-------AEEA 1802
Cdd:pfam17380 343 AMER-------------------ERELERIRQE------------ERKRELERIRQEEIAMEISRMRELerlqmerQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1803 ARLRAVSEEAKRQRQLAEEdatRQRAEAERilkekltaineatrMRTEAEIALKEKEAENERLRRLAEDEA--YQRKLLE 1880
Cdd:pfam17380 392 ERVRQELEAARKVKILEEE---RQRKIQQQ--------------KVEMEQIRAEQEEARQREVRRLEEERAreMERVRLE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1881 EQAAQHKqdieekIHQLKQSsENELERQKTIVDETLKHRRVIEEEIRILkinfekasvgksdLELELQKLKNIADETQKS 1960
Cdd:pfam17380 455 EQERQQQ------VERLRQQ-EEERKRKKLELEKEKRDRKRAEEQRRKI-------------LEKELEERKQAMIEEERK 514
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072265250 1961 KEKAEQDAEkQRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQ 2036
Cdd:pfam17380 515 RKLLEKEME-ERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1353-1893 |
2.18e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.44 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1353 LKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQQKKTIQQELHQMKNNSETEI 1432
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1433 KAKVK---LIEEAEYNRKKVEEEIRiiriqleTSQKQKSGAEDELRALraraeEAERQKKLAQ-EEAERLR--KQVKDEA 1506
Cdd:pfam05483 342 KAKAAhsfVVTEFEATTCSLEELLR-------TEQQRLEKNEDQLKII-----TMELQKKSSElEEMTKFKnnKEVELEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1507 QKKREAEDE--LHRKVQAEKDAarEKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQSKRMSF 1584
Cdd:pfam05483 410 LKKILAEDEklLDEKKQFEKIA--EELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKN 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1585 LEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQ 1664
Cdd:pfam05483 488 IELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1665 KEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEdlfrlknEVNE 1744
Cdd:pfam05483 568 LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEI-------KVNK 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1745 aiqrrrgLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKskqmLEVEASKLRELAEEAARLRavSEEAKR-QRQLAEEDA 1823
Cdd:pfam05483 641 -------LELELASAKQKFEEIIDNYQKEIEDKKISEEK----LLEEVEKAKAIADEAVKLQ--KEIDKRcQHKIAEMVA 707
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072265250 1824 --TRQRAEAERILKEKLTAI-------NEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEK 1893
Cdd:pfam05483 708 lmEKHKHQYDKIIEERDSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2006-2624 |
2.18e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2006 ALEEVER----LKIKADEAKKQKDLaeKEAEKQIQLAQDAARLKidaEEKAYYAAVQQKEQEMLQTRIQEQSIYDKLKEE 2081
Cdd:TIGR02168 194 ILNELERqlksLERQAEKAERYKEL--KAELRELELALLVLRLE---ELREELEELQEELKEAEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2082 AEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERlkqkaEIEAQAKGQAQEDAEKVRKEAELEAAKRgQAEQAALKLKQM 2161
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELYALANEISRLEQ-----QKQILRERLANLERQLEELEAQLEELES-KLDELAEELAEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2162 AdaemekhKQFAEKTVrQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELFKVKIQMEELVK 2241
Cdd:TIGR02168 343 E-------EKLEELKE-ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2242 LKLRIEQENKMLILKGKDNTQQFLAEEAEKMKQVAEEAArlsvEAQEAARLRKIAEDdlnEQRALAEKILKEKMQAVQEA 2321
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ----EELERLEEALEELR---EELEEAEQALDAAERELAQL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2322 SRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQ------QLAEETEGFQKTLEAerrrqldisAEAERLKLQVVEMSKSQ 2395
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGVKALLKNQSGLSGilgvlsELISVDEGYEAAIEA---------ALGGRLQAVVVENLNAA 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2396 AKAEEdakkFRKQAEdiSEKLHQTELSTKE--KMTVVHTLEIQRQHS--------DKEAEELRKAIADLENEKEKlkkea 2465
Cdd:TIGR02168 559 KKAIA----FLKQNE--LGRVTFLPLDSIKgtEIQGNDREILKNIEGflgvakdlVKFDPKLRKALSYLLGGVLV----- 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2466 ellqkkSEEMQKAQkEQLRQETQ-----TLQSTFLT-----------EKQILIQKEKYIEEEKAKLEKLFDNEvgkaqkl 2529
Cdd:TIGR02168 628 ------VDDLDNAL-ELAKKLRPgyrivTLDGDLVRpggvitggsakTNSSILERRREIEELEEKIEELEEKI------- 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2530 kSEKERQLAQLEEEKRLLQTSMDDAMKKQLDAEDRIRQKQEELQQLDKKRQEQERLLEEENRkLRERLEQLEQEHRIALE 2609
Cdd:TIGR02168 694 -AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK-ELTELEAEIEELEERLE 771
|
650
....*....|....*
gi 1072265250 2610 KTREVIITKETVITQ 2624
Cdd:TIGR02168 772 EAEEELAEAEAEIEE 786
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1753-2520 |
2.33e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.45 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1753 EEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQ------ 1826
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQlqntvh 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1827 RAEAERILKEKL-----TAINEATRMRTEAEIALKE--------KEAENERL-----------RRLAEDEAYQRKLLEEQ 1882
Cdd:pfam15921 153 ELEAAKCLKEDMledsnTQIEQLRKMMLSHEGVLQEirsilvdfEEASGKKIyehdsmstmhfRSLGSAISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1883 AAQHKQDI---EEKIHQLKQSSENELE---RQKTIVDETLkhrrVIEEEIRILKINfEKASVGKSdlelelqKLKNIADE 1956
Cdd:pfam15921 233 ISYLKGRIfpvEDQLEALKSESQNKIElllQQHQDRIEQL----ISEHEVEITGLT-EKASSARS-------QANSIQSQ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1957 TQKSKEKAE-QDAEKQRQLAlveearrkEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEakkqkDLAEKEAEKQi 2035
Cdd:pfam15921 301 LEIIQEQARnQNSMYMRQLS--------DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANS-----ELTEARTERD- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2036 QLAQDAARLkiDAEEKAYYAAVQQKEQEMLQTRIQEQSIYDK----------LKEEAEKAKRAAE--EAERAKIKAEHEA 2103
Cdd:pfam15921 367 QFSQESGNL--DDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitidhLRRELDDRNMEVQrlEALLKAMKSECQG 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2104 ALSRQQAE---EAERLKQKAEIEAQAkgqaQEDAEKVRKEAELEAAKRGQAEQAALKLKQMADAEMEKHkqfaektvRQK 2180
Cdd:pfam15921 445 QMERQMAAiqgKNESLEKVSSLTAQL----ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE--------RAI 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2181 EQVEGELTK----VKLQLEETDHqkailddelgrLKEEvTESLRQkklVEEELFKVKIQMEELVKLK--LRIEQENKMLI 2254
Cdd:pfam15921 513 EATNAEITKlrsrVDLKLQELQH-----------LKNE-GDHLRN---VQTECEALKLQMAEKDKVIeiLRQQIENMTQL 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2255 LKGKDNTQ-QFLAEEAEKMKQVAEEaarlSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEAS-RLKAEAEMLQ 2332
Cdd:pfam15921 578 VGQHGRTAgAMQVEKAQLEKEINDR----RLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSeRLRAVKDIKQ 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2333 KQKEMAME------QAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKKFR 2406
Cdd:pfam15921 654 ERDQLLNEvktsrnELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2407 KQaedISEKLHQTE-LSTK-----EKMTVVHTleiQRQHSDKEAEELRKAIADLENEKEKLKKEAellqkkseEMQKAQK 2480
Cdd:pfam15921 734 KQ---ITAKRGQIDaLQSKiqfleEAMTNANK---EKHFLKEEKNKLSQELSTVATEKNKMAGEL--------EVLRSQE 799
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1072265250 2481 EQLRQETQTLQ------STFLTEKQILIQKEKYiEEEKAKLEKLFD 2520
Cdd:pfam15921 800 RRLKEKVANMEvaldkaSLQFAECQDIIQRQEQ-ESVRLKLQHTLD 844
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1472-1893 |
2.40e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1472 DELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDEL--HRKVQAEKDAAREKQKALEDLEKFRLQAEEAER 1549
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELekLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1550 RMKQ-AELEKE-RQIKQAHDVAQQSADAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLK--KQQLEAETAKEE 1625
Cdd:COG4717 154 RLEElRELEEElEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQeeLEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1626 AEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETAS 1705
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1706 HKLsAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEI---LLKAKSKAEEDSRSTSE 1782
Cdd:COG4717 314 EEL-EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAALE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1783 KSKQMLEVEA------SKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERI-LKEKLTAINEATRM---RTEAE 1852
Cdd:COG4717 393 QAEEYQELKEeleeleEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEeLREELAELEAELEQleeDGELA 472
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1072265250 1853 IALKEKEAENERLRRLAEDEAYqRKLLEEQAAQHKQDIEEK 1893
Cdd:COG4717 473 ELLQELEELKAELRELAEEWAA-LKLALELLEEAREEYREE 512
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1775-2136 |
2.90e-10 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 66.46 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1775 EDSRSTSEKSKQML------EVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINEATRMR 1848
Cdd:pfam07888 10 EEESHGEEGGTDMLlvvpraELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1849 TEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDI---EEKIHQLKQSS---ENELERQKTIVDETLKHRRVI 1922
Cdd:pfam07888 90 RQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIrelEEDIKTLTQRVlerETELERMKERAKKAGAQRKEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1923 EEEIRILKINFEKASVGKSDLELELQKLKNIADEtQKSKEKAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQE--AG 2000
Cdd:pfam07888 170 EAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQ-RDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQErlNA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2001 RQRKVALEEVERLKIKADEAKKQKDLAE---KEAEKQIQLAQDAARLKidaEEKAYYAavqQKEQEMLQTRIQEQSIYDK 2077
Cdd:pfam07888 249 SERKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQLADASLALR---EGRARWA---QERETLQQSAEADKDRIEK 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072265250 2078 LKEEAEKAKRAAEEA--ERAKIKAE--HEAALSRQQAEEAERLKQ--KAEIEAQAKGQAQEDAEK 2136
Cdd:pfam07888 323 LSAELQRLEERLQEErmEREKLEVElgREKDCNRVQLSESRRELQelKASLRVAQKEKEQLQAEK 387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1668-1898 |
3.47e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.56 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1668 AERETRKRTKAEESALRQK-DLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAI 1746
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1747 QRRRGLEEELAKV---------RAEMEILLKAKSKAEEDSRSTSEKS-KQMLEVEASKLRELAEEAARLRAVSEEAKRQR 1816
Cdd:COG4942 97 AELEAQKEELAELlralyrlgrQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1817 QLAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEdeayqrKLLEEQAAQHKQDIEEKIHQ 1896
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA------RLEAEAAAAAERTPAAGFAA 250
|
..
gi 1072265250 1897 LK 1898
Cdd:COG4942 251 LK 252
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2009-2643 |
3.54e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 66.77 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2009 EVERLKIKADEAKKqkDLAEKEAekqiqlaQDAARLKIDAEEKAYYAAVQ------QKEQEMLQTRIQEQSIydkLKEEA 2082
Cdd:NF041483 44 QVEVLRAKLHEARR--SLASRPA-------YDGADIGYQAEQLLRNAQIQadqlraDAERELRDARAQTQRI---LQEHA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2083 EKAKR-AAE---EAERAKIKAEHEAALSRQQAEE--AERLKQKAEIEAQAKGQAQEDAEKVRKEAELE-AAKRGQAEQAA 2155
Cdd:NF041483 112 EHQARlQAElhtEAVQRRQQLDQELAERRQTVEShvNENVAWAEQLRARTESQARRLLDESRAEAEQAlAAARAEAERLA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2156 LKLKQMADAEMEKHKQFAEKTV-RQKEQVEGELTKVKLQLEE-TDHqkailddelgrlkeevTESLRQKKLVEEElfKVK 2233
Cdd:NF041483 192 EEARQRLGSEAESARAEAEAILrRARKDAERLLNAASTQAQEaTDH----------------AEQLRSSTAAESD--QAR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2234 IQMEELVKlklrieqenkmlilkgkdNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALA--EKIL 2311
Cdd:NF041483 254 RQAAELSR------------------AAEQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESANEQRTRTakEEIA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2312 KEKMQAVQEASRLKAEAEmlQKQKEMAMEQAKKLQEDKEQMQQQLAEET------------EGFQKTLEAERRRQLDISA 2379
Cdd:NF041483 316 RLVGEATKEAEALKAEAE--QALADARAEAEKLVAEAAEKARTVAAEDTaaqlakaartaeEVLTKASEDAKATTRAAAE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2380 EAERLKlqvvemsksqAKAEEDAKKFRKQAEDISEKLH-QTELSTKEKMTVVHTLEIQRQHSDKEAEELRKAIADLENEK 2458
Cdd:NF041483 394 EAERIR----------REAEAEADRLRGEAADQAEQLKgAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2459 EKLKKEAELLQ-----KKSEEM---QKAQKEQLRQETQTLQSTFLTE-----KQILIQKEKYIEEEKAKLEKLFDNEVGK 2525
Cdd:NF041483 464 RGEARREAVQQieeaaRTAEELltkAKADADELRSTATAESERVRTEaieraTTLRRQAEETLERTRAEAERLRAEAEEQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2526 AQKLKSEKERQLAQLEEE-KRLLQTSMDDAmkkqldAEDRIRQKQEELQQLDKKRQEQERLLEEENRKLRERLEQLEQEH 2604
Cdd:NF041483 544 AEEVRAAAERAARELREEtERAIAARQAEA------AEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLR 617
|
650 660 670
....*....|....*....|....*....|....*....
gi 1072265250 2605 RIALEKTREVIITKETVITQTKTmpngRDAADGSAQNGE 2643
Cdd:NF041483 618 TEAAERIRTLQAQAEQEAERLRT----EAAADASAARAE 652
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2168-2558 |
4.42e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2168 KHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQkailddeLGRLKEEVTESLRQKKLvEEELFKVKIQMeelvkLKLRIE 2247
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQ-------LKSLERQAEKAERYKEL-KAELRELELAL-----LVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2248 QENKML--ILKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLK 2325
Cdd:TIGR02168 236 ELREELeeLQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2326 AEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEetegfqktleaerrrqldISAEAERLKLQVVEMSKSQAKAEEDAKKF 2405
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEE------------------LKEELESLEAELEELEAELEELESRLEEL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2406 RKQAEDISEKLHQTELSTKekmtvVHTLEIQRQHSDKEAEELRKaiadlenekeklkkeaellQKKSEEMQKAQKEQLRQ 2485
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIA-----SLNNEIERLEARLERLEDRR-------------------ERLQQEIEELLKKLEEA 433
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 2486 ETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLfDNEVGKAQKLKSEKERQLAQLEEEKRLLQTSMDDAMKKQ 2558
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEEL-REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFS 505
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
46-147 |
5.43e-10 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 59.51 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 46 KKTFTKWVNKHL-----IKHWRAEAQrHVNDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 115
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDP-DGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNA 81
|
90 100 110
....*....|....*....|....*....|..
gi 1072265250 116 LKLRQVKLVNIRNDDIADGNPKLTLGLIWTII 147
Cdd:cd21217 82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2007-2577 |
6.99e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2007 LEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKayyaaVQQKEQEMLQTRIQEQsiydKLKEEAEKAK 2086
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKE-----LEEVLREINEISSELP----ELREELEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2087 RAAEEAErakikaEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAaKRGQAEqaalKLKQMADaEM 2166
Cdd:PRK03918 228 KEVKELE------ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELK----ELKEKAE-EY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2167 EKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDD---ELGRLKEEVTESLRQKKLVEE---ELFKVKIQMEELV 2240
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEErheLYEEAKAKKEELE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2241 KLKLRIEQENKMLILKGKDNTQQFLAEEAEKMKQVAEEAARL---------SVEAQEAARL------RKIAEDD----LN 2301
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELkkeikelkkAIEELKKAKGkcpvcgRELTEEHrkelLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2302 EQRALAEKILKEKMQAVQEASRLKAEAEMLqkqkEMAMEQAKKLQEDKEQMQQ--QLAEETEGFQ-KTLEAERRrqldis 2378
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELREL----EKVLKKESELIKLKELAEQlkELEEKLKKYNlEELEKKAE------ 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2379 aEAERLKLQVVEMSKSQAKAEEDAKK---FRKQAEDISEKLHQTElstKEKMTVVHTLEIQRQHSDKEAEELRKAIADLE 2455
Cdd:PRK03918 526 -EYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELE---EELAELLKELEELGFESVEELEERLKELEPFY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2456 NEKEKLKKEAELLQKKSEEMQKAQKE--QLRQETQTLQSTF-LTEKQILIQKEKYIEEEKAKLEKLFdnevgkaQKLKSE 2532
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEEldKAFEELAETEKRLeELRKELEELEKKYSEEEYEELREEY-------LELSRE 674
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1072265250 2533 KERQLAQLEEEKRLLQTSMDDAMKKQLDAEDRiRQKQEELQQLDK 2577
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEER-EKAKKELEKLEK 718
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2173-2613 |
7.99e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 7.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2173 AEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELFKVKIQmEELVKLKLRIEQenkm 2252
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-AELAELPERLEE---- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2253 lilkgkdntqqfLAEEAEKMKQVAEEAARLSVEAQEAarlrkiaeddlneQRALAEKILKEKMQAVQEASRLKAEAEMLQ 2332
Cdd:COG4717 151 ------------LEERLEELRELEEELEELEAELAEL-------------QEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2333 KQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAEE------------ 2400
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2401 ----------DAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAEELRKAIADLENEKeklkkeaellQK 2470
Cdd:COG4717 286 lallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL----------RE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2471 KSEEMQKAQKEQLRQETQTLQSTFLTEK-----QILIQKEKY--IEEEKAKLEKLFDNEVGKAQKLksEKERQLAQLEEE 2543
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVEDeeelrAALEQAEEYqeLKEELEELEEQLEELLGELEEL--LEALDEEELEEE 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072265250 2544 KRLLQTSMDDAMKKQLDAEDRIRQKQEELQQLDKKRQEQERLLEEENrkLRERLEQLEQEHRIA------LEKTRE 2613
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEE--LKAELRELAEEWAALklalelLEEARE 507
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1377-2373 |
8.57e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.75 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1377 AHAQAKAVAEKEALELRMNMQEEVTRREvvavdAEQQKKT-IQQELHQMKNN-SETE-----IKAKVKLIEEAEYNRKKV 1449
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLA-----AEQYRLVeMARELAELNEAeSDLEqdyqaASDHLNLVQTALRQQEKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1450 EEeiriiriqletsqkqksgAEDELRALRARAEEAERQKKLAQEEAERLRKQvkdeaqkKREAEDElhrkVQAEKDAARE 1529
Cdd:PRK04863 351 ER------------------YQADLEELEERLEEQNEVVEEADEQQEENEAR-------AEAAEEE----VDELKSQLAD 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1530 KQKALEDLEKFRLQAEEAerrmKQAeLEKERQIKQAHDVAQQSAD---AELQSKRMSFLEKTTQLE--MSLKQEHitvtH 1604
Cdd:PRK04863 402 YQQALDVQQTRAIQYQQA----VQA-LERAKQLCGLPDLTADNAEdwlEEFQAKEQEATEELLSLEqkLSVAQAA----H 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1605 LQEEaerlkkQQLEAETAKEEAEKELEKWrQKANEALRlrlqaeeiahkktlaqeEAEKQKEDAERETRKRtkAEESALR 1684
Cdd:PRK04863 473 SQFE------QAYQLVRKIAGEVSRSEAW-DVARELLR-----------------RLREQRHLAEQLQQLR--MRLSELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1685 QKDLAEEELEKQRKLAEETASHKLSAEQELirlkaevdsgEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEME 1764
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRLGKNLDDEDEL----------EQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQ 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1765 IL-------LKAKSKAE----------EDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQR 1827
Cdd:PRK04863 597 RLaarapawLAAQDALArlreqsgeefEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLN 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1828 AEAERILKEKLTAINEatrmrteaEIALKEK---EAENERLRR---LAEDEAYQRKLLEEqaaqhkQD-------IEEKI 1894
Cdd:PRK04863 677 ALAERFGGVLLSEIYD--------DVSLEDApyfSALYGPARHaivVPDLSDAAEQLAGL------EDcpedlylIEGDP 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1895 HQLKQSSENELERQKTIVDetlkhrRVIEEEIRILKINfEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEK-QR- 1972
Cdd:PRK04863 743 DSFDDSVFSVEELEKAVVV------KIADRQWRYSRFP-EVPLFGRAAREKRIEQLRAEREELAERYATLSFDVQKlQRl 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1973 ----------QLALVeeaRRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEK------------- 2029
Cdd:PRK04863 816 hqafsrfigsHLAVA---FEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRllprlnlladetl 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2030 -----EAEKQIQLAQDAARLKidaeeKAYYAAVQQKEQeMLQTRIQEQSIYDKLKEEAEKAKRAAEEAeRAKIKA----- 2099
Cdd:PRK04863 893 adrveEIREQLDEAEEAKRFV-----QQHGNALAQLEP-IVSVLQSDPEQFEQLKQDYQQAQQTQRDA-KQQAFAltevv 965
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2100 EHEAALSRQQAeeAERLKQKAEIEAQAKG---QAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMADAEMEKHKQFA--- 2173
Cdd:PRK04863 966 QRRAHFSYEDA--AEMLAKNSDLNEKLRQrleQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKqel 1043
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2174 ------------EKTVRQKEQVEGeltkvklQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELfkvKIQMEELVK 2241
Cdd:PRK04863 1044 qdlgvpadsgaeERARARRDELHA-------RLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDY---HEMREQVVN 1113
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2242 LKLRIEQENKMliLKGKDNTQQFLAEEAEKMKqvAEEAARLSVEAQEAARLRKIAEDDLNEQRALAE--KILKEKMQ--- 2316
Cdd:PRK04863 1114 AKAGWCAVLRL--VKDNGVERRLHRRELAYLS--ADELRSMSDKALGALRLAVADNEHLRDVLRLSEdpKRPERKVQfyi 1189
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072265250 2317 AVQEASRLKAEA---------EMLQkqkemAME-QAKKLQEDKEQMQQQLAEETE----GFQKTLEAERRR 2373
Cdd:PRK04863 1190 AVYQHLRERIRQdiirtddpvEAIE-----QMEiELSRLTEELTSREQKLAISSEsvanIIRKTIQREQNR 1255
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1826-2228 |
1.08e-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: 64.76 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1826 QRAEAERILKEKLTAInEATRMRTEAEialkEKEAENERLRRLAEDEAYQRKLLEEQAAqhkqdIEEKIHQLKQSSENEL 1905
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAA-----IYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1906 ERQKtivdetLKHRRVIEEEIRILKINFEKAsvgksdlelELQKLKNIADETQKSKEKAEQDAEKQRQLALveearrkea 1985
Cdd:pfam17380 351 ERIR------QEERKRELERIRQEEIAMEIS---------RMRELERLQMERQQKNERVRQELEAARKVKI--------- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1986 eekvkkiiaaeQEAGRQRKVALEEVERLKIKAdeakkqkdlaEKEAEKQIQLAqdaaRLKidaeekayyaavQQKEQEML 2065
Cdd:pfam17380 407 -----------LEEERQRKIQQQKVEMEQIRA----------EQEEARQREVR----RLE------------EERAREME 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2066 QTRIQEQsiydklkeeaekakraaeeaERakikaEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRkEAELEA 2145
Cdd:pfam17380 450 RVRLEEQ--------------------ER-----QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL-EKELEE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2146 AKRGQAEQAalKLKQMADAEME-KHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKL 2224
Cdd:pfam17380 504 RKQAMIEEE--RKRKLLEKEMEeRQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQI 581
|
....
gi 1072265250 2225 VEEE 2228
Cdd:pfam17380 582 VESE 585
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1748-2609 |
1.30e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.98 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1748 RRRGLEEELAKVRAEMEillkakskaeeDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEdATRQR 1827
Cdd:PRK04863 280 ERRVHLEEALELRRELY-----------TSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQT-ALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1828 ----------AEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLR-RLAEdeaYQRKLLEEQ--AAQHKQDIE--E 1892
Cdd:PRK04863 348 ekieryqadlEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsQLAD---YQQALDVQQtrAIQYQQAVQalE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1893 KIHQLKQSSENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEK-----AEQD 1967
Cdd:PRK04863 425 RAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWdvareLLRR 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1968 AEKQRQLAlveearrkeaeekvkkiiaaEQEAGRQRKvaLEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKID 2047
Cdd:PRK04863 505 LREQRHLA--------------------EQLQQLRMR--LSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2048 AEEKayYAAVQQKEQEMLQTRIQEQSIYDKLKEeaekakRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAK 2127
Cdd:PRK04863 563 LEAR--LESLSESVSEARERRMALRQQLEQLQA------RIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQ 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2128 GQAQEDAEKVRKEAELEAAKRgQAEQAALKLKQMADAEMEKHKQFAEktvrqkeQVEGELTK-----VKLQ--------L 2194
Cdd:PRK04863 635 QLLERERELTVERDELAARKQ-ALDEEIERLSQPGGSEDPRLNALAE-------RFGGVLLSeiyddVSLEdapyfsalY 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2195 EETDHqkAILDDELGRLKEEVTE----------------SLRQKKLVEEELFKVKIQmeELVKLKLRIEQENKMLILkGK 2258
Cdd:PRK04863 707 GPARH--AIVVPDLSDAAEQLAGledcpedlyliegdpdSFDDSVFSVEELEKAVVV--KIADRQWRYSRFPEVPLF-GR 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2259 DNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALA-----EKILKEKMQAVQEASRLKAEAEMLQK 2333
Cdd:PRK04863 782 AAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALADHESQEQ 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2334 QKEMAMEQAKKLQEDKEQMQQQ---LAEETegFQKTLEaERRRQLDISAEAERLKLQ----VVEMSKSQAKAEEDAKKF- 2405
Cdd:PRK04863 862 QQRSQLEQAKEGLSALNRLLPRlnlLADET--LADRVE-EIREQLDEAEEAKRFVQQhgnaLAQLEPIVSVLQSDPEQFe 938
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2406 --RKQAEDISEKLHQTelstKEKMTVVHTLEIQRQH-SDKEAEELRKAIADLENEKEKLkkeaellQKKSEEMQKAQKEQ 2482
Cdd:PRK04863 939 qlKQDYQQAQQTQRDA----KQQAFALTEVVQRRAHfSYEDAAEMLAKNSDLNEKLRQR-------LEQAEQERTRAREQ 1007
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2483 LRQEtqtlQSTFLTEKQILiqkekyieeekakleklfdnevgkaQKLKSEKERQLAQLEEEKRLLQtsmddAMKKQLD-- 2560
Cdd:PRK04863 1008 LRQA----QAQLAQYNQVL-------------------------ASLKSSYDAKRQMLQELKQELQ-----DLGVPADsg 1053
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2561 AEDRIRQKQEELQ-----------QLDKKRQEQERLLEEENRKLRErleqLEQEHRIALE 2609
Cdd:PRK04863 1054 AEERARARRDELHarlsanrsrrnQLEKQLTFCEAEMDNLTKKLRK----LERDYHEMRE 1109
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2044-2613 |
1.41e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2044 LKIDAEEKAYYAAVQQKEQEML--QTRIQEQSIYD------KLKEEAEKAKRAAEEAERakIKAEHEAALSRQQAEEAEr 2115
Cdd:PRK02224 122 LRMDAEAFVNCAYVRQGEVNKLinATPSDRQDMIDdllqlgKLEEYRERASDARLGVER--VLSDQRGSLDQLKAQIEE- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2116 lKQKAEIEAQAKGQAQEDAEkVRKEAELEAAKRGQAEQAalklKQMADAEMEKHkqfaEKTVRQKEQVEGELTKVKLQLE 2195
Cdd:PRK02224 199 -KEEKDLHERLNGLESELAE-LDEEIERYEEQREQARET----RDEADEVLEEH----EERREELETLEAEIEDLRETIA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2196 ETDHQKAILDDE-------LGRLKEEVTESLRQKKLVEEELFKVKIQMEELVKLK--LRIEQENKMLILKGKDNTQQFLA 2266
Cdd:PRK02224 269 ETEREREELAEEvrdlrerLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDeeLRDRLEECRVAAQAHNEEAESLR 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2267 EEAEKMKQVA----EEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQA 2342
Cdd:PRK02224 349 EDADDLEERAeelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2343 KKLQEDKEQMQQQLAE-----------------ETEGFQKTLEAERRRQLDISAEAERLKLQV------VEMSKSQAKAE 2399
Cdd:PRK02224 429 AELEATLRTARERVEEaealleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVeeveerLERAEDLVEAE 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2400 EDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQK-- 2477
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKEri 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2478 ----------AQKEQLRQETQTLQSTF--LTEKQILiQKEKYIE--EEKAKLEKLFDNE-VGKAQKLKSEKERQLAQLEE 2542
Cdd:PRK02224 589 eslerirtllAAIADAEDEIERLREKReaLAELNDE-RRERLAEkrERKRELEAEFDEArIEEAREDKERAEEYLEQVEE 667
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072265250 2543 EKRLLQTSMDdamkkqlDAEDRIRQKQEELQQLDkkrqeqerlleeenrKLRERLEQLEqEHRIALEKTRE 2613
Cdd:PRK02224 668 KLDELREERD-------DLQAEIGAVENELEELE---------------ELRERREALE-NRVEALEALYD 715
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
167-266 |
1.49e-09 |
|
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: 58.12 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 167 KEKLLLWSQRMSEGYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDmNRVYRQTN----LENLDQAFTVAERE-LGVTRL 241
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIP-KINKKPKSpfkkRENINLFLNACKKLgLPELDL 79
|
90 100
....*....|....*....|....*
gi 1072265250 242 LDPEDVdVPQPDEKSIITYVSSLYD 266
Cdd:cd00014 80 FEPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1350-1918 |
1.65e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1350 AEKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELR-----------MNMQEEVTRREVVAVDAEQQKKTIQ 1418
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEaqirgnggdrlEQLEREIERLERELEERERRRARLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1419 QELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERL 1498
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1499 RKQVKDEAQKKreaEDELhrKVQAE----KDAAREKQKALEDL---EKFRL--------QAEEAERRMK-QAELEKERQI 1562
Cdd:COG4913 446 RDALAEALGLD---EAEL--PFVGElievRPEEERWRGAIERVlggFALTLlvppehyaAALRWVNRLHlRGRLVYERVR 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1563 KQAHDVAQQSADAELQSKRMSFLEKTTQ--LEMSLKQE--HITVTHLQE---EAERLKKQQLEAETAKEEAEKELEKWRQ 1635
Cdd:COG4913 521 TGLPDPERPRLDPDSLAGKLDFKPHPFRawLEAELGRRfdYVCVDSPEElrrHPRAITRAGQVKGNGTRHEKDDRRRIRS 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1636 KA-----NEALRLRLQAEEIAHKKTLAqeEAEKQKEDAERETRKRTKAEESALRQKDLAEEEL---EKQRKLAEetashk 1707
Cdd:COG4913 601 RYvlgfdNRAKLAALEAELAELEEELA--EAEERLEALEAELDALQERREALQRLAEYSWDEIdvaSAEREIAE------ 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1708 lsAEQELIRLKAEVDSGEQhrivLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQM 1787
Cdd:COG4913 673 --LEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1788 LEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKE-KLTAINEATRMRTEAEiALKEKEAeneRLR 1866
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLE-SLPEYLA---LLD 822
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 1867 RLAEDE--AYQRKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKTIvDETLKH 1918
Cdd:COG4913 823 RLEEDGlpEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDPL-NDSLKR 875
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1350-2298 |
1.86e-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: 64.59 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1350 AEKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEkealELrmnmqEEVTRREvvavdaeqqkKTIQQElHQMKNNSE 1429
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMAR----EL-----EELSARE----------SDLEQD-YQAASDHL 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1430 TEIKAKVKLIEEAEYNRKKVEEeiriIRIQLETSQKQKSGAEDELralraraEEAERQKKLAQEEAERLRKQVKDEAQkk 1509
Cdd:COG3096 337 NLVQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLADYQQ-- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1510 reAEDELHRKvqaekdaAREKQKALEDLEKFRLQAEEAERRMKQAELEkerqikqahdvaQQSADAELQSKRMSFLEKTT 1589
Cdd:COG3096 404 --ALDVQQTR-------AIQYQQAVQALEKARALCGLPDLTPENAEDY------------LAAFRAKEQQATEEVLELEQ 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1590 QLEMSlkqehitvthlqEEAERLKKQQLEAETAKEEAEKELEKWrQKANEALRlrlqaEEIAHKKTLAQEEAEKQK-EDA 1668
Cdd:COG3096 463 KLSVA------------DAARRQFEKAYELVCKIAGEVERSQAW-QTARELLR-----RYRSQQALAQRLQQLRAQlAEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1669 ERETRKRTKAEESAlrqkdlaeEELEKQrklaeetASHKLSAEQELIRLKAEvdsgeqhrivLEEDLFRLKNEVNEAIQR 1748
Cdd:COG3096 525 EQRLRQQQNAERLL--------EEFCQR-------IGQQLDAAEELEELLAE----------LEAQLEELEEQAAEAVEQ 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1749 RRGLEEELAKVRAEMEIL-------LKAKSKAE----------EDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEE 1811
Cdd:COG3096 580 RSELRQQLEQLRARIKELaarapawLAAQDALErlreqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQ 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1812 AKRQRQLAEEDATRQRAEAERILKEKLTAINEatrmrteaEIALkekeaenerlrrlaEDEAYQRKLLEEqaAQHK---- 1887
Cdd:COG3096 660 IERLSQPGGAEDPRLLALAERLGGVLLSEIYD--------DVTL--------------EDAPYFSALYGP--ARHAivvp 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1888 --QDIEEKIHQLKQSSEN-------------------ELERQKTIVDET------------LKHRRVIEEEIRILKINFE 1934
Cdd:COG3096 716 dlSAVKEQLAGLEDCPEDlyliegdpdsfddsvfdaeELEDAVVVKLSDrqwrysrfpevpLFGRAAREKRLEELRAERD 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1935 KASVGKSDLELELQKLKNI-----------------ADETQKSKEKAEQDAEKQRQLAlveearrkeaeeKVKKIIAAEQ 1997
Cdd:COG3096 796 ELAEQYAKASFDVQKLQRLhqafsqfvgghlavafaPDPEAELAALRQRRSELERELA------------QHRAQEQQLR 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1998 EAGRQRKVALEEVERL----KIKADEakkqkDLAEK--EAEKQIQLAQDAARlkidaEEKAYYAAVQQKEqEMLQTRIQE 2071
Cdd:COG3096 864 QQLDQLKEQLQLLNKLlpqaNLLADE-----TLADRleELREELDAAQEAQA-----FIQQHGKALAQLE-PLVAVLQSD 932
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2072 QSIYDKLKEEAEKAKRAAEEAeRAKIKA-------------EHEAALSRQQAEEAERLKQKAEieaqakgQAQEDAEKVR 2138
Cdd:COG3096 933 PEQFEQLQADYLQAKEQQRRL-KQQIFAlsevvqrrphfsyEDAVGLLGENSDLNEKLRARLE-------QAEEARREAR 1004
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2139 KEAELEAAKRGQAEQAALKLKQMADAEMEKHKQF--------------AEKTVRQ-KEQVEGELTKVKLQLEETDHQKAI 2203
Cdd:COG3096 1005 EQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELeqeleelgvqadaeAEERARIrRDELHEELSQNRSRRSQLEKQLTR 1084
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2204 LDDELGRLKEEVTESLRQKKLVEEELFKVKIQMEELvklkLRIEQENKMLilkGKDNTQQFLAEEAEKMKQVAEE---AA 2280
Cdd:COG3096 1085 CEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAV----LRLARDNDVE---RRLHRRELAYLSADELRSMSDKalgAL 1157
|
1050
....*....|....*....
gi 1072265250 2281 RLSVEAQEAAR-LRKIAED 2298
Cdd:COG3096 1158 RLAVADNEHLRdALRLSED 1176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1756-2221 |
2.36e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1756 LAKVRAEMEILLKAKSKaeedsrsTSEKSKQMLEVEASKLRELAEEAARLRavseEAKRQRQLAEED-----ATRQRAEA 1830
Cdd:COG4717 48 LERLEKEADELFKPQGR-------KPELNLKELKELEEELKEAEEKEEEYA----ELQEELEELEEEleeleAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1831 ERILKEKLTAINEATRMRTEAEIALKEKEAENERLR-RLAEDEAYQRKL--LEEQAAQHKQDIEEKIHQLKQSSENELEr 1907
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEeRLEELRELEEELeeLEAELAELQEELEELLEQLSLATEEELQ- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1908 qktivdETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIAdETQKSKEKAEQDAEKQRQLALVEEARRKEAEE 1987
Cdd:COG4717 196 ------DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-EAAALEERLKEARLLLLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1988 KVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQlaqdAARLKIDAEEKAYYAAVQQKEQEMLQT 2067
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE----EEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2068 RIQEqsiydkLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEieaqAKGQAQEDAEKVRK-EAELEAA 2146
Cdd:COG4717 345 RIEE------LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE----QAEEYQELKEELEElEEQLEEL 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 2147 KRGQAEQAALKLKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLE--ETDHQKAILDDELGRLKEEVTESLRQ 2221
Cdd:COG4717 415 LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEE 491
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3965-4003 |
2.92e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 55.03 E-value: 2.92e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1072265250 3965 LLEAQAATGYVIDPIKCLKLAVEDAVRMGIVGTEFKDKL 4003
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2290-2720 |
3.21e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2290 ARLRKIAEDDLNEQRALAEKILKEKMQAVQEASrlKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEA 2369
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEAR--KAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2370 ERRRQLDISAEAERLKlqvvemsksQAKAEEDAKKFRKQAE-DISEKLHQTELSTKEKmTVVHTLEIQRQHSDKEAEELR 2448
Cdd:PTZ00121 1161 EDARKAEEARKAEDAK---------KAEAARKAEEVRKAEElRKAEDARKAEAARKAE-EERKAEEARKAEDAKKAEAVK 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2449 KAiadlenekeklkkeaELLQKKSEEMQKAQKEQLRQETQTLQSTFLTEKQILIQKEKYIEEEKAkleklfdNEVGKAQK 2528
Cdd:PTZ00121 1231 KA---------------EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA-------DELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2529 LKSEKErqlAQLEEEKRllqtSMDDAMKKqldAEDRirQKQEELQqldKKRQEQERLLEEENRKLRERLEQLEQEHRIAL 2608
Cdd:PTZ00121 1289 KKKADE---AKKAEEKK----KADEAKKK---AEEA--KKADEAK---KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2609 EKTREVIITKETVITQTKTMPNGRDAADGSAQNGELLNAFDGLRQKISPDKlfeagiLTKEQLDKLASGQLTVDDLSKR- 2687
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK------KKADELKKAAAAKKKADEAKKKa 1427
|
410 420 430
....*....|....*....|....*....|....*...
gi 1072265250 2688 EEIRRYLQGKSSI-----AGLLLKPSNEKMSIYNAMKK 2720
Cdd:PTZ00121 1428 EEKKKADEAKKKAeeakkADEAKKKAEEAKKAEEAKKK 1465
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1821-2461 |
3.63e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.20 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1821 EDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLL--EEQAAQHKQDIeekihqLK 1898
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikENNATRHLCNL------LK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1899 QSSENELERQKTIVDETLKHRRV---IEEEIRILKINFEKASVGKSDLELELQ-KLKNIADETQKSKEKAEQ---DAEKQ 1971
Cdd:pfam05483 162 ETCARSAEKTKKYEYEREETRQVymdLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKeinDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1972 RQLALVEEARRKEAEEKVKKIIaaeqEAGRQRKVALEEVERLKikaDEAKKQKDlaekeaEKQIQLAQDAARLKIDAEEK 2051
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLL----EESRDKANQLEEKTKLQ---DENLKELI------EKKDHLTKELEDIKMSLQRS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2052 -AYYAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRA----AEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQA 2126
Cdd:pfam05483 309 mSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAhsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2127 KGQAQEDAEKVR--KEAELEAAKRGQAEQAALKLKQMADAEMEKHKQFAEKTV------RQKE--QVEGELTKVKLQLEE 2196
Cdd:pfam05483 389 KSSELEEMTKFKnnKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqaREKEihDLEIQLTAIKTSEEH 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2197 TDHQKAILDDELGRLKEEVTE--------SLRQKKLVEEE---LFKVKIQMEELVKLKlriEQENKMLI-LKGKDNTQQF 2264
Cdd:pfam05483 469 YLKEVEDLKTELEKEKLKNIEltahcdklLLENKELTQEAsdmTLELKKHQEDIINCK---KQEERMLKqIENLEEKEMN 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2265 LAEEAE---------------KMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAE 2329
Cdd:pfam05483 546 LRDELEsvreefiqkgdevkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2330 MLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQ-------------- 2395
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQkeidkrcqhkiaem 705
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 2396 -AKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAEELRKAIADLENEKEKL 2461
Cdd:pfam05483 706 vALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKL 772
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1997-2155 |
4.74e-09 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 62.33 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1997 QEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAyyAAVQQKEQEMLQtriqeqsiyD 2076
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPA--DTSSPKEDKQVA---------E 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2077 KLKEEAEKA----KRAAEEAERAKikaEHEAALSRQQAEEAERLKQKAEIEAQAKGQ-AQEDAEKVRKEAELEAAKRGQA 2151
Cdd:pfam05262 278 NQKREIEKAqieiKKNDEEALKAK---DHKAFDLKQESKASEKEAEDKELEAQKKREpVAEDLQKTKPQVEAQPTSLNED 354
|
....
gi 1072265250 2152 EQAA 2155
Cdd:pfam05262 355 AIDS 358
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
35-149 |
4.90e-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: 57.13 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 35 QDAEDERdrvqkkTFTKWVNKhlikhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPREKG-----RMRFHKLQNV 109
Cdd:cd21299 1 ETSREER------CFRLWINS-------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENC 67
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1072265250 110 QIALDFLKLRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 149
Cdd:cd21299 68 NQVVKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
522-710 |
5.44e-09 |
|
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: 59.38 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 522 LRYFQDLLAWVEENQKRINTAEWGSDLPSVESQLGSHRGLHQSINEFRAKIERARTDEGQIPGSRGAY----QDYLGKLD 597
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 598 LQYAKLLNSSKARLRNLE---SLNTFVAAATKELMWLNDKEEEEVNFDWSDRNTNMTSKKDNYSGLMRELELKEKKIKEI 674
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1072265250 675 QNTGDRLLRDDHPGKS-TIEAFQAALQTQWSWMLQLC 710
Cdd:cd00176 166 NELAEELLEEGHPDADeEIEEKLEELNERWEELLELA 202
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1953-2302 |
5.55e-09 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 62.19 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1953 IADETQKSKE---KAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLK--IKADEAKKQKDLA 2027
Cdd:pfam02029 1 IEDEEEAARErrrRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLdrTAKREERRQKRLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2028 E-----KEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQ-EMLQTRIQEQSIYDKLKEEAEKAKRaaEEAERAKIKAEH 2101
Cdd:pfam02029 81 EalerqKEFDPTIADEKESVAERKENNEEEENSSWEKEEKrDSRLGRYKEEETEIREKEYQENKWS--TEVRQAEEEGEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2102 EAalsRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAAlklkQMADAEMEKHKQFAEKTVRQKE 2181
Cdd:pfam02029 159 EE---DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKS----QNGEEEVTKLKVTTKRRQGGLS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2182 QVEGELTKVKLQLeETDHQKAILDDELGRLKEEVTESLRQKKL-VEEELFKVKIQMEElvKLKLRIEQENKmlilKGKDN 2260
Cdd:pfam02029 232 QSQEREEEAEVFL-EAEQKLEELRRRRQEKESEEFEKLRQKQQeAELELEELKKKREE--RRKLLEEEEQR----RKQEE 304
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1072265250 2261 TQQFLAEEAEKmKQVAEEAARLSVEAQEaaRLRKIAEDDLNE 2302
Cdd:pfam02029 305 AERKLREEEEK-RRMKEEIERRRAEAAE--KRQKLPEDSSSE 343
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2022-2211 |
6.08e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.75 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2022 KQKDLAEKEAEKQIQLAQDAARLkidaEEKAyyAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEH 2101
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEEL----QQKQ--AAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2102 EAALsrQQAEEAERLkqkaeieAQAKGQAQEDAEKV-------------RKEAELEAAKRGQAE-----------QAALK 2157
Cdd:PRK09510 144 AAKA--KAEAEAKRA-------AAAAKKAAAEAKKKaeaeaakkaaaeaKKKAEAEAAAKAAAEakkkaeaeakkKAAAE 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 2158 LKQMADAEMEKHKQFAEKtvRQKEQVEGELTKVKLQLEETDHQKAILDDELGRL 2211
Cdd:PRK09510 215 AKKKAAAEAKAAAAKAAA--EAKAAAEKAAAAKAAEKAAAAKAAAEVDDLFGGL 266
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4385-4423 |
6.33e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 54.26 E-value: 6.33e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1072265250 4385 FLEVQYLTGGLIEPDVEGRVNLDEALHKGTIDARTAQKL 4423
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2301-2606 |
6.86e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.45 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2301 NEQRALAEKILKEKMQAVQEAsrlKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQ-QLAEETEGFQKTLEAERRRQLDISA 2379
Cdd:pfam17380 261 NGQTMTENEFLNQLLHIVQHQ---KAVSERQQQEKFEKMEQERLRQEKEEKAREvERRRKLEEAEKARQAEMDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2380 EAERLKLQVvEMSKSQAKAEEDAKKFrkqaedisEKLHQTELSTK-EKMTVVHTLEIQRQHSD----KEAEELRKAIADL 2454
Cdd:pfam17380 338 EQERMAMER-ERELERIRQEERKREL--------ERIRQEEIAMEiSRMRELERLQMERQQKNervrQELEAARKVKILE 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2455 ENEKEKLKKEAELLQKKSEEMQKAQKEQLR---------------QETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLF 2519
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREVRrleeeraremervrlEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2520 DNEVGKAQKLKSEKERQLAQLEEE--KRLLQTSMDDAMKKQLDAEDRIRQKQEELQQLDKKRQEQERLLEEENRKLRERL 2597
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEErkRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRL 568
|
....*....
gi 1072265250 2598 EQLEQEHRI 2606
Cdd:pfam17380 569 EAMEREREM 577
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
165-267 |
7.74e-09 |
|
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: 56.62 E-value: 7.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 165 TAKEKLLLWSQ-RMSEgyqgLRCDNFTSNWRDGRLFSAIIHRHKPMLI-DMNRVYRQTNLENLDQAFTVAERELGVTRLL 242
Cdd:cd21314 11 TPKQRLLGWIQnKVPQ----LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVI 86
|
90 100
....*....|....*....|....*
gi 1072265250 243 DPEDVDVPQPDEKSIITYVSSLYDA 267
Cdd:cd21314 87 APEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
158-267 |
8.21e-09 |
|
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: 56.25 E-value: 8.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 158 TGQSEDMTAKEKLLLWSQRMsegYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLI-DMNRVYRQTNLENLDQAFTVAEREL 236
Cdd:cd21313 1 DDDAKKQTPKQRLLGWIQNK---IPYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWL 77
|
90 100 110
....*....|....*....|....*....|.
gi 1072265250 237 GVTRLLDPEDVDVPQPDEKSIITYVSSLYDA 267
Cdd:cd21313 78 GVPQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1477-1920 |
8.44e-09 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 62.38 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1477 LRARAEEAERQKKLAQEEA-ERL---------RKQVKDEAQKKREAEDE---LHRKVQAEKDAAREKQKALEDlekfRLQ 1543
Cdd:PRK10929 28 ITQELEQAKAAKTPAQAEIvEALqsalnwleeRKGSLERAKQYQQVIDNfpkLSAELRQQLNNERDEPRSVPP----NMS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1544 AEEAERRMKQAE---LEKERQIKQAHDVAQQSADaelqskrmsflekttqlemSLKQehitVTHLQEEAERLkkqqleae 1620
Cdd:PRK10929 104 TDALEQEILQVSsqlLEKSRQAQQEQDRAREISD-------------------SLSQ----LPQQQTEARRQ-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1621 takeeaekelekwrqkANEALRlRLQAeeiAHKKTLAQEEAEkqkedaeretRKRTKAEESALRQKdlaEEELEkqrkLA 1700
Cdd:PRK10929 153 ----------------LNEIER-RLQT---LGTPNTPLAQAQ----------LTALQAESAALKAL---VDELE----LA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1701 EETASHKlsaeQELIRLKAEVDSGEQHRivLEEDLFRLKNEVNeaIQRRRglEEELAKVRAEMeillkakskAEEDSRST 1780
Cdd:PRK10929 196 QLSANNR----QELARLRSELAKKRSQQ--LDAYLQALRNQLN--SQRQR--EAERALESTEL---------LAEQSGDL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1781 SEKSKQMLEVEasklRELAeeaarlRAVSEEAKRQRQLAEedatRQRAEAERIL--KEKLTAINEATRMrteaeiaLKEK 1858
Cdd:PRK10929 257 PKSIVAQFKIN----RELS------QALNQQAQRMDLIAS----QQRQAASQTLqvRQALNTLREQSQW-------LGVS 315
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072265250 1859 EAENERLR----RLAEDEAYQRklLEEQAAQ------HKQDIEEKIHQLKQSSENE----LERQKTIVDETLKHRR 1920
Cdd:PRK10929 316 NALGEALRaqvaRLPEMPKPQQ--LDTEMAQlrvqrlRYEDLLNKQPQLRQIRQADgqplTAEQNRILDAQLRTQR 389
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1460-1671 |
9.58e-09 |
|
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: 61.51 E-value: 9.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1460 LETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQkaledLEK 1539
Cdd:pfam15709 324 LLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQR-----LEE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1540 FRLQAEEAER---RMKQAELEKERQIKQAHDVAQQSADAELQSKRMSFLEKTTQ----LEMSLKQEHITVTHLQEEaERL 1612
Cdd:pfam15709 399 ERQRQEEEERkqrLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQrqkeLEMQLAEEQKRLMEMAEE-ERL 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 1613 KKQqleaetakeeaekelekwRQKANEALRLRLQAEEIAHKKT----LAQEEAEKQKEDAERE 1671
Cdd:pfam15709 478 EYQ------------------RQKQEAEEKARLEAEERRQKEEeaarLALEEAMKQAQEQARQ 522
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2145-2386 |
1.07e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2145 AAKRGQAEQAALKLKQmADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKL 2224
Cdd:COG4942 16 AAQADAAAEAEAELEQ-LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2225 VEEELFKVKIQMEELVKLKLRIEQENKMLILKGKDNTQQFlAEEAEKMKQVA----EEAARLSVEAQEAARLRKIAEDDL 2300
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDA-VRRLQYLKYLAparrEQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2301 NEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEetegFQKTLEAERRRQLDISAE 2380
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR----LEAEAAAAAERTPAAGFA 249
|
....*.
gi 1072265250 2381 AERLKL 2386
Cdd:COG4942 250 ALKGKL 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1657-2179 |
1.43e-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: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1657 AQEEAEKQKEDAERETRKRTKAEE--SALRQKDLAEEELEKQRKLAEETASHKLsaEQELIRLKAEVDSGEQHRIVLEED 1734
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERyaAARERLAELEYLRAALRLWFAQRRLELL--EAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1735 LFRLKNEVNEAIQRRRG--------LEEELAKVRAEMEILLKAKSKAEEDSRS---TSEKSKQMLEVEASKLRELAEEAA 1803
Cdd:COG4913 318 LDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAAlglPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1804 RLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAIN----EATRMRTEAEIALKEKEAEnerLRRLAEdeayqrkLL 1879
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEAE---LPFVGE-------LI 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1880 EEQAAQHK-QD-IEEKIHQLKQS---SENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDL----------- 1943
Cdd:COG4913 468 EVRPEEERwRGaIERVLGGFALTllvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLagkldfkphpf 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1944 ----ELELQKLKNIA---DETQ---------------KSKEKAEQDAEKQRQLALVEEARRKeaeekvKKIIAAEQEAGR 2001
Cdd:COG4913 548 rawlEAELGRRFDYVcvdSPEElrrhpraitragqvkGNGTRHEKDDRRRIRSRYVLGFDNR------AKLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2002 QRkvalEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLkIDAEEKAyyAAVQQKEQEMLQTRiQEQSIYDKLKEE 2081
Cdd:COG4913 622 LE----EELAEAEERLEALEAELDALQERREALQRLAEYSWDE-IDVASAE--REIAELEAELERLD-ASSDDLAALEEQ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2082 AEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAE-----IEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAAL 2156
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdrleaAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
570 580
....*....|....*....|...
gi 1072265250 2157 KLKQmADAEMEKHKQFAEKTVRQ 2179
Cdd:COG4913 774 RIDA-LRARLNRAEEELERAMRA 795
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
47-146 |
1.67e-08 |
|
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: 55.04 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 47 KTFTKWVNKHLIKhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETL------PREKGRMrfhkLQNVQIALDFLKLRQ 120
Cdd:cd21286 3 KIYTDWANHYLAK---SGHKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARG 75
|
90 100
....*....|....*....|....*.
gi 1072265250 121 VKLVNIRNDDIADGNPKLTLGLIWTI 146
Cdd:cd21286 76 VNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1905-2446 |
1.70e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 60.81 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1905 LERQKTIVDETLKhrrvIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQ---LALVEEAR 1981
Cdd:pfam05701 34 VERRKLVELELEK----VQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQdseLAKLRVEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1982 RKEAEEKVKKIIAAEQ-EAGRQR-KVALEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQq 2059
Cdd:pfam05701 110 MEQGIADEASVAAKAQlEVAKARhAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIE- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2060 keqemlqtriqeqsiYDKLKEEAEKAKRAAEEAERAKIKaeheAALSRQQaeeaERLKQKAEIEaqakgQAQEDAEKVRK 2139
Cdd:pfam05701 189 ---------------LIATKESLESAHAAHLEAEEHRIG----AALAREQ----DKLNWEKELK-----QAEEELQRLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2140 --------EAELEAAKRGQ----AEQAAL---KLKQMADAEMEKHKqfaeKTVRQKEQVEG---ELTKVKLQLEE-TDHQ 2200
Cdd:pfam05701 241 qllsakdlKSKLETASALLldlkAELAAYmesKLKEEADGEGNEKK----TSTSIQAALASakkELEEVKANIEKaKDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2201 KAI------LDDELGRLKEEVTeSLRQKklveEELFKVKI-QMEELVKlklRIEQENKMLILKGKdntqqflaEEAEKMK 2273
Cdd:pfam05701 317 NCLrvaaasLRSELEKEKAELA-SLRQR----EGMASIAVsSLEAELN---RTKSEIALVQAKEK--------EAREKMV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2274 QVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKIlKEKMQAVQeaSRLKA---EAEMLQKQKEMAMEQAKKLQEDKE 2350
Cdd:pfam05701 381 ELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQA-KAAASTVE--SRLEAvlkEIEAAKASEKLALAAIKALQESES 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2351 QMQQQLAEETEgfqktleaerrRQLDISAEaerlklQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVV 2430
Cdd:pfam05701 458 SAESTNQEDSP-----------RGVTLSLE------EYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEV 520
|
570
....*....|....*.
gi 1072265250 2431 HTLEIQRQHSDKEAEE 2446
Cdd:pfam05701 521 NREMEERKEALKIALE 536
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1633-2420 |
1.95e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.13 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1633 WRQKANEALRlrlQAEEIAH------KKTLAQEEAEKQKEDA-ERETRKRTKAEESALRQKDLAEEELEKQRKL--AEET 1703
Cdd:PRK04863 336 HLNLVQTALR---QQEKIERyqadleELEERLEEQNEVVEEAdEQQEENEARAEAAEEEVDELKSQLADYQQALdvQQTR 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1704 ASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKA----KSKAEEDSRS 1779
Cdd:PRK04863 413 AIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAyqlvRKIAGEVSRS 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1780 TSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLaEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKE 1859
Cdd:PRK04863 493 EAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQ-QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1860 AENERLRRLAEDEAYQRKLLEEQAAQHKQdIEEKIHQLKQSseneLERQKTIVDETLKHRRVIEEEIRILKINFEKASVG 1939
Cdd:PRK04863 572 ESVSEARERRMALRQQLEQLQARIQRLAA-RAPAWLAAQDA----LARLREQSGEEFEDSQDVTEYMQQLLERERELTVE 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1940 KSDLELELQKLKNIADETQkSKEKAEqdAEKQRQLAlveearrkeaeEKVKKIIAAE-------QEAG---------RQR 2003
Cdd:PRK04863 647 RDELAARKQALDEEIERLS-QPGGSE--DPRLNALA-----------ERFGGVLLSEiyddvslEDAPyfsalygpaRHA 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2004 KValeeVERLKIKADEAKKQKDLAEK----EAEKQiqlAQDAARLKIDAEEKAyyAAVQQKEQEMLQTRIQEQSIYDklk 2079
Cdd:PRK04863 713 IV----VPDLSDAAEQLAGLEDCPEDlyliEGDPD---SFDDSVFSVEELEKA--VVVKIADRQWRYSRFPEVPLFG--- 780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2080 eeaekakRAAEEAERAKIKAEHEaALSRQQAEEA------ERLKQKAEieaQAKGQAQEDAEKVRKEAELEAA--KRGQA 2151
Cdd:PRK04863 781 -------RAAREKRIEQLRAERE-ELAERYATLSfdvqklQRLHQAFS---RFIGSHLAVAFEADPEAELRQLnrRRVEL 849
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2152 EQAalklkqMADAEmEKHKQFAEKTVRQKEQV---EGELTKVKLQLEETdhqkaiLDDELGRLKEEVTESLRQKK----- 2223
Cdd:PRK04863 850 ERA------LADHE-SQEQQQRSQLEQAKEGLsalNRLLPRLNLLADET------LADRVEEIREQLDEAEEAKRfvqqh 916
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2224 -----LVEEELFKVKIQMEELVKLKLRIEQenkmlilkgKDNTQQFLAEEAEKMKQVAEEAARLSVEaqEAARLRkIAED 2298
Cdd:PRK04863 917 gnalaQLEPIVSVLQSDPEQFEQLKQDYQQ---------AQQTQRDAKQQAFALTEVVQRRAHFSYE--DAAEML-AKNS 984
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2299 DLNEQralaekiLKEKM-QAVQEASRLKAEAemlqKQKEMAMEQAKKLQED-------KEQMQQQLAEETE--GFQKTLE 2368
Cdd:PRK04863 985 DLNEK-------LRQRLeQAEQERTRAREQL----RQAQAQLAQYNQVLASlkssydaKRQMLQELKQELQdlGVPADSG 1053
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 1072265250 2369 AE---RRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTE 2420
Cdd:PRK04863 1054 AEeraRARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1350-2154 |
2.04e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.13 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1350 AEKLkEQERKKLAEVEDQLEKQR--------QLAEAHAQAKAvAEKEALELRMNMQEEVTRREVvavdaeQQKKTIQqeL 1421
Cdd:PRK04863 347 QEKI-ERYQADLEELEERLEEQNevveeadeQQEENEARAEA-AEEEVDELKSQLADYQQALDV------QQTRAIQ--Y 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1422 HQmknnseteikaKVKLIEEAeynrkkveeeiriiRIQLETSQKQKSGAEDELRALRARAEEAErqkkLAQEEAERlRKQ 1501
Cdd:PRK04863 417 QQ-----------AVQALERA--------------KQLCGLPDLTADNAEDWLEEFQAKEQEAT----EELLSLEQ-KLS 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1502 VKDEAQKKREAEDELHRKVQAEKDAAREKQKA---LEDLEKFRLQAEEAE-RRMKQAELEKERQIKQahDVAQQSADAEL 1577
Cdd:PRK04863 467 VAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVArelLRRLREQRHLAEQLQqLRMRLSELEQRLRQQQ--RAERLLAEFCK 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1578 QSKRMsfLEKTTQLEMSLKQEHITVTHLQEEAER-------LKKQQLEAETAKEEAEKELEKWRQkANEAL-RLRLQAEE 1649
Cdd:PRK04863 545 RLGKN--LDDEDELEQLQEELEARLESLSESVSEarerrmaLRQQLEQLQARIQRLAARAPAWLA-AQDALaRLREQSGE 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1650 --------IAHKKTLAQEEAEKQKEDAERETRKRT-KAEESALRQKDLAeeELEKQRKLAEETASHKLSAEQELIRLKae 1720
Cdd:PRK04863 622 efedsqdvTEYMQQLLERERELTVERDELAARKQAlDEEIERLSQPGGS--EDPRLNALAERFGGVLLSEIYDDVSLE-- 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1721 vDSGE--------QHRIVLeEDLfrlkNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMlEVEA 1792
Cdd:PRK04863 698 -DAPYfsalygpaRHAIVV-PDL----SDAAEQLAGLEDCPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIADR-QWRY 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1793 SKLRE--LAEEAARlRAVSEEAKRQRQ-LAEEDATR--QRAEAERILK--EKLTAINEATRMRTEAEIALKEKEAE-NER 1864
Cdd:PRK04863 771 SRFPEvpLFGRAAR-EKRIEQLRAEREeLAERYATLsfDVQKLQRLHQafSRFIGSHLAVAFEADPEAELRQLNRRrVEL 849
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1865 LRRLAEDEAYqrkllEEQAAQHKQDIEEKIHQLkqsseNELERQ-KTIVDETLKHR-RVIEEEIrilkinfEKASVGKSD 1942
Cdd:PRK04863 850 ERALADHESQ-----EQQQRSQLEQAKEGLSAL-----NRLLPRlNLLADETLADRvEEIREQL-------DEAEEAKRF 912
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1943 LELELQKLKNIADETQKSKEKAEQDAEKQRQLALVEearrkeaeekvkkiiaAEQEAGRQRKVALEEVERLKIKADEAKK 2022
Cdd:PRK04863 913 VQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQ----------------QTQRDAKQQAFALTEVVQRRAHFSYEDA 976
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2023 QKDLAeKEAEKQIQLAQDAARLKIDAEE-KAYYAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKR---------AAEEA 2092
Cdd:PRK04863 977 AEMLA-KNSDLNEKLRQRLEQAEQERTRaREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQelqdlgvpaDSGAE 1055
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 2093 ERAKI-KAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQedaeKVRKEAELEAAKRGQAEQA 2154
Cdd:PRK04863 1056 ERARArRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTK----KLRKLERDYHEMREQVVNA 1114
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2179-2603 |
2.19e-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: 60.80 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2179 QKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTES-------LRQKKLVEEELFKVKIQMEEL------VKLKLR 2245
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLnnkyndlKKQKEELENELNLLEKEKLNIqknidkIKNKLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2246 IeQENKMLILKGKDNTQQFLAEEAEKMK----QVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKI---LKEKMQAV 2318
Cdd:TIGR04523 198 K-LELLLSNLKKKIQKNKSLESQISELKkqnnQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIkkqLSEKQKEL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2319 QEASR-----------LKAEAEMLQKQKEMAM-----EQAKKLQEDKEQMQQQLA----------EETEGFQKTLEAERR 2372
Cdd:TIGR04523 277 EQNNKkikelekqlnqLKSEISDLNNQKEQDWnkelkSELKNQEKKLEEIQNQISqnnkiisqlnEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2373 RQLDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAEELRKAIA 2452
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2453 DLENEKEKLKKEAELLQKKSEEMqKAQKEQLRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKL-------------- 2518
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNL-DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLneekkeleekvkdl 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2519 ------FDNEVGKAQKLKSEKERQLAQLEEEKRllqtSMDDAMKKQLdAEDRIRQKQEELQQLdkkrQEQERLLEEENRK 2592
Cdd:TIGR04523 516 tkkissLKEKIEKLESEKKEKESKISDLEDELN----KDDFELKKEN-LEKEIDEKNKEIEEL----KQTQKSLKKKQEE 586
|
490
....*....|.
gi 1072265250 2593 LRERLEQLEQE 2603
Cdd:TIGR04523 587 KQELIDQKEKE 597
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1351-1537 |
2.21e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.82 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1351 EKLKEQERKKLAEVEDQL--EKQRQLAEAHAQAKAVAEKEAlelrmnmQEEVTRREVVAVDAEQQKKTIQQELHQMKNNS 1428
Cdd:PRK09510 109 ERLAAQEQKKQAEEAAKQaaLKQKQAEEAAAKAAAAAKAKA-------EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1429 ETEIKAkvklieEAEYNRKKVEEEiriiriqletsqKQKSGAEDELRALRARAEEAERQKKLAQEEAerlrkqvkdEAQK 1508
Cdd:PRK09510 182 EAKKKA------EAEAAAKAAAEA------------KKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA---------AAEA 234
|
170 180
....*....|....*....|....*....
gi 1072265250 1509 KREAEDELHRKvQAEKDAAREKQKALEDL 1537
Cdd:PRK09510 235 KAAAEKAAAAK-AAEKAAAAKAAAEVDDL 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1476-1707 |
2.33e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1476 ALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAE 1555
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1556 LEKERQIKQAHDVAQQSADAELQSKRMSFL--EKTTQLEMSLKQEHITVTHLQEEAERLKKQQ--LEAETAKEEAEKELE 1631
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLaeLAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072265250 1632 KWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHK 1707
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2020-2221 |
2.52e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 59.47 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2020 AKKQKDLAEKEAEKQIQLAQDAARLKIDaeekayyaavQQKEQEMLQtRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKA 2099
Cdd:TIGR02794 56 QQQKKPAAKKEQERQKKLEQQAEEAEKQ----------RAAEQARQK-ELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2100 EHEAALSRQQAEEAERL-KQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKL-KQMADAEMEKHKQFAEKTV 2177
Cdd:TIGR02794 125 KAKQAAEAKAKAEAEAErKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEaEAKAKAEEAKAKAEAAKAK 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1072265250 2178 RQKEQVEGELTKVKLQLEETDHQKAI---LDDELGRLKEEVTESLRQ 2221
Cdd:TIGR02794 205 AAAEAAAKAEAEAAAAAAAEAERKADeaeLGDIFGLASGSNAEKQGG 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1850-2299 |
2.98e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1850 EAEIALKEKEAENERLRRLAEDEAYQRKLLEEqAAQHKQDIEEKIHQLKQSSENElerqktivdETLKHRRVIEEEIRIL 1929
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQLL---------PLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1930 KINFEKAsvgKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEE 2009
Cdd:COG4717 145 PERLEEL---EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2010 VERLKIKADEAKKQKDLAEKE---AEKQIQLAQDAARLKIDAEEKAYYAAVQQ-KEQEMLQTRIQEQSIYDKLKEEAEKA 2085
Cdd:COG4717 222 LEELEEELEQLENELEAAALEerlKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2086 KRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEA-AKRGQAEQAALKLKQMADA 2164
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEeLQLEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2165 EMEKHKQFAEKTVRQKEQVEGELTKVKLQLEEtdhqkaILDDELGRLKEEVTESLRQK-KLVEEELFKVKIQMEELVKLK 2243
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQLEE------LLGELEELLEALDEEELEEElEELEEELEELEEELEELREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 2244 LRIEQENKMLILKGK-DNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDD 2299
Cdd:COG4717 456 AELEAELEQLEEDGElAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
160-262 |
3.11e-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: 54.79 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 160 QSEDMTAKEKLLLWSQ-RMSEgyqgLRCDNFTSNWRDGRLFSAIIHRHKPMLI-DMNRVYRQTNLENLDQAFTVAERELG 237
Cdd:cd21315 11 DGKGPTPKQRLLGWIQsKVPD----LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLD 86
|
90 100
....*....|....*....|....*
gi 1072265250 238 VTRLLDPEDVDVPQPDEKSIITYVS 262
Cdd:cd21315 87 VPQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4307-4344 |
3.21e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 52.10 E-value: 3.21e-08
10 20 30
....*....|....*....|....*....|....*...
gi 1072265250 4307 QRLLEAQACTGGIIDPITGEKFAVADAVNKGLVDKIMV 4344
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1031-2038 |
3.63e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 60.06 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1031 ELETIQKNLDKVNDKTRKVLAQPDLgdsgpllrSELDVTLHKMEQVHSMSSIYLDKLKTINLVIRNT--------HGAEE 1102
Cdd:TIGR00606 167 EGKALKQKFDEIFSATRYIKALETL--------RQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQitskeaqlESSRE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1103 VVKTYEDQLKEVQTvpgDLKELESSKADLKRMRGQVEGHQPLFNGLENDLTKAREVSERMLKVHSERDVDLERYREKVQL 1182
Cdd:TIGR00606 239 IVKSYENELDPLKN---RLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1183 LLERWQAIVlqievrQRELEQLGKQLRYYRESYEWLIRWITEAKKRQEKIQ-NVPITDSKTVKEQLmeekklleeseknR 1261
Cdd:TIGR00606 316 EKERELVDC------QRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQeHIRARDSLIQSLAT-------------R 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1262 GKVDECQKYAKQYIEaIKDFevqlvtykaqvEPVVSPLKKPKVHSASDNIIQEYVELRTKYSELTTLTSQYIKFITETLR 1341
Cdd:TIGR00606 377 LELDGFERGPFSERQ-IKNF-----------HTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIEL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1342 RLEEEERTAEKLK---EQERKKLAEVEDQLEKQRQLAEAHAQAkAVAEKEALELRMNMQEEVTRREvvAVDAEQQKKTIQ 1418
Cdd:TIGR00606 445 KKEILEKKQEELKfviKELQQLEGSSDRILELDQELRKAEREL-SKAEKNSLTETLKKEVKSLQNE--KADLDRKLRKLD 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1419 QELHQMknNSETEIKAKVKLIeeaeyNRKKVEEEIRIIRIQLETSQKQKSGAED--ELRALRARAEEAERQKKLAQEEAE 1496
Cdd:TIGR00606 522 QEMEQL--NHHTTTRTQMEML-----TKDKMDKDEQIRKIKSRHSDELTSLLGYfpNKKQLEDWLHSKSKEINQTRDRLA 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1497 RLRKQVKDEAQKKREAEDELHRKvqaekdaaREKQKALED--LEKFRLQAEEAERRMKQAELEKERQikqahDVAQQSAD 1574
Cdd:TIGR00606 595 KLNKELASLEQNKNHINNELESK--------EEQLSSYEDklFDVCGSQDEESDLERLKEEIEKSSK-----QRAMLAGA 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1575 AELQSKRMSFLEKTTQLEMSLKQEHI-TVTHLQEEAERLKKQQLEAETakeeaekelekwRQKANEAL--RLRLQAEEIA 1651
Cdd:TIGR00606 662 TAVYSQFITQLTDENQSCCPVCQRVFqTEAELQEFISDLQSKLRLAPD------------KLKSTESElkKKEKRRDEML 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1652 HKKTLAQEEAE-KQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIrlkaevdsgEQHRIV 1730
Cdd:TIGR00606 730 GLAPGRQSIIDlKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIM---------ERFQME 800
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1731 LEEDLFRLKNEVNE--AIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEaSKLRELAEEAARLrav 1808
Cdd:TIGR00606 801 LKDVERKIAQQAAKlqGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLK-SKTNELKSEKLQI--- 876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1809 SEEAKRQRQLAEedatrQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERL-------RRLAEDEAYQRKLLEE 1881
Cdd:TIGR00606 877 GTNLQRRQQFEE-----QLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELissketsNKKAQDKVNDIKEKVK 951
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1882 QAAQHKQDIEEKIHQ----LKQSSENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKnIADET 1957
Cdd:TIGR00606 952 NIHGYMKDIENKIQDgkddYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK-RENEL 1030
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1958 QKSKEKAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQL 2037
Cdd:TIGR00606 1031 KEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVM 1110
|
.
gi 1072265250 2038 A 2038
Cdd:TIGR00606 1111 R 1111
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2014-2165 |
4.01e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 59.12 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2014 KIKADeAKKQKDLAEKEAEKQIQLA---QDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSiyDKLKEEAEKAKRAAE 2090
Cdd:COG2268 196 EIIRD-ARIAEAEAERETEIAIAQAnreAEEAELEQEREIETARIAEAEAELAKKKAEERREA--ETARAEAEAAYEIAE 272
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072265250 2091 EAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEaakrgqAEQAALKLKQMADAE 2165
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAE------AEAEAIRAKGLAEAE 341
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2008-2610 |
4.28e-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: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2008 EEVERLKIKADEAKKQKDL---AEKEAEKQIQLAQDAARLKIDAEEKAYYAAvqQKEQEMLQTRIQEqsiydkLKEEAEK 2084
Cdd:COG4913 235 DDLERAHEALEDAREQIELlepIRELAERYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEE------LRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2085 AKRAAEEAErakikaeheAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAA--LKLKQMA 2162
Cdd:COG4913 307 LEAELERLE---------ARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLaaLGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2163 DAEM-----EKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKeevteslRQKKLVEeelfkvkiqmE 2237
Cdd:COG4913 378 SAEEfaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE-------RRKSNIP----------A 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2238 ELVKLKLRIEQEnkmliLKGKDNTQQFLAE-----EAEKMKQVAEEAA------RLSVEAQEAARLRKIAEDDLNEQRAL 2306
Cdd:COG4913 441 RLLALRDALAEA-----LGLDEAELPFVGElievrPEEERWRGAIERVlggfalTLLVPPEHYAAALRWVNRLHLRGRLV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2307 AEKIlkekMQAVQEASRLKAEAEMLqkqkemameqAKKLQED--------KEQMQQQL-------AEETEGFQKTLEAE- 2370
Cdd:COG4913 516 YERV----RTGLPDPERPRLDPDSL----------AGKLDFKphpfrawlEAELGRRFdyvcvdsPEELRRHPRAITRAg 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2371 ------RRRQLDI------------SAEA--ERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVV 2430
Cdd:COG4913 582 qvkgngTRHEKDDrrrirsryvlgfDNRAklAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2431 HTLEIQRQHSDKEAE--ELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQLRQETQtlqstfLTEKQILIQKEKYI 2508
Cdd:COG4913 662 DVASAEREIAELEAEleRLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE------LEQAEEELDELQDR 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2509 EEEKAKLEKLFDNEVGKAQKLKSEKERQLAQLEEEkrlLQTSMDDAMKKQLDAEDRIRQKQEELQQLDKKRQEQERLLEE 2588
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAALGDAVERELREN---LEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLE 812
|
650 660
....*....|....*....|..
gi 1072265250 2589 ENRKLRERLEQLEQEHRIALEK 2610
Cdd:COG4913 813 SLPEYLALLDRLEEDGLPEYEE 834
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1367-1579 |
4.90e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.66 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1367 QLEKQRQLAEAHAQAKAVAEKEALELRMNmqeevtrrevvaVDAEQQKktiQQELHQMKNNSETEIKAKVKLIEEAEYNR 1446
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQK------------QAAEQER---LKQLEKERLAAQEQKKQAEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1447 KKVEEEiriiriQLETSQKQKSGAEDELRALRARAEEAERQ-KKLAQEEAErlrKQVKDEAQKKREAEDELHRKVQAEKD 1525
Cdd:PRK09510 132 KQAEEA------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEAA---KKAAAEAKKKAEAEAAAKAAAEAKKK 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 1526 AAREKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQS 1579
Cdd:PRK09510 203 AEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1410-1580 |
5.80e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.32 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1410 AEQQKKTIQQELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKK 1489
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1490 LAQE-----EAERLRKQvKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKfrlqAEEAERRMKQ--AELEKERQI 1562
Cdd:TIGR02794 128 QAAEakakaEAEAERKA-KEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA----KAEAEAKAKAeeAKAKAEAAK 202
|
170
....*....|....*...
gi 1072265250 1563 KQAHDVAQQSADAELQSK 1580
Cdd:TIGR02794 203 AKAAAEAAAKAEAEAAAA 220
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1423-1615 |
6.18e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1423 QMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQV 1502
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1503 KDEAQKKREAEDELHRK---------------VQAEKDAAREKQKALEDLEKFR-LQAEEAERRMKQAELEKERQIKQAH 1566
Cdd:COG4942 100 EAQKEELAELLRALYRLgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEeLRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1072265250 1567 DVAQQSADAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQ 1615
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1100-1557 |
6.44e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1100 AEEVVKTYEDQLKEVQTVPGDLKELESSKADLKRMRGQVEGHQPLFNGLENDLTKAREVSERMLKVHSERDVDLERYREK 1179
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1180 VQLLLERWQAIVLQIEVRQRELEQLGKQLRYYRESYEWLIRWITEAKKRQEKIQNVPITDSKTVKEQLMEEKKLLEESEK 1259
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1260 NRGKVDEcqkyAKQYIEAIKDFEVQLVTYKAQVEPVVSPLKKPKVHSASDNIIQEYVELRTKYSELTTLTSQYIkfiteT 1339
Cdd:COG1196 482 LLEELAE----AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI-----V 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1340 LRRLEEEERTAEKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQQkktiqq 1419
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT------ 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1420 elhqmknnseteikAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLR 1499
Cdd:COG1196 627 --------------LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1072265250 1500 KQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELE 1557
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
169-264 |
6.89e-08 |
|
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: 54.23 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 169 KLLL-WSQRMSEGYqGLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNL-----------------------EN 224
Cdd:cd21224 3 SLLLkWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 225 LDQAFTVAER-----------ELG-VTRLLDPEDVDVPQPDEKSIITYVSSL 264
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2367-2627 |
7.50e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2367 LEAERRRQLD-ISAEAER-LKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKmtvvHTLEIQRQHSDKEA 2444
Cdd:COG1196 194 ILGELERQLEpLERQAEKaERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAEL----EELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2445 EELRKAIADLENEKEKLKKEAELLQKKSEEMQKaQKEQLRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLfDNEVG 2524
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQ-DIARLEERRRELEERLEELEEELAELEEELEELEEELEEL-EEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2525 KAQKLKSEKERQLAQLEEEKRLLQTSMDDAMKKQLDAEDRIRQKQEELQQLDKKRQEQERLLEEENRKLRERLEQLEQEH 2604
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
250 260
....*....|....*....|...
gi 1072265250 2605 RIALEKTREVIITKETVITQTKT 2627
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEE 450
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1350-1617 |
8.28e-08 |
|
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: 58.61 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1350 AEKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQQKKTIQQELHQMKNNSE 1429
Cdd:pfam09731 192 AEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDII 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1430 TEIKAKvKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEaerQKKLAQEEAERL-RKQVKDEAQK 1508
Cdd:pfam09731 272 PVLKED-NLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEE---LDKLAEELSARLeEVRAADEAQL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1509 KREAEdelhRKVQAEKDAAREKQKAleDLEKfrlQAEEAERRMKQAELEKERQIKQAHdvaQQSADAELQSKRMSFLEKT 1588
Cdd:pfam09731 348 RLEFE----REREEIRESYEEKLRT--ELER---QAEAHEEHLKDVLVEQEIELQREF---LQDIKEKVEEERAGRLLKL 415
|
250 260 270
....*....|....*....|....*....|
gi 1072265250 1589 TQLEMSLKQ-EHITVTHLQEEAERLKKQQL 1617
Cdd:pfam09731 416 NELLANLKGlEKATSSHSEVEDENRKAQQL 445
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2174-2499 |
8.67e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.60 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2174 EKTVRQKEQVEGELTKVKLQLEETDHQKAILDD---------ELGRLKEEVTESLRQ----KKLVEEElfkvKIQMEELV 2240
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERqqqekfekmEQERLRQEKEEKAREverrRKLEEAE----KARQAEMD 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2241 KLKLRIEQENKMLILKGKDNTQQFLAEEAEKMKQVAEEAArlsveAQEAARLRKIAEDDLNEQRAlaEKILKEKMQAVQE 2320
Cdd:pfam17380 331 RQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEI-----AMEISRMRELERLQMERQQK--NERVRQELEAARK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2321 ASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEgfQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAEE 2400
Cdd:pfam17380 404 VKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER--AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEK 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2401 DAKKfRKQAEDISEKLHQTELST--------KEKMTVVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKS 2472
Cdd:pfam17380 482 EKRD-RKRAEEQRRKILEKELEErkqamieeERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRK 560
|
330 340
....*....|....*....|....*..
gi 1072265250 2473 EEMQKAQKEQLRQETQTLQSTFLTEKQ 2499
Cdd:pfam17380 561 ATEERSRLEAMEREREMMRQIVESEKA 587
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2162-2402 |
9.19e-08 |
|
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: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2162 ADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELFKVKIQMEELVK 2241
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2242 -LKLRIEQENKMLILKGKDNTQQFLaEEAEKMKQVAEEAARLsVEAQEAARlrkiaeDDLNEQRALAEKILKEKMQAVQE 2320
Cdd:COG3883 94 aLYRSGGSVSYLDVLLGSESFSDFL-DRLSALSKIADADADL-LEELKADK------AELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2321 ASRLKAEAEMLQKQKEMAMEQakkLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAEE 2400
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQ---LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
..
gi 1072265250 2401 DA 2402
Cdd:COG3883 243 AA 244
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1481-1871 |
9.98e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 57.96 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1481 AEEAERQK-KLAQEEAERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKF--RLQAEEaERRMKQAELE 1557
Cdd:pfam02029 4 EEEAARERrRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFldRTAKRE-ERRQKRLQEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1558 KERQIKQAHDVAQQSADAELQSKRMSFLEKTTqlemslkqehitvthlqeeaerlkkqqleaetakeeaekelekWRQKA 1637
Cdd:pfam02029 83 LERQKEFDPTIADEKESVAERKENNEEEENSS-------------------------------------------WEKEE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1638 NEALRLRLQAEEIAHKKTlaQEEAEKQKEDAERETRKRTKAEEsalrQKDLAEEELEKQRKLAEETASHKLSAEQElirL 1717
Cdd:pfam02029 120 KRDSRLGRYKEEETEIRE--KEYQENKWSTEVRQAEEEGEEEE----DKSEEAEEVPTENFAKEEVKDEKIKKEKK---V 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1718 KAEVDSGEQHRIVLEE------DLFRLKNEVNEaiQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVE 1791
Cdd:pfam02029 191 KYESKVFLDQKRGHPEvksqngEEEVTKLKVTT--KRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1792 ASKLRELAEEAARLRAVSEEakRQRQLAEEDATRQRAEAERILKEkltainEATRMRTEAEIALKEKEAEnERLRRLAED 1871
Cdd:pfam02029 269 RQKQQEAELELEELKKKREE--RRKLLEEEEQRRKQEEAERKLRE------EEEKRRMKEEIERRRAEAA-EKRQKLPED 339
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
36-150 |
1.37e-07 |
|
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: 52.97 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 36 DAEDERDRVQKKTFTKWVNKHLikhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLP----REKGRMRFHKLQNVQI 111
Cdd:cd21222 8 DEAPEKLAEVKELLLQFVNKHL-----AKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKL 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 1072265250 112 ALDFLKLRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 150
Cdd:cd21222 83 ALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1395-1891 |
1.39e-07 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 57.73 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1395 NMQEEVTRREVVAVDAEQQKKTIQQELHQMKNNSEtEIKAKVKLIEEAEYNRKKVEE--EIRIIRIQLETSQKQKSGAED 1472
Cdd:pfam05701 46 KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIE-ELKLNLERAQTEEAQAKQDSElaKLRVEEMEQGIADEASVAAKA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1473 ELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEdelhRKVQAEKDAAREKQKALEDLekfrlqaeEAERRMK 1552
Cdd:pfam05701 125 QLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAI----KRAEEAVSASKEIEKTVEEL--------TIELIAT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1553 QAELEKERqikQAHDvaqqsaDAELQSKR--MSFLEKTTQLEMSLKQehitvthLQEEAERLKKQQLEAETAKEEAekel 1630
Cdd:pfam05701 193 KESLESAH---AAHL------EAEEHRIGaaLAREQDKLNWEKELKQ-------AEEELQRLNQQLLSAKDLKSKL---- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1631 ekwrqKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETrkrtkaeeSALRQKDLAEEELEKQRKLAEetashKLSA 1710
Cdd:pfam05701 253 -----ETASALLLDLKAELAAYMESKLKEEADGEGNEKKTST--------SIQAALASAKKELEEVKANIE-----KAKD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1711 EQELIRLKAEvdsgeqhriVLEEDLFRLKNEVnEAIQRRRG--------LEEELAKVRAEMEiLLKAKSKAeedsrsTSE 1782
Cdd:pfam05701 315 EVNCLRVAAA---------SLRSELEKEKAEL-ASLRQREGmasiavssLEAELNRTKSEIA-LVQAKEKE------ARE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1783 KSKQMleveASKLRELAEEAarlravsEEAKRQRQLAEEDATRQRAEAERilkekltAINEATRMRTEAEIALKEKEAEN 1862
Cdd:pfam05701 378 KMVEL----PKQLQQAAQEA-------EEAKSLAQAAREELRKAKEEAEQ-------AKAAASTVESRLEAVLKEIEAAK 439
|
490 500
....*....|....*....|....*....
gi 1072265250 1863 ERlRRLAEDEAyqRKLLEEQAAQHKQDIE 1891
Cdd:pfam05701 440 AS-EKLALAAI--KALQESESSAESTNQE 465
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2060-2447 |
1.40e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2060 KEQEMLQTRIQE-QSIYDKLKEEAEKAKR--AAEEAERAKIKAEH-EAALSRQQaeeaERLKQKAEIEAQakgqaQEDAE 2135
Cdd:PRK04863 240 RENRMTLEAIRVtQSDRDLFKHLITESTNyvAADYMRHANERRVHlEEALELRR----ELYTSRRQLAAE-----QYRLV 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2136 KVRKEAELEAAKRGQAEQAAlklkQMADAemekHKQFAEKTVRQKEQVE---GELTKVKLQLEEtdhQKAILDDelgrLK 2212
Cdd:PRK04863 311 EMARELAELNEAESDLEQDY----QAASD----HLNLVQTALRQQEKIEryqADLEELEERLEE---QNEVVEE----AD 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2213 EEVTESLRQKKLVEEELFKVK-----------------IQMEELVKLKLRIEQENKMLILkGKDNTQQFLAEEAEKMKQV 2275
Cdd:PRK04863 376 EQQEENEARAEAAEEEVDELKsqladyqqaldvqqtraIQYQQAVQALERAKQLCGLPDL-TADNAEDWLEEFQAKEQEA 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2276 AEE----AARLSVeAQEAAR--------LRKIAED---------------DLNEQRALAEKI---------LKEKMQAVQ 2319
Cdd:PRK04863 455 TEEllslEQKLSV-AQAAHSqfeqayqlVRKIAGEvsrseawdvarellrRLREQRHLAEQLqqlrmrlseLEQRLRQQQ 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2320 EASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAE 2399
Cdd:PRK04863 534 RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALA 613
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1072265250 2400 edakKFRKQ-------AEDISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAEEL 2447
Cdd:PRK04863 614 ----RLREQsgeefedSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1513-1931 |
1.42e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1513 EDELHRKVQA-EKDAAREKQKALEDLEKFRLQAEEAERRMKQ-AELEKERQIKQAHDVAQQSADAELQSKRMSfLEKTTQ 1590
Cdd:COG4717 48 LERLEKEADElFKPQGRKPELNLKELKELEEELKEAEEKEEEyAELQEELEELEEELEELEAELEELREELEK-LEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1591 LEMSLKQEHITVTHLQEEAERLK--KQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLaqEEAEKQKEDA 1668
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEelEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL--QDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1669 ERETRKRTKAEESALRQKDLAEEELEK-QRKLAEETASHKLSAEQELIRLKAEVDSGEQHR------------------- 1728
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGgsllsliltiagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1729 --IVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLR 1806
Cdd:COG4717 285 llALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1807 AVSEEAKRQRQLAEEDAT-----RQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKL--L 1879
Cdd:COG4717 365 LEELEQEIAALLAEAGVEdeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELeeL 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 1880 EEQAAQHKQDIEEKIHQLKQ-SSENELERQKTIVDETLKHRRVIEEEIRILKI 1931
Cdd:COG4717 445 EEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2007-2614 |
1.68e-07 |
|
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: 58.06 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2007 LEEVERLKIKADEAKKQKDLAEKEAEKqiqLAQDAARLKIDAEEKAYYA----AVQQKEQEMLQTRIQEQSI-------Y 2075
Cdd:TIGR00618 172 LFPLDQYTQLALMEFAKKKSLHGKAEL---LTLRSQLLTLCTPCMPDTYherkQVLEKELKHLREALQQTQQshayltqK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2076 DKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAA 2155
Cdd:TIGR00618 249 REAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2156 LKLKQMAD-AEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAiLDDELGRLKEEVTESLRQKKLVEEELfkvki 2234
Cdd:TIGR00618 329 KRAAHVKQqSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT-LTQHIHTLQQQKTTLTQKLQSLCKEL----- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2235 qmeelvkLKLRIEQENkmlilkgkdntqqflaEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEK 2314
Cdd:TIGR00618 403 -------DILQREQAT----------------IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2315 MQaVQEASRLKAEAEMLQkQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLE--AERRRQLDISAEAERLKLQVVEMS 2392
Cdd:TIGR00618 460 HL-QESAQSLKEREQQLQ-TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpNPARQDIDNPGPLTRRMQRGEQTY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2393 KSQAKAEEDAkkfrkQAEDISEKLHQTELSTKEkmtvvhTLEIQrqhsdkeaEELRKAIADlenekeklkkeaellQKKS 2472
Cdd:TIGR00618 538 AQLETSEEDV-----YHQLTSERKQRASLKEQM------QEIQQ--------SFSILTQCD---------------NRSK 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2473 EEMQKaqkeqLRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLFDNEVGKAQKLKSEKERQLAQLEEEKRLLQTSMD 2552
Cdd:TIGR00618 584 EDIPN-----LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE 658
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 2553 DAMKKQLDAEDRIRQKQEELQQLDKKRQEQERLLEEENRKLRERLEQLEQEHRIALEKTREV 2614
Cdd:TIGR00618 659 RVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREF 720
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1555-2285 |
1.77e-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: 57.91 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1555 ELEKERQIKQAhdvaqqsadaelQSKRMSFLE---KTTQLEmsLKQEHITVTHLQEE--AERLKKQQLEAETAKEEAEKE 1629
Cdd:pfam10174 40 ELKKERALRKE------------EAARISVLKeqyRVTQEE--NQHLQLTIQALQDElrAQRDLNQLLQQDFTTSPVDGE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1630 LEKWRQKANEALRLRLQAEeiaHKKTlAQEEAEKQKEDAERETRKRTkaeesalrQKDLAEEELEKQRKLAEETASHKLS 1709
Cdd:pfam10174 106 DKFSTPELTEENFRRLQSE---HERQ-AKELFLLRKTLEEMELRIET--------QKQTLGARDESIKKLLEMLQSKGLP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1710 A-----EQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKS 1784
Cdd:pfam10174 174 KksgeeDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1785 KQMLEVEASKL---RELAEEAARLRAVSEEAKRQRQLAEE-DATRQRAEAERI-LKEKL-TAINEATRMRTEAEIaLKEK 1858
Cdd:pfam10174 254 DEVQMLKTNGLlhtEDREEEIKQMEVYKSHSKFMKNKIDQlKQELSKKESELLaLQTKLeTLTNQNSDCKQHIEV-LKES 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1859 -EAENERLRRLAEDEAYQRKLLEEQAA--QHKQDIEEKIHQLKQSSENELERQKTIVDetLKHRRV------IEEEIRIL 1929
Cdd:pfam10174 333 lTAKEQRAAILQTEVDALRLRLEEKESflNKKTKQLQDLTEEKSTLAGEIRDLKDMLD--VKERKInvlqkkIENLQEQL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1930 KiNFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKqrqlalveearrkeaeekvkkIIAAEQEA-GRQRKVALE 2008
Cdd:pfam10174 411 R-DKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKER---------------------IIERLKEQrEREDRERLE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2009 EVERLKIKADEAKK-----QKDLAEKEAE----KQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQS------ 2073
Cdd:pfam10174 469 ELESLKKENKDLKEkvsalQPELTEKESSlidlKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKahnaee 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2074 -------IYDKLKEEAEKAKRAAEEAERAKIKAEH-EAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKeaelea 2145
Cdd:pfam10174 549 avrtnpeINDRIRLLEQEVARYKEESGKAQAEVERlLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN------ 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2146 AKRGQAEQAALKLKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRlKEEVTESLRQKKlv 2225
Cdd:pfam10174 623 IKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAE-KDGHLTNLRAER-- 699
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2226 eeelfkvKIQMEELVKLKlrieQENKMLILKGKDNTQQFLAEEAEKMKQVAEEAARLSVE 2285
Cdd:pfam10174 700 -------RKQLEEILEMK----QEALLAAISEKDANIALLELSSSKKKKTQEEVMALKRE 748
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2079-2341 |
1.88e-07 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 56.91 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2079 KEEAEK---AKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKG-----QAQEDAEKVRKEaELEAAKRGQ 2150
Cdd:PRK07735 19 KEEARKrlvAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAaalakQKREGTEEVTEE-EKAKAKAKA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2151 AEQAALKLKQMAdaemekhKQFAEKTvrqKEQVEGELTKVKLQLEETDHQKAildDELGRLKEEVTESLRQkklVEEELF 2230
Cdd:PRK07735 98 AAAAKAKAAALA-------KQKREGT---EEVTEEEKAAAKAKAAAAAKAKA---AALAKQKREGTEEVTE---EEEETD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2231 KVKIQMEELVKLKLRIEQENKMLILKGKDNTQQFLAEEAEKMKQVAEEAARLSVEA---QEAARLRKIAEDDLNEQRALA 2307
Cdd:PRK07735 162 KEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAAlakQKASQGNGDSGDEDAKAKAIA 241
|
250 260 270
....*....|....*....|....*....|....
gi 1072265250 2308 EKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQ 2341
Cdd:PRK07735 242 AAKAKAAAAARAKTKGAEGKKEEEPKQEEPSVNQ 275
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1354-1548 |
1.92e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.74 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1354 KEQERKKLAEveDQLEKQRQLAEAHAQAKAVAEKEalelRMNMQEEVTRREVVAVDAEQQKKTIQQELHQMKNNSETEIK 1433
Cdd:PRK09510 77 AEEQRKKKEQ--QQAEELQQKQAAEQERLKQLEKE----RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1434 AKVKLIEEAEynrKKVEEEIRIiRIQLETSQKQKSGAEDELRALRARAEEAERQKKlAQEEAErlrKQVKDEAQKKREAE 1513
Cdd:PRK09510 151 AEAKRAAAAA---KKAAAEAKK-KAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK-AEAEAK---KKAAAEAKKKAAAE 222
|
170 180 190
....*....|....*....|....*....|....*.
gi 1072265250 1514 -DELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAE 1548
Cdd:PRK09510 223 aKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1464-1722 |
2.04e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.74 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1464 QKQKSGAedelralrARAEEaeRQKKLAQEEAERLRKQVKDEAQKKREAEdelhrkvqAEKDAAREKQKaledlekfrlQ 1543
Cdd:PRK09510 68 QQQQKSA--------KRAEE--QRKKKEQQQAEELQQKQAAEQERLKQLE--------KERLAAQEQKK----------Q 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1544 AEEAERRMKQAELEKERQIKQAHDVAQQSADAElqSKRMSFLEKttqlemslkqehitvthlQEEAERLKKQQLEaetak 1623
Cdd:PRK09510 120 AEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAE--AKRAAAAAK------------------KAAAEAKKKAEAE----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1624 eeaekelekwrQKANEALRLRLQAEEIAHKKtlAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEET 1703
Cdd:PRK09510 175 -----------AAKKAAAEAKKKAEAEAAAK--AAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKA 241
|
250
....*....|....*....
gi 1072265250 1704 ASHKLSAEQELIRLKAEVD 1722
Cdd:PRK09510 242 AAAKAAEKAAAAKAAAEVD 260
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4039-4075 |
2.10e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 49.79 E-value: 2.10e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1072265250 4039 IRLLEAQIATGGIIDPEESHRLPVEMAYKRGLFDEEM 4075
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2180-2598 |
2.17e-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: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2180 KEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELFKVKIQMEELVKLK---LRIEQENKMLILK 2256
Cdd:pfam07888 54 NRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKdalLAQRAAHEARIRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2257 GKDNTQQFlaeeAEKMKQVAEEAARLSVEAQEAARLRKiaeDDLNEQRALAEKILkekmQAVQEASRLKAEAEMLQKQKE 2336
Cdd:pfam07888 134 LEEDIKTL----TQRVLERETELERMKERAKKAGAQRK---EEEAERKQLQAKLQ----QTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2337 MAMEQAKKLQEDKEQMQQQLAE------ETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAE 2410
Cdd:pfam07888 203 QRDTQVLQLQDTITTLTQKLTTahrkeaENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2411 DISEKLHQTELSTKEkmtvvhtleiQRQHSDKEAEELRkaiadlenekeklkkeaellqkKSEEMQKAQKEQLRQETQtl 2490
Cdd:pfam07888 283 QLTLQLADASLALRE----------GRARWAQERETLQ----------------------QSAEADKDRIEKLSAELQ-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2491 qstfltekqiliQKEKYIEEEKAKLEKLfdnEVgkaqKLKSEKERQLAQLEEEKRLLQtsmddamkkQLDAEDRIRQKQE 2570
Cdd:pfam07888 329 ------------RLEERLQEERMEREKL---EV----ELGREKDCNRVQLSESRRELQ---------ELKASLRVAQKEK 380
|
410 420
....*....|....*....|....*...
gi 1072265250 2571 ELQQLDKKRQEQERlleeenRKLRERLE 2598
Cdd:pfam07888 381 EQLQAEKQELLEYI------RQLEQRLE 402
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2129-2613 |
2.19e-07 |
|
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: 57.54 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2129 QAQEDAEKVRKEAELEAAKRGQAEQAALKL-------KQMADAEMEKHKQFAEKTVRQKEQVE--------------GEL 2187
Cdd:pfam12128 231 QAIAGIMKIRPEFTKLQQEFNTLESAELRLshlhfgyKSDETLIASRQEERQETSAELNQLLRtlddqwkekrdelnGEL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2188 TKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKklvEEELFKVKIQMEELvklklriEQENKMLILKGKDNTQQFLAE 2267
Cdd:pfam12128 311 SAADAAVAKDRSELEALEDQHGAFLDADIETAAAD---QEQLPSWQSELENL-------EERLKALTGKHQDVTAKYNRR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2268 EAEKMKQVAEEAARLSVEA----QEAARLRKIAEDDLNEQralaEKILKEKMQAVqeasrlKAEAEMLQKQKEMAMEQAK 2343
Cdd:pfam12128 381 RSKIKEQNNRDIAGIKDKLakirEARDRQLAVAEDDLQAL----ESELREQLEAG------KLEFNEEEYRLKSRLGELK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2344 kLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLklqvvemsksqAKAEEDAKKFRKQAEDISEKLHQTELST 2423
Cdd:pfam12128 451 -LRLNQATATPELLLQLENFDERIERAREEQEAANAEVERL-----------QSELRQARKRRDQASEALRQASRRLEER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2424 KEKMTVVHTLEIQRQHS-----DKEA----EELRKAIADLENEKEKLKKEAELLQKKSEemqkaqkeqlrqetQTLQSTF 2494
Cdd:pfam12128 519 QSALDELELQLFPQAGTllhflRKEApdweQSIGKVISPELLHRTDLDPEVWDGSVGGE--------------LNLYGVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2495 LTEKQILI----QKEKYIEEEKAKLEKLFDNEVGKAQKLksekERQLAQLEEEKRLLQTSMDDAMKKQLDAEDRIR---- 2566
Cdd:pfam12128 585 LDLKRIDVpewaASEEELRERLDKAEEALQSAREKQAAA----EEQLVQANGELEKASREETFARTALKNARLDLRrlfd 660
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1072265250 2567 QKQEELQQLDKKRQEQERLLEEENRKLRERLEQLEQEHRIALEKTRE 2613
Cdd:pfam12128 661 EKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKE 707
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1748-2094 |
2.22e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 57.18 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1748 RRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQR 1827
Cdd:pfam02029 19 RRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1828 AEAERILKEKLtaineatrmrTEAEIALKEKEAENERLRrlAEDEAYQRKLLEEQaaqhKQDIEEKIHQLKQssENELER 1907
Cdd:pfam02029 99 SVAERKENNEE----------EENSSWEKEEKRDSRLGR--YKEEETEIREKEYQ----ENKWSTEVRQAEE--EGEEEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1908 QKTIVDETLKHRRVIEEEIRILKINFEKASVGKSdlelelqklKNIADETQKSKEKAEQDAEKQRQLALVEEARRKEAEE 1987
Cdd:pfam02029 161 DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYES---------KVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1988 KVKKIiaaeQEAGRQRKVALEEVERLKIKADEAKKQKdlAEKEAEKQIQLAQDAARLKIDAEE--KAYYAAVQQKEQEML 2065
Cdd:pfam02029 232 QSQER----EEEAEVFLEAEQKLEELRRRRQEKESEE--FEKLRQKQQEAELELEELKKKREErrKLLEEEEQRRKQEEA 305
|
330 340
....*....|....*....|....*....
gi 1072265250 2066 QTRIQEQSIYDKLKEEAEkaKRAAEEAER 2094
Cdd:pfam02029 306 ERKLREEEEKRRMKEEIE--RRRAEAAEK 332
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1409-1577 |
2.46e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.93 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1409 DAEQQKKTIQ-QELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQ 1487
Cdd:COG1579 2 MPEDLRALLDlQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1488 KKLA--QEEAERLRKQVKDEAQKKREAED---ELHRKVQAEKDAAREKQKALEDLEKfRLQAEEAERRMKQAELEKER-Q 1561
Cdd:COG1579 82 LGNVrnNKEYEALQKEIESLKRRISDLEDeilELMERIEELEEELAELEAELAELEA-ELEEKKAELDEELAELEAELeE 160
|
170
....*....|....*.
gi 1072265250 1562 IKQAHDVAQQSADAEL 1577
Cdd:COG1579 161 LEAEREELAAKIPPEL 176
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1437-1563 |
2.72e-07 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 57.07 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1437 KLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRAR--------AEEAERQKKLAQEEAERLRKQVkdeaqk 1508
Cdd:COG1193 518 KLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEkeeilekaREEAEEILREARKEAEELIREL------ 591
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1072265250 1509 kreaedelhRKVQAEKDAAREKQKALEDLEKfRLQAEEAERRMKQAELEKERQIK 1563
Cdd:COG1193 592 ---------REAQAEEEELKEARKKLEELKQ-ELEEKLEKPKKKAKPAKPPEELK 636
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2168-2517 |
2.82e-07 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 56.65 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2168 KHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEvtESLRQKKLVE---EELFKVKIQMEELvklkl 2244
Cdd:pfam03528 1 QPDEDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEE--DLKRQNAVLQeaqVELDALQNQLALA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2245 RIEQENKMLILKGKDNTQQFLAEEAEKmkQVAEEAARLSVEAQEAARLRKIA-EDDLNEQRALAEKILKEKMQAVQEASR 2323
Cdd:pfam03528 74 RAEMENIKAVATVSENTKQEAIDEVKS--QWQEEVASLQAIMKETVREYEVQfHRRLEQERAQWNQYRESAEREIADLRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2324 LKAEA---EMLQKQKEMAMEQAKKLQEDKEQMQQQLAE------ETEGFQKTLEAERRRQLDISAEAER-----LKLQVV 2389
Cdd:pfam03528 152 RLSEGqeeENLEDEMKKAQEDAEKLRSVVMPMEKEIAAlkakltEAEDKIKELEASKMKELNHYLEAEKscrtdLEMYVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2390 EMSKSQAKAEEDAKKFRKQAEDISEKLhqtELSTKEKMTVVHTLEiqrQHSDKEAEELRKAIADLENEKE--KLKKEAEL 2467
Cdd:pfam03528 232 VLNTQKSVLQEDAEKLRKELHEVCHLL---EQERQQHNQLKHTWQ---KANDQFLESQRLLMRDMQRMESvlTSEQLRQV 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2468 LQKKSEEMQKAQKEQLRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEK 2517
Cdd:pfam03528 306 EEIKKKDQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPLSN 355
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2011-2404 |
2.94e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 56.59 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2011 ERLKIKADEAKKQKDLAEKEAEKQI-QLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAA 2089
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAEAEKRAaAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2090 EEA----------ERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEA--AKRGQAEQAALK 2157
Cdd:COG3064 83 EKAaaeaekkaaaEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAaaKAEAEAARAAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2158 LKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELFKVKIQME 2237
Cdd:COG3064 163 AAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2238 ELVKLKLRIEQENKMLILKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQA 2317
Cdd:COG3064 243 AALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2318 VQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAK 2397
Cdd:COG3064 323 AAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLG 402
|
....*..
gi 1072265250 2398 AEEDAKK 2404
Cdd:COG3064 403 LRLDLGA 409
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1792-2574 |
3.10e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1792 ASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAErilkekltainEATRMRTEAEIALkekEAENERLRRLAED 1871
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELA-----------ELNEAESDLEQDY---QAASDHLNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1872 EAYQRKL---------LEEQAAQHKQDIEEkIHQLKQSSENELERQKTIVDETLKH-----RRVIEEEIRILKIN----- 1932
Cdd:PRK04863 344 LRQQEKIeryqadleeLEERLEEQNEVVEE-ADEQQEENEARAEAAEEEVDELKSQladyqQALDVQQTRAIQYQqavqa 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1933 FEKASVGKSDLELELQKLKNIADE-TQKSKEKAEQDAEKQRQLALveearrkeaeekvkkiiaaEQEAGRQRKVALEEVE 2011
Cdd:PRK04863 423 LERAKQLCGLPDLTADNAEDWLEEfQAKEQEATEELLSLEQKLSV-------------------AQAAHSQFEQAYQLVR 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2012 RL--KIKADEAKKQKDLAEKEAEKQIQLAQ--DAARLKIDAEEKAYyaaVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKR 2087
Cdd:PRK04863 484 KIagEVSRSEAWDVARELLRRLREQRHLAEqlQQLRMRLSELEQRL---RQQQRAERLLAEFCKRLGKNLDDEDELEQLQ 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2088 AAEEAERAKIKAEHEAALSRQQAEEAE---------RLKQKAE--IEAQAK--------GQAQEDAEKV--------RKE 2140
Cdd:PRK04863 561 EELEARLESLSESVSEARERRMALRQQleqlqariqRLAARAPawLAAQDAlarlreqsGEEFEDSQDVteymqqllERE 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2141 AELE------AAKRGQAEQAALKLKQMADAEMEKHKQFAektvrqkEQVEGELTK-----VKLQ--------LEETDHqk 2201
Cdd:PRK04863 641 RELTverdelAARKQALDEEIERLSQPGGSEDPRLNALA-------ERFGGVLLSeiyddVSLEdapyfsalYGPARH-- 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2202 AILDDELGRLKEEVTE----------------SLRQKKLVEEELFKVKIQmeELVKLKLRIEQENKMLILkGKDNTQQFL 2265
Cdd:PRK04863 712 AIVVPDLSDAAEQLAGledcpedlyliegdpdSFDDSVFSVEELEKAVVV--KIADRQWRYSRFPEVPLF-GRAAREKRI 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2266 AEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALA-----EKILKEKMQAVQEASRLKAEAEMLQKQKEMAME 2340
Cdd:PRK04863 789 EQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALADHESQEQQQRSQLE 868
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2341 QAKKLQEDKEQMQQQ---LAEETegFQKTLEaERRRQLDISAEAERLKLQ----VVEMSKSQAKAEEDAKKF---RKQAE 2410
Cdd:PRK04863 869 QAKEGLSALNRLLPRlnlLADET--LADRVE-EIREQLDEAEEAKRFVQQhgnaLAQLEPIVSVLQSDPEQFeqlKQDYQ 945
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2411 DISEKLHQtelsTKEKMTVVHTLEIQRQH-SDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQLRQETQ- 2488
Cdd:PRK04863 946 QAQQTQRD----AKQQAFALTEVVQRRAHfSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQv 1021
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2489 --TLQSTFLTEKQILIQKEKYIE----------EEKAKL--EKLfDNEVGKAQKLKSEKERQLAQLEEEkrllqtsMDDA 2554
Cdd:PRK04863 1022 laSLKSSYDAKRQMLQELKQELQdlgvpadsgaEERARArrDEL-HARLSANRSRRNQLEKQLTFCEAE-------MDNL 1093
|
890 900
....*....|....*....|
gi 1072265250 2555 MKKQLDAEDRIRQKQEELQQ 2574
Cdd:PRK04863 1094 TKKLRKLERDYHEMREQVVN 1113
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2059-2453 |
3.17e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2059 QKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVR 2138
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2139 KEAELEAAKRgqaeqaalKLKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTES 2218
Cdd:COG4717 154 RLEELRELEE--------ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2219 LRQKKLVEEELFKVKIQmEELVKLKLRIEQENKMLILKGKDNTQQFLAEE---------------AEKMKQVAEEAARLS 2283
Cdd:COG4717 226 EEELEQLENELEAAALE-ERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2284 VEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQ---MQQQLAEET 2360
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2361 EGFQKTLEAERRRQlDISAEAERLKLQVVEMSKS--QAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQRQ 2438
Cdd:COG4717 385 EELRAALEQAEEYQ-ELKEELEELEEQLEELLGEleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
410
....*....|....*..
gi 1072265250 2439 H--SDKEAEELRKAIAD 2453
Cdd:COG4717 464 QleEDGELAELLQELEE 480
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1786-2412 |
3.24e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1786 QMLE-----VEASKLRELAEEAARLRAVSEEAKRQR-QLAEEDATRQRAEAERILKEKLTAINEATRMRTeAEIALKEKE 1859
Cdd:COG4913 216 YMLEepdtfEAADALVEHFDDLERAHEALEDAREQIeLLEPIRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1860 AENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVG 1939
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1940 KSDLELELQKLKNIADETQKSKEKAEQDAEKQRQlalveearrkeaeekvkKIIAAEQEAGRQRKVALEEVERLK----- 2014
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALA-----------------EAEAALRDLRRELRELEAEIASLErrksn 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2015 IKADEAKKQKDLAEkeaekqiQLAQDAARLKIDAE----------------------------EKAYYAAVQQK-EQEML 2065
Cdd:COG4913 438 IPARLLALRDALAE-------ALGLDEAELPFVGElievrpeeerwrgaiervlggfaltllvPPEHYAAALRWvNRLHL 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2066 QTRIQeqsiYDKLKEEAEKAKRAAEE----AERAKIKaEHEAAlsrqqaeeaERLKQkaEIEAQAkgqaqeDAEKVRKEA 2141
Cdd:COG4913 511 RGRLV----YERVRTGLPDPERPRLDpdslAGKLDFK-PHPFR---------AWLEA--ELGRRF------DYVCVDSPE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2142 ELEAAKRGqaeqaalklkqMADAEMEKHKqfaeKTVRQKeQVEGELTKvKLQL-EETDHQKAILDDELGRLKEEVTEslr 2220
Cdd:COG4913 569 ELRRHPRA-----------ITRAGQVKGN----GTRHEK-DDRRRIRS-RYVLgFDNRAKLAALEAELAELEEELAE--- 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2221 qkklVEEELFKVKIQMEELVKLKLRIEQenkmlilkgkdntQQFLAEEAEKMKQVAEEAARLSveaQEAARLRKiAEDDL 2300
Cdd:COG4913 629 ----AEERLEALEAELDALQERREALQR-------------LAEYSWDEIDVASAEREIAELE---AELERLDA-SSDDL 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2301 NEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQkemaMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAE 2380
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
650 660 670
....*....|....*....|....*....|..
gi 1072265250 2381 AERLKLQvveMSKSQAKAEEDAKKFRKQAEDI 2412
Cdd:COG4913 764 ERELREN---LEERIDALRARLNRAEEELERA 792
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3798-3836 |
3.31e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 49.25 E-value: 3.31e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1072265250 3798 LLDAQLTTGGVIDPRFGFHIPNETAYMRGYLNKETLDML 3836
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1351-1592 |
3.91e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1351 EKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALElrmnmqEEVTRREVVAVDAEQqkktIQQELHQMKNNSET 1430
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE------EEVSRIEARLREIEQ----KLNRLTLEKEYLEK 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1431 EIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQ--------------KQKSGAEDELRALRARAEEAERQKKLAQEEAE 1496
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEeeleeleaalrdleSRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1497 RLRKQVKDEAQKKREAEDELhRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQqsADAE 1576
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK--RLDE 990
|
250
....*....|....*.
gi 1072265250 1577 LQSKRMSFLEKTTQLE 1592
Cdd:TIGR02169 991 LKEKRAKLEEERKAIL 1006
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1525-2123 |
4.06e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1525 DAAREKQKALEDLEKFRLQAEEAERRMKQaeLEKERQIKQAHDVAQQSADaelqskrmsflekttqlemslkqehitvtH 1604
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIEL--LEPIRELAERYAAARERLA-----------------------------E 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1605 LQEEAERLKKQQleaetakeeaekelekwRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAE--ESA 1682
Cdd:COG4913 274 LEYLRAALRLWF-----------------AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirGNG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1683 LRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGE-----------QHRIVLEEDLFRLKNEVNEAIQRRRG 1751
Cdd:COG4913 337 GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaalraeaaALLEALEEELEALEEALAEAEAALRD 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1752 LEEELAKVRAEMEILLKAKSKAEEDsrstsekskqMLEVEASKLRELAEEAARLRAVSEEAkrqrQLAEEDATRQRAeAE 1831
Cdd:COG4913 417 LRRELRELEAEIASLERRKSNIPAR----------LLALRDALAEALGLDEAELPFVGELI----EVRPEEERWRGA-IE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1832 RIL--------------KEKLTAINE---ATRMRTEaeialKEKEAENERLRRLAEDEAYQRKL-LEEQAAQH--KQDIE 1891
Cdd:COG4913 482 RVLggfaltllvppehyAAALRWVNRlhlRGRLVYE-----RVRTGLPDPERPRLDPDSLAGKLdFKPHPFRAwlEAELG 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1892 EKIHQLKQSSENELERQKTIVDET--LKH---RRVIEEEIRILKINF--EKASVGKSDLELELQKLKNIADETQKSKEKA 1964
Cdd:COG4913 557 RRFDYVCVDSPEELRRHPRAITRAgqVKGngtRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEAL 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1965 EQDAEKQRQLALVEEARRKEAEEKVKkiIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEkQIQLAQDAARL 2044
Cdd:COG4913 637 EAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELE-ELEEELDELKG 713
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072265250 2045 KIDAEEKAYYAAVQQKEQemLQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIE 2123
Cdd:COG4913 714 EIGRLEKELEQAEEELDE--LQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2000-2452 |
4.34e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2000 GRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIYDKLK 2079
Cdd:COG4717 63 GRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2080 EEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAEleaAKRGQAEQAALKLK 2159
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ---QRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2160 QMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLrqkkLVEEELFKVKIQMEEL 2239
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL----FLVLGLLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2240 VKLKLRIEQENKMLILKGKDNTQQFLAEEAEK-MKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAV 2318
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAAlGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2319 QEASRLKAEAEMLQKQKemAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAerrrqldisAEAERLKLQVVEMSKSQAKA 2398
Cdd:COG4717 376 LAEAGVEDEEELRAALE--QAEEYQELKEELEELEEQLEELLGELEELLEA---------LDEEELEEELEELEEELEEL 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 2399 EEDAKKFRKQAEDISEKLHQTELSTKekmtvVHTLEIQRQHSDKEAEELRKAIA 2452
Cdd:COG4717 445 EEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAELRELAEEWA 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1629-2387 |
4.74e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.67 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1629 ELEKWRQKANEaLRLRLQAEEIAHKK----------TLAQEEAEKQKE-DAERETRKRTKAEESALRQ------------ 1685
Cdd:pfam15921 79 VLEEYSHQVKD-LQRRLNESNELHEKqkfylrqsviDLQTKLQEMQMErDAMADIRRRESQSQEDLRNqlqntvheleaa 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1686 KDLAEEELEKQRKLAEETASHKLSAE---QELIRLKAEVDSGEQHRIVLEEDL----FR--------LKNEVNEAIQRRR 1750
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMstmhFRslgsaiskILRELDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1751 G----LEEELAKVRAEmeillkAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQ 1826
Cdd:pfam15921 238 GrifpVEDQLEALKSE------SQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1827 RAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQL-----KQSS 1901
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1902 ENELERQ--KTIVDETLKHRRVIEEEIRILkinfekasvgkSDLELELQKLkniadETQKSKEKAEQDAEKQRQLALVee 1979
Cdd:pfam15921 392 ELSLEKEqnKRLWDRDTGNSITIDHLRREL-----------DDRNMEVQRL-----EALLKAMKSECQGQMERQMAAI-- 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1980 ARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQ-KDLAEKEAEKQiqlaqdAARLKIDAEEKAYYAAVQ 2058
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTvSDLTASLQEKE------RAIEATNAEITKLRSRVD 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2059 QKEQEMlqtriqeqsiyDKLKEEAEKAKRAAEEAErakikaeheaALSRQQAEE---AERLKQKAEIEAQAKGQAQEDAE 2135
Cdd:pfam15921 528 LKLQEL-----------QHLKNEGDHLRNVQTECE----------ALKLQMAEKdkvIEILRQQIENMTQLVGQHGRTAG 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2136 KVRKE-AELEAakrgQAEQAALKLKQMADAEMEKHKQFAEKTVRQKEQvegELTKVKLQLEETDHQKAILD--DELGRLK 2212
Cdd:pfam15921 587 AMQVEkAQLEK----EINDRRLELQEFKILKDKKDAKIRELEARVSDL---ELEKVKLVNAGSERLRAVKDikQERDQLL 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2213 EEVTESLRQKKLVEEEL------FKVKIQMEELVKLKLRIEQENKMLILKGKDNTQQFL-AEEAEKMK-----QVAEEAA 2280
Cdd:pfam15921 660 NEVKTSRNELNSLSEDYevlkrnFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMeGSDGHAMKvamgmQKQITAK 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2281 RLSVEA-QEAARLRKIAEDDLNEQRALAEkilKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEE 2359
Cdd:pfam15921 740 RGQIDAlQSKIQFLEEAMTNANKEKHFLK---EEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA 816
|
810 820
....*....|....*....|....*...
gi 1072265250 2360 TEGFQKTLEAERRRQldisAEAERLKLQ 2387
Cdd:pfam15921 817 SLQFAECQDIIQRQE----QESVRLKLQ 840
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1351-1573 |
4.83e-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: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1351 EKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEAlelrmnmqEEVTRRevvAVDAEQQKKTIQQELHQMKNNSET 1430
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAA--------EKAAKQ---AEQAAKQAEEKQKQAEEAKAKQAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1431 EIKAKvkliEEAEYNRKKVEEEIRiiriQLETSQKQKSGAEDelralRARAEEAERQKKL-AQEEAERLRKQVKDEAQKK 1509
Cdd:TIGR02794 131 EAKAK----AEAEAERKAKEEAAK----QAEEEAKAKAAAEA-----KKKAEEAKKKAEAeAKAKAEAEAKAKAEEAKAK 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 1510 REAEdelhrKVQAEKDAAREKQKaledlEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSA 1573
Cdd:TIGR02794 198 AEAA-----KAKAAAEAAAKAEA-----EAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGG 251
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1101-1720 |
5.88e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1101 EEVVKTYEDQLKEVQTVPGDLKELESSKADLKRMRGQVEGHQPLFNGLENDLTKaREVSERMLKvhsERDVDLERYREKV 1180
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELES-LEGSKRKLE---EKIRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1181 QLLLERWQAIVLQIEvrqrELEQLGKQLRYYRESYEWLIRWITEAKKRQEKIQNvpitDSKTVKEQLMEEKKLLEESEKN 1260
Cdd:PRK03918 272 KKEIEELEEKVKELK----ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE----EINGIEERIKELEEKEERLEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1261 RGKVDECQK-------YAKQYiEAIKDFEVQLVTYKAQ-----VEPVVSPLKKpkVHSASDNIIQEYVELRTKYSELTTL 1328
Cdd:PRK03918 344 KKKLKELEKrleeleeRHELY-EEAKAKKEELERLKKRltgltPEKLEKELEE--LEKAKEEIEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1329 TSQYIKFITETLRRLEEEERTAEKLKEQERKKL-----AEVEDQLEKQRQLAEAHAQAKAVAEKeaLELRMNMQEEVTRR 1403
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCPVCGRELTEEHRKELleeytAELKRIEKELKEIEEKERKLRKELRE--LEKVLKKESELIKL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1404 EVVAvdaeQQKKTIQQELHqmKNNSEtEIKAKVKLIEEAEYNRKKVEEEIRIiriqLETSQKQKSGAEDELRALRARAEE 1483
Cdd:PRK03918 499 KELA----EQLKELEEKLK--KYNLE-ELEKKAEEYEKLKEKLIKLKGEIKS----LKKELEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1484 AERQKKLAQEEAERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEKERQIK 1563
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1564 QAHDVAQQSADAELQSKRMSFLEKTTQLEmslkqehitvtHLQEEAERLKKQqleaetakeeaekelekwRQKANEALR- 1642
Cdd:PRK03918 648 ELEELEKKYSEEEYEELREEYLELSRELA-----------GLRAELEELEKR------------------REEIKKTLEk 698
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072265250 1643 LRLQAEEIahkktlaqEEAEKQKEDAERETRKRTKAEESALRQKDLAEEE-LEKQRKLAEETASHKLSAEQELIRLKAE 1720
Cdd:PRK03918 699 LKEELEER--------EKAKKELEKLEKALERVEELREKVKKYKALLKERaLSKVGEIASEIFEELTEGKYSGVRVKAE 769
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1471-1838 |
5.90e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.92 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1471 EDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAE----- 1545
Cdd:pfam13868 5 SDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEeqiee 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1546 -EAERRMKQAELEKERQIKQAHDVAQQSADAELQSKRMsflekttQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKE 1624
Cdd:pfam13868 85 rEQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKL-------EKQRQLREEIDEFNEEQAEWKELEKEEEREEDERI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1625 EAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAEREtrkrtkaeesALRQKDLAEEELEKQRKLAEETA 1704
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERD----------ELRAKLYQEEQERKERQKEREEA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1705 SHKLSAEQELIRLKAEvdsgeqhrivleedlfrlknevnEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKS 1784
Cdd:pfam13868 228 EKKARQRQELQQAREE-----------------------QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKR 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 1785 KQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKL 1838
Cdd:pfam13868 285 RMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2103-2375 |
6.74e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2103 AALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRgqaeqaalklkQMADAEmekhkqfaektvRQKEQ 2182
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----------RIAALA------------RRIRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2183 VEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQkklveeeLFKvkiqMEELVKLKLRIEQENKMLILKGKDNTQ 2262
Cdd:COG4942 74 LEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA-------LYR----LGRQPPLALLLSPEDFLDAVRRLQYLK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2263 QFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQA 2342
Cdd:COG4942 143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
250 260 270
....*....|....*....|....*....|...
gi 1072265250 2343 KKLQEDKEQMQQQLAEETEGFQKTLEAERRRQL 2375
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1355-1925 |
6.85e-07 |
|
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: 55.91 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1355 EQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQQKktiQQELHQMKNNSETEIKA 1434
Cdd:pfam07111 79 EEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGS---QRELEEIQRLHQEQLSS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1435 KVKLIEEAeynrkkveeeiriiriqLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKdEAQKKREAED 1514
Cdd:pfam07111 156 LTQAHEEA-----------------LSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLS-KTQEELEAQV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1515 ELhrkvqaekdaarekqkaLEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADaelqskrmsfLEKTTQLEMS 1594
Cdd:pfam07111 218 TL-----------------VESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRAD----------LQATVELLQV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1595 LKQEHITVTHLQEEAERLKKQQLEAETAK--EEAEKELEKWRQKANeALRLRLQAEEIAHKKTLAQEEAEKqkedAERET 1672
Cdd:pfam07111 271 RVQSLTHMLALQEEELTRKIQPSDSLEPEfpKKCRSLLNRWREKVF-ALMVQLKAQDLEHRDSVKQLRGQV----AELQE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1673 RKRTKAEESALRQKDLAEE--ELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQH-----------RIVLEEDLFR-- 1737
Cdd:pfam07111 346 QVTSQSQEQAILQRALQDKaaEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQlkfvvnamsstQIWLETTMTRve 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1738 --------LKNEVNEAIQRR---RGL---EEELAKVRAE------------MEILLKAKSKAEEDSRSTSE--KSKQMLE 1789
Cdd:pfam07111 426 qavaripsLSNRLSYAVRKVhtiKGLmarKVALAQLRQEscpppppappvdADLSLELEQLREERNRLDAElqLSAHLIQ 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1790 VEASKLRELAE-EAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINEATRMRTE----AEI---ALKEKEAE 1861
Cdd:pfam07111 506 QEVGRAREQGEaERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQEltqqQEIygqALQEKVAE 585
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 1862 NE-RLRRLAEDEayQRKLLEEQAAQHKQDIEEKIHQLKQSSENELERQ-KTIVDETLKH------RRVIEEE 1925
Cdd:pfam07111 586 VEtRLREQLSDT--KRRLNEARREQAKAVVSLRQIQHRATQEKERNQElRRLQDEARKEegqrlaRRVQELE 655
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1966-2576 |
7.64e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1966 QDAEKQR-QLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEkQIQLAQDAARL 2044
Cdd:COG4913 245 EDAREQIeLLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE-RLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2045 KIDAEEKAYYAAVQQKEQEmLQTRIQEQSiyDKLKEEAEKAKRAAEEAERAKIKAEHEAA-LSRQQAEEAERLKQKAEIE 2123
Cdd:COG4913 324 ELDELEAQIRGNGGDRLEQ-LEREIERLE--RELEERERRRARLEALLAALGLPLPASAEeFAALRAEAAALLEALEEEL 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2124 AQAkgQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMA-DAEMEK-HKQFAEKTVRQKEQVE--GELTKVKlqLEETDH 2199
Cdd:COG4913 401 EAL--EEALAEAEAALRDLRRELRELEAEIASLERRKSNiPARLLAlRDALAEALGLDEAELPfvGELIEVR--PEEERW 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2200 QKAIlddelgrlkEEVTESLRQKKLVEEELFKVKIQMEELVKLKLRIeQENKMLILKGKDNTQQFLAEE-AEKMK----- 2273
Cdd:COG4913 477 RGAI---------ERVLGGFALTLLVPPEHYAAALRWVNRLHLRGRL-VYERVRTGLPDPERPRLDPDSlAGKLDfkphp 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2274 -------QVAEEAARLSVEAQEA------------------ARLRKIAEDDLNEQRAL---AEKILKEKMQAVQEASRLK 2325
Cdd:COG4913 547 frawleaELGRRFDYVCVDSPEElrrhpraitragqvkgngTRHEKDDRRRIRSRYVLgfdNRAKLAALEAELAELEEEL 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2326 AEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEE--TEGFQKT---LEAERRRQLDISAEAERLKLQVVEMSKSQAKAEE 2400
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEidVASAEREiaeLEAELERLDASSDDLAALEEQLEELEAELEELEE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2401 DAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLE-IQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQ 2479
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAE 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2480 kEQLRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLFDNEVgkAQKLKSEKERQLAQLEEEKRLLQTSMDDAMKkql 2559
Cdd:COG4913 787 -EELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGL--PEYEERFKELLNENSIEFVADLLSKLRRAIR--- 860
|
650
....*....|....*..
gi 1072265250 2560 DAEDRIRQKQEELQQLD 2576
Cdd:COG4913 861 EIKERIDPLNDSLKRIP 877
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1676-1908 |
8.31e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1676 TKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEE 1755
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1756 LAKVRAEMEILLKAKSKaeedsrsTSEKSKQMLEVEASKLRELAEEAARLRAVSEEakRQRQLAEEDATRQRAEAERilk 1835
Cdd:COG4942 99 LEAQKEELAELLRALYR-------LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA--RREQAEELRADLAELAALR--- 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 1836 ekltaiNEATRMRTEAEIALKEKEAEnerLRRLAEDEAYQRKLLEEQAAQHKQDiEEKIHQLKQsSENELERQ 1908
Cdd:COG4942 167 ------AELEAERAELEALLAELEEE---RAALEALKAERQKLLARLEKELAEL-AAELAELQQ-EAEELEAL 228
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1362-1579 |
8.96e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.47 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1362 AEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQQKKTIQQELhqmknnSETEIKAKVKLIEE 1441
Cdd:TIGR02794 40 AVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAA------AEKAAKQAEQAAKQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1442 AEYNRKKVEEEiriiRIQLETSQKQKSGAEDELRALRARAEEAErQKKLAQEEAERLRKQvkDEAQKKREAEDElhRKVQ 1521
Cdd:TIGR02794 114 AEEKQKQAEEA----KAKQAAEAKAKAEAEAERKAKEEAAKQAE-EEAKAKAAAEAKKKA--EEAKKKAEAEAK--AKAE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1072265250 1522 AEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQS 1579
Cdd:TIGR02794 185 AEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLAS 242
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1722-2133 |
9.24e-07 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 55.40 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1722 DSGEQHRIVLEEDLFRLKNEVNEAIQRRR-----GLEEELAKVRAEM---EILLKAKSKAEEDSRSTSEKS-------KQ 1786
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKhtqnvALNKKLSDIKTEYlyeLNVLKEKSEAELTSKTKKELDaafeqfkKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1787 MLEV-----EASKLRELAEEAARlrAVSEEAKR----------QRQLAEEDATRQRAEAERILKEKLTAINEATRMRTEA 1851
Cdd:NF033838 134 TLEPgkkvaEATKKVEEAEKKAK--DQKEEDRRnyptntyktlELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1852 EIalKEKEAENERLRRLAEDeayqRKLLEEQAaQHKQDIEEKIHQLKQSSENELERQKTIVdetlkHRRVIEEEIRI-LK 1930
Cdd:NF033838 212 KV--ESKKAEATRLEKIKTD----REKAEEEA-KRRADAKLKEAVEKNVATSEQDKPKRRA-----KRGVLGEPATPdKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1931 INFEKA---SVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQR-----------------QLALVEEARRKEAEEKVK 1990
Cdd:NF033838 280 ENDAKSsdsSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKeedrrnyptntyktlelEIAESDVKVKEAELELVK 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1991 KIiAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTriq 2070
Cdd:NF033838 360 EE-AKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKP--- 435
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072265250 2071 eqsiyDKLKEEAEKAKRAAEEAER--AKIKAEHEAALSRQQAEEAERlkqKAEIEAQAKGQAQED 2133
Cdd:NF033838 436 -----EKPAEQPKAEKPADQQAEEdyARRSEEEYNRLTQQQPPKTEK---PAQPSTPKTGWKQEN 492
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4142-4170 |
9.71e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.09 E-value: 9.71e-07
10 20
....*....|....*....|....*....
gi 1072265250 4142 IVDPETGKEMSVYEAYRKGLIDHQTYIEL 4170
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2107-2639 |
9.95e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.51 E-value: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2107 RQQAEEAERLKQKAEIEAQA-------KGQAQEDAEKVRKEA--ELEAAKrgqaeqaALKLKQMADAEMEKHKqfAEKTV 2177
Cdd:pfam15921 109 RQSVIDLQTKLQEMQMERDAmadirrrESQSQEDLRNQLQNTvhELEAAK-------CLKEDMLEDSNTQIEQ--LRKMM 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2178 RQKEQVEGELTKVKLQLEETDHQKAILDDELG-----RLKEEVTESLRQK----KLVEEELFKVKIQMEelvklKLRIEQ 2248
Cdd:pfam15921 180 LSHEGVLQEIRSILVDFEEASGKKIYEHDSMStmhfrSLGSAISKILRELdteiSYLKGRIFPVEDQLE-----ALKSES 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2249 ENKM--LILKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAV-------Q 2319
Cdd:pfam15921 255 QNKIelLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVsqlrselR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2320 EASRL-KAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAER--------------- 2383
Cdd:pfam15921 335 EAKRMyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQnkrlwdrdtgnsiti 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2384 -----------LKLQVVE-----------------MSKSQAKAE--EDAKKFRKQAEDISEKLHQT-ELSTKEKMTV--- 2429
Cdd:pfam15921 415 dhlrrelddrnMEVQRLEallkamksecqgqmerqMAAIQGKNEslEKVSSLTAQLESTKEMLRKVvEELTAKKMTLess 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2430 ---VHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKE------QLRQE---TQTLQSTFLTE 2497
Cdd:pfam15921 495 ertVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealklQMAEKdkvIEILRQQIENM 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2498 KQILIQKEKY---IEEEKAKLEKLFDNEVGKAQKLKSEKERQLAQLEE-EKR-----LLQTSMDDAMKKQLDAEDRIRQK 2568
Cdd:pfam15921 575 TQLVGQHGRTagaMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRElEARvsdleLEKVKLVNAGSERLRAVKDIKQE 654
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072265250 2569 QEELQQLDKKRQEQERLLEEENRKLRERLEQLEQEHRIALEKTREVIITKETVITQTKTMPNGRDAADGSA 2639
Cdd:pfam15921 655 RDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHA 725
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2805-2841 |
1.01e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.86 E-value: 1.01e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1072265250 2805 IRLLEAQIATGGIVDPVNSHRLPLDVAYKRGYFDEEM 2841
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1355-1695 |
1.01e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 54.27 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1355 EQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQQKKtiQQELHQMKNNSETEIKA 1434
Cdd:pfam15558 35 EELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESR--WREQAEDQENQRQEKLE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1435 KVKLIEEA-----EYNRKKVEEEIRIIRIQLETSQKQKsgaedELRALRARAEEAERQKKLAQEE--AERLRKQVKDEAQ 1507
Cdd:pfam15558 113 RARQEAEQrkqcqEQRLKEKEEELQALREQNSLQLQER-----LEEACHKRQLKEREEQKKVQENnlSELLNHQARKVLV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1508 KKREAEDELHRKVQAEkdaarekQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQSKRMSFLEK 1587
Cdd:pfam15558 188 DCQAKAEELLRRLSLE-------QSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERQEHKEALAELA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1588 TTQLEMSLKQEHITVthlQEEAERLKKQQLEaetakeeaekelekwRQKANEALRLRLQAEEIAHKKTLaqeeaekqKED 1667
Cdd:pfam15558 261 DRKIQQARQVAHKTV---QDKAQRARELNLE---------------REKNHHILKLKVEKEEKCHREGI--------KEA 314
|
330 340
....*....|....*....|....*...
gi 1072265250 1668 AERETRKRtkaeESALRQKDLAEEELEK 1695
Cdd:pfam15558 315 IKKKEQRS----EQISREKEATLEEARK 338
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1224-1564 |
1.04e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.13 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1224 EAKKRQEKIQNVPITDSKTVKEQLMEEKKLLEESEKNRGKvdECQKYAKQYIEAikdfEVQLVTYKAQVEPVVSPLKKPK 1303
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQA--EMDRQAAIYAEQ----ERMAMERERELERIRQEERKRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1304 VhsasDNIIQEyvELRTKYSELTTLtsqyikfitetlrrleeeertaEKLKEQERKKLAEVEDQLEKQR--QLAEAHAQA 1381
Cdd:pfam17380 362 L----ERIRQE--EIAMEISRMREL----------------------ERLQMERQQKNERVRQELEAARkvKILEEERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1382 KAVAEKEALELRMNMQEEVTRREVVAVDAEQQKKTIQQELHQMKNNSETEIKAKvkliEEAEYNRKKVEEEiRIIRIQLE 1461
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQ----QEEERKRKKLELE-KEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1462 TSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEaQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFR 1541
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-ERRREAEEERRKQQEMEERRRIQEQMRKATEERSR 567
|
330 340
....*....|....*....|...
gi 1072265250 1542 LQAEEAERRMKQAELEKERQIKQ 1564
Cdd:pfam17380 568 LEAMEREREMMRQIVESEKARAE 590
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1746-2358 |
1.06e-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: 55.13 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1746 IQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKsKQMLEVEASKLRELAEEA-ARLRAVSEEAKRQRQLAE---- 1820
Cdd:pfam05557 12 SQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDR-NQELQKRIRLLEKREAEAeEALREQAELNRLKKKYLEalnk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1821 --EDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRlaedeayQRKLLEEQAAQHKQDIEEKIHQLK 1898
Cdd:pfam05557 91 klNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQE-------RLDLLKAKASEAEQLRQNLEKQQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1899 QSSENELERQktivdetlkhrrvieeeirilkinfekasvgksDLELELQKLKNIADETQKSKEKAEQDAEKQRQLALVE 1978
Cdd:pfam05557 164 SLAEAEQRIK---------------------------------ELEFEIQSQEQDSEIVKNSKSELARIPELEKELERLR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1979 EARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAE-KEAEKQIQLAQDAARLKIDAEEKayyaaV 2057
Cdd:pfam05557 211 EHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQElQSWVKLAQDTGLNLRSPEDLSRR-----I 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2058 QQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKV 2137
Cdd:pfam05557 286 EQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2138 RKEAELEAAkrgqAEQAALKLKQMADAEMEKHKQFAEKTVrQKEQVEGELTKVKLQLeetdhqkAILDDELGRLKEEvtE 2217
Cdd:pfam05557 366 DKELTMSNY----SPQLLERIEEAEDMTQKMQAHNEEMEA-QLSVAEEELGGYKQQA-------QTLERELQALRQQ--E 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2218 SLRQKKLVEEELFKVKIQMEELVKLKLRIEQENKMLILK------------GKDNTQQFLAEEAEKMKQV-AEEAARLSV 2284
Cdd:pfam05557 432 SLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMElerrclqgdydpKKTKVLHLSMNPAAEAYQQrKNQLEKLQA 511
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 2285 EAQEAARLRKIAEDDLneqralaekilkEKMQAVQEASRLKAEAEMLQKQKEMAmEQAKKLQEDKEQMQQQLAE 2358
Cdd:pfam05557 512 EIERLKRLLKKLEDDL------------EQVLRLPETTSTMNFKEVLDLRKELE-SAELKNQRLKEVFQAKIQE 572
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
40-152 |
1.19e-06 |
|
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: 50.77 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 40 ERDRVQKKTFTKWVNKHLIkhwraeaQRHVNDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQ 110
Cdd:cd21331 18 EGETREERTFRNWMNSLGV-------NPHVNHLYGDLQDALVILQLYEKIkvpvdwnkvNKPPYPKLGANMK--KLENCN 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1072265250 111 IALDFLKLR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 152
Cdd:cd21331 89 YAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1407-1581 |
1.26e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.04 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1407 AVDAEQQKKTIQQ----ELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRiiriqlETSQKQKSGAEDELRALRARAE 1482
Cdd:PRK09510 74 AKRAEEQRKKKEQqqaeELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAK------QAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1483 EAERQKKLAQEEA----ERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEK 1558
Cdd:PRK09510 148 KAEAEAKRAAAAAkkaaAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAA 227
|
170 180
....*....|....*....|...
gi 1072265250 1559 ERQIKQAHDVAQQSADAELQSKR 1581
Cdd:PRK09510 228 AKAAAEAKAAAEKAAAAKAAEKA 250
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1959-2168 |
1.28e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.95 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1959 KSKEKAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQLA 2038
Cdd:PRK05035 472 RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2039 QDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEE---AERAKIKAEHEAALSRQQAeeaer 2115
Cdd:PRK05035 552 AAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEeqvAEVDPKKAAVAAAIARAKA----- 626
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 2116 lkQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMADAEMEK 2168
Cdd:PRK05035 627 --KKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKK 677
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2033-2171 |
1.40e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 55.02 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2033 KQIQLAqdaarlkIDAEEKAYYAAVQQ----KEQEMlQTRIQEQSIYDKLKEEAEK-------AKRAAEEAE---RAKIK 2098
Cdd:PTZ00491 651 KSVQLA-------IEITTKSQEAAARHqaelLEQEA-RGRLERQKMHDKAKAEEQRtkllelqAESAAVESSgqsRAEAL 722
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072265250 2099 AEHEAALSRQQAE-EAERLKQKA-EIEAqakgQAQEDAEKVRKEAELEAAKRgQAEQAALKLKQMADAEMEKHKQ 2171
Cdd:PTZ00491 723 AEAEARLIEAEAEvEQAELRAKAlRIEA----EAELEKLRKRQELELEYEQA-QNELEIAKAKELADIEATKFER 792
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1471-1879 |
1.41e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.96 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1471 EDELRALRARAEEAERQkkLAQEEAERlrKQVKDEAQKKREAEDELHRKV-QAEKDAAREKQKALEDLEKFRLQAEEAER 1549
Cdd:COG3096 835 EAELAALRQRRSELERE--LAQHRAQE--QQLRQQLDQLKEQLQLLNKLLpQANLLADETLADRLEELREELDAAQEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1550 RMKQ-----AELEKE----RQIKQAHDVAQQS---ADAELQSKRmsflektTQLEmSLKQEHITVTHL--QEEAERLKKQ 1615
Cdd:COG3096 911 FIQQhgkalAQLEPLvavlQSDPEQFEQLQADylqAKEQQRRLK-------QQIF-ALSEVVQRRPHFsyEDAVGLLGEN 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1616 QleaetakeeaekelekwrqKANEALRLRL-QAEEIAHKKTLAQEEAEKQKEDAERE-----TRKRTKAEEsalrqkdla 1689
Cdd:COG3096 983 S-------------------DLNEKLRARLeQAEEARREAREQLRQAQAQYSQYNQVlaslkSSRDAKQQT--------- 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1690 eeelekqrkLAEetashklsAEQELIRLKAEVDSGEQHRIVLEEDlfRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKA 1769
Cdd:COG3096 1035 ---------LQE--------LEQELEELGVQADAEAEERARIRRD--ELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKR 1095
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1770 KSKAEEDSRSTSEkskqmlEVEASKLR-ELAEEAARLRAVSEEAKRqRQLAEEDATRQRAeaerilkekltaineatrMR 1848
Cdd:COG3096 1096 LRKAERDYKQERE------QVVQAKAGwCAVLRLARDNDVERRLHR-RELAYLSADELRS------------------MS 1150
|
410 420 430
....*....|....*....|....*....|....*
gi 1072265250 1849 TEAEIALKEKEAENERLR---RLAEDEAY-QRKLL 1879
Cdd:COG3096 1151 DKALGALRLAVADNEHLRdalRLSEDPRRpERKVQ 1185
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2008-2376 |
1.41e-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: 53.77 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2008 EEVERLKIKADEAKKQKDLAEKEAEKQ---IQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIYDKLKEEAEK 2084
Cdd:pfam13868 6 DELRELNSKLLAAKCNKERDAQIAEKKrikAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2085 AKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEaeLEAAKRGQAEQAALKLKQMADA 2164
Cdd:pfam13868 86 EQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAE--WKELEKEEEREEDERILEYLKE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2165 EMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDelgrlkeevtesLRQKKLVEEELFKVKIQMEELVKLKL 2244
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE------------LRAKLYQEEQERKERQKEREEAEKKA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2245 RIEQENKmlilkgkdntQQFLAEEAEKMKQVAEEAARlsvEAQEAARLRkiaeddlneqRALAEKILKEKMQAVQEASRL 2324
Cdd:pfam13868 232 RQRQELQ----------QAREEQIELKERRLAEEAER---EEEEFERML----------RKQAEDEEIEQEEAEKRRMKR 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 2325 KAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLD 2376
Cdd:pfam13868 289 LEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2001-2191 |
1.55e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.57 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2001 RQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIYDKLKE 2080
Cdd:PRK05035 461 RLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAA 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2081 EAEKAKRAAEEA--ERAKIKAEHEAALSRQQAEEAERLKQK---AEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAA 2155
Cdd:PRK05035 541 AAADPKKAAVAAaiARAKAKKAAQQAANAEAEEEVDPKKAAvaaAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAA 620
|
170 180 190
....*....|....*....|....*....|....*.
gi 1072265250 2156 LKLKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVK 2191
Cdd:PRK05035 621 IARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAK 656
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1990-2361 |
1.71e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.13 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1990 KKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEA----EKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEML 2065
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELrqsrEKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2066 QTRIQEqsIYDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEieaqakgqaQEDAEKVRKEAELEA 2145
Cdd:pfam07888 128 EARIRE--LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ---------QTEEELRSLSKEFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2146 AKRGQAEQAALKLKQMADAEMEKHK-QFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILddelgrlKEEVTESLRQKKL 2224
Cdd:pfam07888 197 LRNSLAQRDTQVLQLQDTITTLTQKlTTAHRKEAENEALLEELRSLQERLNASERKVEGL-------GEELSSMAAQRDR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2225 VEEELFKVKIQMEEL------VKLKLRieqENKMLILKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAED 2298
Cdd:pfam07888 270 TQAELHQARLQAAQLtlqladASLALR---EGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEV 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 2299 DLNEQRALAEKILKEKMQAVQEasrLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETE 2361
Cdd:pfam07888 347 ELGREKDCNRVQLSESRRELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1936-2170 |
1.72e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1936 ASVGKSDLELELQKLKNIADETQKSKEKAEQDAEK-QRQLALVEEARRKEAeekvKKIIAAEQEAGR-QRKVALEEVERL 2013
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKAlLKQLAALERRIAALA----RRIRALEQELAAlEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2014 KIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEE-------KAYYAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKAK 2086
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2087 raaeeAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMADAEM 2166
Cdd:COG4942 174 -----AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....
gi 1072265250 2167 EKHK 2170
Cdd:COG4942 249 AALK 252
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1470-1710 |
1.85e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.18 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1470 AEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDELHR---KVQAEKDAAREK--QKALEDLEKFRLQA 1544
Cdd:PRK05035 442 EQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAKDKDAVAAalaRVKAKKAAATQPivIKAGARPDNSAVIA 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1545 EEAERRMKQAELEKERQIKQAHD-----VAQQSADAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAerlKKQQLEA 1619
Cdd:PRK05035 522 AREARKAQARARQAEKQAAAAADpkkaaVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKA---KKAAQQA 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1620 ETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKL 1699
Cdd:PRK05035 599 ASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKA 678
|
250
....*....|.
gi 1072265250 1700 AEETASHKLSA 1710
Cdd:PRK05035 679 AVAAAIARAKA 689
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2231-2624 |
1.99e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2231 KVKIQMEELVKLKLRIEQENkmliLKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALaeKI 2310
Cdd:COG4717 50 RLEKEADELFKPQGRKPELN----LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL--EK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2311 LKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQVVE 2390
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2391 MSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEK---------------MTVVHTLEIQRQHSDKEAEELRKAIAdlE 2455
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAaleerlkearlllliAAALLALLGLGGSLLSLILTIAGVLF--L 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2456 NEKEKLKKEAELLQKKSEEMQKAQKEQLRQETQTLQSTFLTEkqILIQKEKYIEEEKAKLEKLFDNEVGKAQKLKS---- 2531
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE--LLAALGLPPDLSPEELLELLDRIEELQELLREaeel 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2532 EKERQLAQLEEEKRLL----QTSMDDAMKKQLDAEDRIRQKQEELQQLD-----KKRQEQERLLEEENRKLRERLEQLEQ 2602
Cdd:COG4717 360 EEELQLEELEQEIAALlaeaGVEDEEELRAALEQAEEYQELKEELEELEeqleeLLGELEELLEALDEEELEEELEELEE 439
|
410 420
....*....|....*....|..
gi 1072265250 2603 EHRiALEKTREVIITKETVITQ 2624
Cdd:COG4717 440 ELE-ELEEELEELREELAELEA 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1350-1550 |
2.13e-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: 53.61 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1350 AEKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQQKKTIQQ---ELHQMKN 1426
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllrALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1427 NSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDea 1506
Cdd:COG4942 119 QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE-- 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1072265250 1507 qkKREAEDELHRKVQAEKDAAREKQKALEDLEKF--RLQAEEAERR 1550
Cdd:COG4942 197 --RQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1883-2120 |
2.17e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1883 AAQHKQDIEEKIHQLKQssenELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKE 1962
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1963 KAEQDAEKQRQLalveearrkeaeekVKKIIAAEQEAGRQRKVAL--------EEVERLKIKADEAKKQKDLAEKEAEKQ 2034
Cdd:COG4942 94 ELRAELEAQKEE--------------LAELLRALYRLGRQPPLALllspedflDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2035 IQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIYDKlKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAE 2114
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA-RLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
....*.
gi 1072265250 2115 RLKQKA 2120
Cdd:COG4942 239 AAERTP 244
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3925-3962 |
2.30e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.71 E-value: 2.30e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1072265250 3925 QKFLEGTSCIAGVYVEASKDRYSIYQAMKKGMIRPGTA 3962
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2129-2575 |
2.55e-06 |
|
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: 53.97 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2129 QAQEDAEKVRKEAELEAAKRGQAEQAALKLK-QMADAEMEKHkqfAEKTVRQKEQVEGELTKVKLQ--LEETDHQKAILD 2205
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSVIDLQtKLQEMQMERD---AMADIRRRESQSQEDLRNQLQntVHELEAAKCLKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2206 DELGRLKEEVtESLRQKKLVEE----ELFKVKIQMEELVKLKLRiEQENKML------------ILKGKDNTQQFLA--- 2266
Cdd:pfam15921 163 DMLEDSNTQI-EQLRKMMLSHEgvlqEIRSILVDFEEASGKKIY-EHDSMSTmhfrslgsaiskILRELDTEISYLKgri 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2267 ----EEAEKMKQVAEEAARLSVEaQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQA 2342
Cdd:pfam15921 241 fpveDQLEALKSESQNKIELLLQ-QHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2343 KKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKK----FRKQAEDIS-EKLH 2417
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKlladLHKREKELSlEKEQ 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2418 QTEL---STKEKMTVVH--------TLEIQR-------QHSDKEAEELRKAIADLENEKEKLKKEAELLQKKS-EEMQKA 2478
Cdd:pfam15921 400 NKRLwdrDTGNSITIDHlrrelddrNMEVQRleallkaMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEStKEMLRK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2479 QKEQLRQETQTLQSTFLTEKQI---LIQKEKYIEEEKAKLEKL---FDNEVGKAQKLKSEkerqlaqlEEEKRLLQTSMd 2552
Cdd:pfam15921 480 VVEELTAKKMTLESSERTVSDLtasLQEKERAIEATNAEITKLrsrVDLKLQELQHLKNE--------GDHLRNVQTEC- 550
|
490 500
....*....|....*....|....*..
gi 1072265250 2553 DAMKKQLDAEDRI----RQKQEELQQL 2575
Cdd:pfam15921 551 EALKLQMAEKDKVieilRQQIENMTQL 577
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1459-1865 |
2.91e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 53.37 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1459 QLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLE 1538
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1539 KFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLE 1618
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1619 AETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRK 1698
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1699 LAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSR 1778
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1779 STSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEK 1858
Cdd:COG5278 431 ALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLL 510
|
....*..
gi 1072265250 1859 EAENERL 1865
Cdd:COG5278 511 AAAEAAL 517
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1730-2373 |
2.92e-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: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1730 VLEE-DLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEdsrstsekskqmLEVEASKLRELAEEAARLRAv 1808
Cdd:COG4913 217 MLEEpDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAER------------YAAARERLAELEYLRAALRL- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1809 sEEAKRQRQLAEEDATRQRAEAERilkekltaineatrmrteaeiaLKEKEAENERLRRLAEDEAYQrklLEEQAAQHKQ 1888
Cdd:COG4913 284 -WFAQRRLELLEAELEELRAELAR----------------------LEAELERLEARLDALREELDE---LEAQIRGNGG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1889 DIEEKIhqlkqssENELERQKTIVDETLKHRRVIEEEIRILKINFEkasvgksDLELELQKLKNIADETQKSKEKAEQDA 1968
Cdd:COG4913 338 DRLEQL-------EREIERLERELEERERRRARLEALLAALGLPLP-------ASAEEFAALRAEAAALLEALEEELEAL 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1969 EKQRQlalveearrkeaeekvkKIIAAEQEAGRQRKVALEEVERLK-----IKADEAKKQKDLAEkeaekqiQLAQDAAR 2043
Cdd:COG4913 404 EEALA-----------------EAEAALRDLRRELRELEAEIASLErrksnIPARLLALRDALAE-------ALGLDEAE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2044 LKIDAE----------------------------EKAYYAA------------------VQQKEQEMLQTRIQEQSIYDK 2077
Cdd:COG4913 460 LPFVGElievrpeeerwrgaiervlggfaltllvPPEHYAAalrwvnrlhlrgrlvyerVRTGLPDPERPRLDPDSLAGK 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2078 LKEEAEKAKRAAEE--AERAK-IKAEHEAALSRQ---------------------QAEEAERL-------KQKAEIEAQA 2126
Cdd:COG4913 540 LDFKPHPFRAWLEAelGRRFDyVCVDSPEELRRHpraitragqvkgngtrhekddRRRIRSRYvlgfdnrAKLAALEAEL 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2127 KgQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMADAemekhkQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDD 2206
Cdd:COG4913 620 A-ELEEELAEAEERLEALEAELDALQERREALQRLAEY------SWDEIDVASAEREIAELEAELERLDASSDDLAALEE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2207 ELGRLKEEVTESLRQKKLVEEELFKVKIQMEELVKLklriEQENKMLILKGKDNTQQFLAEEAEKMKQVAEEAARlsvEA 2286
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELRALLEERFAAALGDAV---ER 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2287 QEAARLRKiAEDDLNEQRALAEKILKEKMQAVQ-----EASRLKAEAE-------MLQKQKEMAMEQAKklQEDKEQMQQ 2354
Cdd:COG4913 766 ELRENLEE-RIDALRARLNRAEEELERAMRAFNrewpaETADLDADLEslpeylaLLDRLEEDGLPEYE--ERFKELLNE 842
|
730
....*....|....*....
gi 1072265250 2355 QLAEETEGFQKTLEAERRR 2373
Cdd:COG4913 843 NSIEFVADLLSKLRRAIRE 861
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1364-1535 |
3.13e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1364 VEDQLEKQRQLAEAHAQAKAVAEKealelRMNMQEEVTRREVVAVDAEQQKKTIQQELHQMK---NNSETEIKAKVKLIE 1440
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHR-----LKELPAELAELEDELAALEARLEAAKTELEDLEkeiKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1441 EAEYNRKKV--EEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDELhr 1518
Cdd:COG1579 77 KYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL-- 154
|
170
....*....|....*..
gi 1072265250 1519 kvQAEKDAAREKQKALE 1535
Cdd:COG1579 155 --EAELEELEAEREELA 169
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1691-2176 |
3.25e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1691 EELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLK---------NEVNEAIQRRRGLEEELAKVRA 1761
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1762 EMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERIlkekltai 1841
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL-------- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1842 neatrmrteaeialkekeaenerlrrlaedeayQRKLLEEQAAQHKQDIEEKIHQLKQSseneLERQKTIVDETLKHRRV 1921
Cdd:COG4717 226 ---------------------------------EEELEQLENELEAAALEERLKEARLL----LLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1922 IEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEagr 2001
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR--- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2002 qrkvaLEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAArlkiDAEEKAYYAAVQQKEQEMLQTRIQEqsIYDKLKEE 2081
Cdd:COG4717 346 -----IEELQELLREAEELEEELQLEELEQEIAALLAEAGV----EDEEELRAALEQAEEYQELKEELEE--LEEQLEEL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2082 AEKAKRAAEEAERAKIKAEH---EAALSRQQAEEAERLKQKAEIEAQAKgQAQEDAEKVRKEAELE--AAKRGQAEQAAL 2156
Cdd:COG4717 415 LGELEELLEALDEEELEEELeelEEELEELEEELEELREELAELEAELE-QLEEDGELAELLQELEelKAELRELAEEWA 493
|
490 500
....*....|....*....|
gi 1072265250 2157 KLKqMADAEMEKHKQFAEKT 2176
Cdd:COG4717 494 ALK-LALELLEEAREEYREE 512
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1869-2224 |
3.30e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 53.61 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1869 AEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKTIVDE----TLKHRRVIEEEIRILKINFEKASVGKSD-L 1943
Cdd:pfam09731 102 AEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVakeaKDDAIQAVKAHTDSLKEASDTAEISREKaT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1944 ELELQKLKNIADETQKSKEKAEQDAEKQ-RQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVaLEEVERLKIKADEaKK 2022
Cdd:pfam09731 182 DSALQKAEALAEKLKEVINLAKQSEEEAaPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKL-VDQYKELVASERI-VF 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2023 QKDLAEKEAEKQIQLAQDAARLKIDAE---EKAYyAAVQQKEQEMLQTRIQEQsiydKLKEEAEKAKRAAEEAERAKIKA 2099
Cdd:pfam09731 260 QQELVSIFPDIIPVLKEDNLLSNDDLNsliAHAH-REIDQLSKKLAELKKREE----KHIERALEKQKEELDKLAEELSA 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2100 EHEAALSRQQAEEaeRLKQKAEIEAQAKgqaqedaekvRKEAELEAAKRGQAEQAALKLKQM-ADAEMEKHKQFAEKTvr 2178
Cdd:pfam09731 335 RLEEVRAADEAQL--RLEFEREREEIRE----------SYEEKLRTELERQAEAHEEHLKDVlVEQEIELQREFLQDI-- 400
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1072265250 2179 qKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKL 2224
Cdd:pfam09731 401 -KEKVEEERAGRLLKLNELLANLKGLEKATSSHSEVEDENRKAQQL 445
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1361-1829 |
3.59e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 53.65 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1361 LAEVEDQLEKQR----QLAEAHAQAKAVAEKEA--LELRMNMQEEVTRREVVAVDAEQQKKTIQQELhqmknnseteikA 1434
Cdd:PRK10246 411 VAAALAQHAEQRplrqRLVALHGQIVPQQKRLAqlQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQL------------A 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1435 KVKLIEEAEYNRKKVEEEiriiRIQLETSQ------KQKSGAEDELRAL-----RARAEEAERQKKLAQEEAERLRKQVK 1503
Cdd:PRK10246 479 DVKTICEQEARIKDLEAQ----RAQLQAGQpcplcgSTSHPAVEAYQALepgvnQSRLDALEKEVKKLGEEGAALRGQLD 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1504 DEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAE-------EAERRMKQAELEKERQIKQAHDVAQQ----S 1572
Cdd:PRK10246 555 ALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDdiqpwldAQEEHERQLRLLSQRHELQGQIAAHNqqiiQ 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1573 ADAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKkqqleaetakeeaekeleKWRQKANEALRLRLQAEEIAH 1652
Cdd:PRK10246 635 YQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQ------------------SWQQRQNELTALQNRIQQLTP 696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1653 -KKTLAQ-----EEAEKQKEDAERETRKRTKAEESALR--QKDLAEEELEKQRKLAEETASHKLS--AEQELIrLKAEVD 1722
Cdd:PRK10246 697 lLETLPQsddlpHSEETVALDNWRQVHEQCLSLHSQLQtlQQQDVLEAQRLQKAQAQFDTALQASvfDDQQAF-LAALLD 775
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1723 SGEQHRivLEEDLFRLKNEVNEAI----QRRRGLEEELAKVRAEMeillkakskaeeDSRSTSEKSKQMLEVEASKLREL 1798
Cdd:PRK10246 776 EETLTQ--LEQLKQNLENQRQQAQtlvtQTAQALAQHQQHRPDGL------------DLTVTVEQIQQELAQLAQQLREN 841
|
490 500 510
....*....|....*....|....*....|....*.
gi 1072265250 1799 AEEAARLRAV--SEEAKRQRQ---LAEEDATRQRAE 1829
Cdd:PRK10246 842 TTRQGEIRQQlkQDADNRQQQqalMQQIAQATQQVE 877
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1112-1766 |
3.71e-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: 53.64 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1112 KEVQTVPGDLKELESSKADLKRMRGQVEGHQPLFNGLENDLTKAR-EVSERMLKVHSE-------------------RDV 1171
Cdd:pfam01576 384 SENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRaELAEKLSKLQSElesvssllneaegkniklsKDV 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1172 D-LERYREKVQLLL--ERWQAIVLQIEVRQRELEQLGKQLRYYREsyewlirwiTEAKKRQEKiqnvpitDSKTVKEQLM 1248
Cdd:pfam01576 464 SsLESQLQDTQELLqeETRQKLNLSTRLRQLEDERNSLQEQLEEE---------EEAKRNVER-------QLSTLQAQLS 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1249 EEKKLLEESEKNRGKVDECQKYAKQYIEAIKdfeVQLVTYKAQVEpvvsplkkpKVHSASDNIIQEY----VELRTKYSE 1324
Cdd:pfam01576 528 DMKKKLEEDAGTLEALEEGKKRLQRELEALT---QQLEEKAAAYD---------KLEKTKNRLQQELddllVDLDHQRQL 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1325 LTTLTSQYIKFITETLRRLEEEERTAEklkEQERkklAEVEDQLEKQRQLAEAHAQAKAVAEKEALE-----LRMNMQEE 1399
Cdd:pfam01576 596 VSNLEKKQKKFDQMLAEEKAISARYAE---ERDR---AEAEAREKETRALSLARALEEALEAKEELErtnkqLRAEMEDL 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1400 VTRREVVAVDA---EQQKKTIQQELHQMKNNSE--------TEiKAKVKL------------------IEEAEYNRKKVE 1450
Cdd:pfam01576 670 VSSKDDVGKNVhelERSKRALEQQVEEMKTQLEeledelqaTE-DAKLRLevnmqalkaqferdlqarDEQGEEKRRQLV 748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1451 EEIRIIRIQLETSQKQKSGA-------EDELRALRARAEEAERQKKLAQEEAERLRKQVKD---EAQKKREAEDELHrkv 1520
Cdd:pfam01576 749 KQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDlqrELEEARASRDEIL--- 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1521 qaekDAAREKQKALEDLEKFRLQAEE----AERRMKQAELEKErqiKQAHDVAQQSADAELQSKRMSFLE-KTTQLEMSL 1595
Cdd:pfam01576 826 ----AQSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERD---ELADEIASGASGKSALQDEKRRLEaRIAQLEEEL 898
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1596 KQEHITVTHLQEEAERLKKQ------QLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIA----HKKTLAQEEA--EK 1663
Cdd:pfam01576 899 EEEQSNTELLNDRLRKSTLQveqlttELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTvkskFKSSIAALEAkiAQ 978
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1664 QKEDAERETRKRTKAEEsALRQKDLAEEEL----EKQRKLAEEtasHKLSAEQELIRLKAevdsgeqhrivLEEDLFRLK 1739
Cdd:pfam01576 979 LEEQLEQESRERQAANK-LVRRTEKKLKEVllqvEDERRHADQ---YKDQAEKGNSRMKQ-----------LKRQLEEAE 1043
|
730 740
....*....|....*....|....*..
gi 1072265250 1740 NEVNEAIQRRRGLEEELAKVRAEMEIL 1766
Cdd:pfam01576 1044 EEASRANAARRKLQRELDDATESNESM 1070
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3132-3168 |
3.79e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.79e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1072265250 3132 LRLLSAQLATGGIIDPVNSHRLPLEIAYKRGHLDEET 3168
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2260-2624 |
3.97e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.42 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2260 NTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNE-QRAL--AEKIlkEKMQA-VQEASRLKAEAEM----L 2331
Cdd:COG3096 296 GARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLvQTALrqQEKI--ERYQEdLEELTERLEEQEEvveeA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2332 QKQKEMAMEQAKKLQEDKEQMQQQLAEetegFQKTLEAERRRQLDIS------AEAERLkLQVVEMSKSQAKAEEDAkkF 2405
Cdd:COG3096 374 AEQLAEAEARLEAAEEEVDSLKSQLAD----YQQALDVQQTRAIQYQqavqalEKARAL-CGLPDLTPENAEDYLAA--F 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2406 RKQAEDISEKLhqteLSTKEKMTVVhtlEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQLRQ 2485
Cdd:COG3096 447 RAKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRYRSQQALAQRLQQLRA 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2486 EtqtlqstfLTEKQILIQKEKYIEEEKAKLEKLFDNEVGKAQKLKSEKERQLAQLEEEKRLLQTSMDDAMkkqldaedRI 2565
Cdd:COG3096 520 Q--------LAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS--------EL 583
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1072265250 2566 RQKQEELQQLDKKRQEQERLLeeenRKLRERLEQLEQEHRIALEKTREVIITKETVITQ 2624
Cdd:COG3096 584 RQQLEQLRARIKELAARAPAW----LAAQDALERLREQSGEALADSQEVTAAMQQLLER 638
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1448-1705 |
4.01e-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: 53.03 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1448 KVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAER-LRKQVKDEAQKKREAEDELHRKVQAEKDa 1526
Cdd:pfam15709 283 KYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQEKaSRDRLRAERAEMRRLEVERKRREQEEQR- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1527 arekqkaledlekfRLQAEEAERRMK-QAELEKERQiKQAHDVAQQSADAELQSKRMSFLEKTTQLEMSLKQEHitvTHL 1605
Cdd:pfam15709 362 --------------RLQQEQLERAEKmREELELEQQ-RRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQER---ARQ 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1606 QEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLrlqAEEIAHKKTLAQEE-AEKQKEDAERETRKRTKAEESALR 1684
Cdd:pfam15709 424 QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQL---AEEQKRLMEMAEEErLEYQRQKQEAEEKARLEAEERRQK 500
|
250 260
....*....|....*....|.
gi 1072265250 1685 QKDLAEEELEKQRKLAEETAS 1705
Cdd:pfam15709 501 EEEAARLALEEAMKQAQEQAR 521
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1350-1720 |
4.15e-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: 53.09 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1350 AEKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAvdaeQQKKTIQQELHQMKNNS- 1428
Cdd:NF033838 60 AKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTS----KTKKELDAAFEQFKKDTl 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1429 --ETEIKAKVKLIEEAEYNRKKVEEE-------IRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLR 1499
Cdd:NF033838 136 epGKKVAEATKKVEEAEKKAKDQKEEdrrnyptNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKVES 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1500 KQVKDEAQKK-----REAEDELHRKVQAEKDAAREKQKALEDLEKfrlqaeeAERRMKQAEL-EKERQIKQAHDvAQQSA 1573
Cdd:NF033838 216 KKAEATRLEKiktdrEKAEEEAKRRADAKLKEAVEKNVATSEQDK-------PKRRAKRGVLgEPATPDKKEND-AKSSD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1574 daelqskrmSFLEKTTQLEMSLKQEhitvthlQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHK 1653
Cdd:NF033838 288 ---------SSVGEETLPSPSLKPE-------KKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKTLELEIAESDVKVK 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 1654 KTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAE 1720
Cdd:NF033838 352 EAELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAE 418
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2076-2180 |
4.51e-06 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 49.77 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2076 DKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAeeaerlkqkAEIEAQAKGQAQEDAEKVRKEAELEAAkrgqaeqaa 2155
Cdd:PRK05759 38 KKIADGLAAAERAKKELELAQAKYEAQLAEARAEA---------AEIIEQAKKRAAQIIEEAKAEAEAEAA--------- 99
|
90 100
....*....|....*....|....*
gi 1072265250 2156 lKLKQMADAEMEKHKQFAEKTVRQK 2180
Cdd:PRK05759 100 -RIKAQAQAEIEQERKRAREELRKQ 123
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1350-1665 |
4.52e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.23 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1350 AEKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEevtRREVVAVDAEQQKKTIQQELHQMKNNSE 1429
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKR---YRQELEEQIEEREQKRQEEYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1430 TEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKK 1509
Cdd:pfam13868 102 QMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1510 REAEDELHRKVQAEKDAAREKQKALedleKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQSKRMsFLEKTT 1589
Cdd:pfam13868 182 KEREIARLRAQQEKAQDEKAERDEL----RAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKER-RLAEEA 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072265250 1590 QLEmslKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQK 1665
Cdd:pfam13868 257 ERE---EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRE 329
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1590-1972 |
4.68e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1590 QLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAE 1669
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1670 RETRKRTKAEESALRQkdlaeEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRR 1749
Cdd:COG4717 155 LEELRELEEELEELEA-----ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1750 RGLEEELAKVRAEMEI--------------LLKAKSKAEEDSRST------------------SEKSKQMLEVEASKLRE 1797
Cdd:COG4717 230 EQLENELEAAALEERLkearlllliaaallALLGLGGSLLSLILTiagvlflvlgllallfllLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1798 LAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEA--YQ 1875
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1876 RKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKTIVDETLKHR-RVIEEEIRILKINFEKASVGKSDLELELQKLKNIA 1954
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
410
....*....|....*...
gi 1072265250 1955 DETQKSKEKAEQDAEKQR 1972
Cdd:COG4717 470 ELAELLQELEELKAELRE 487
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1670-2115 |
4.73e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.99 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1670 RETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRR 1749
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1750 RGLEEELAKVRAEMEILLKAKSKA---EEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQ 1826
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALlalAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1827 RAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENELE 1906
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1907 RQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLALVEEARRKEAE 1986
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1987 EKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQ 2066
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1072265250 2067 TRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAER 2115
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1471-1916 |
4.81e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.60 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1471 EDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKF-RLQAEEAER 1549
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMdEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1550 RMKQAELEKERQIKQAHDVAQQSADAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKE 1629
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1630 LEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLS 1709
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1710 AEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLE 1789
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1790 VEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLA 1869
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1072265250 1870 EDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKTIVDETL 1916
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASA 528
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2074-2557 |
5.74e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2074 IYDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQ 2153
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2154 AALKLKQMADAEMEKhKQFAEKTVRQKEQVEgeltkvklQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEElfKVK 2233
Cdd:COG4717 127 LLPLYQELEALEAEL-AELPERLEELEERLE--------ELRELEEELEELEAELAELQEELEELLEQLSLATEE--ELQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2234 IQMEELVKLKLRIEQEnkmlilkgkdntQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEddLNEQRALAEKILKE 2313
Cdd:COG4717 196 DLAEELEELQQRLAEL------------EEELEEAQEELEELEEELEQLENELEAAALEERLKE--ARLLLLIAAALLAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2314 KMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAE-ETEGFQKTLEAERRRQL--DISAEAERLKLQVVE 2390
Cdd:COG4717 262 LGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEElQALPALEELEEEELEELlaALGLPPDLSPEELLE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2391 MSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLE--IQRQHSDKEAEELRKAIADLENE-KEKLKKEAEL 2467
Cdd:COG4717 342 LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelRAALEQAEEYQELKEELEELEEQlEELLGELEEL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2468 LQKKSEEMQKAQKEQLRQETQTLQStfltEKQILIQKEKYIEEEKAKLEKlfDNEVGKAQKLKSEKERQLAQLEEE---K 2544
Cdd:COG4717 422 LEALDEEELEEELEELEEELEELEE----ELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEwaaL 495
|
490
....*....|...
gi 1072265250 2545 RLLQTSMDDAMKK 2557
Cdd:COG4717 496 KLALELLEEAREE 508
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2059-2361 |
6.16e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 51.96 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2059 QKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEHEAalsRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVR 2138
Cdd:pfam15558 18 KEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQ---WQAEKEQRKARLGREERRRADRREKQVIEKES 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2139 KEAELeAAKRGQAEQAALKLKQMaDAEMEKHKQfaEKTVRQKEqvegELTKVKLQLEETDHQKAILDDELGRLKEEVTES 2218
Cdd:pfam15558 95 RWREQ-AEDQENQRQEKLERARQ-EAEQRKQCQ--EQRLKEKE----EELQALREQNSLQLQERLEEACHKRQLKEREEQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2219 LR-----QKKLVEEELFKV----KIQMEEL-----VKLKLRIEQENKMLILKGKDNTQQFLA-EEAEKMKQVAEEAARLS 2283
Cdd:pfam15558 167 KKvqennLSELLNHQARKVlvdcQAKAEELlrrlsLEQSLQRSQENYEQLVEERHRELREKAqKEEEQFQRAKWRAEEKE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2284 VEAQEAAR-LRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQK-----EMAMEQAKKLQEDKEQMQQQLA 2357
Cdd:pfam15558 247 EERQEHKEaLAELADRKIQQARQVAHKTVQDKAQRARELNLEREKNHHILKLKvekeeKCHREGIKEAIKKKEQRSEQIS 326
|
....
gi 1072265250 2358 EETE 2361
Cdd:pfam15558 327 REKE 330
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1425-2033 |
6.29e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1425 KNNSETEIK---AKVKLIEEAEYNRK----KVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAER 1497
Cdd:TIGR04523 70 INNSNNKIKileQQIKDLNDKLKKNKdkinKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1498 LRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQaeeaeRRMKQAELEKERQIKQAHDvaqqsadaEL 1577
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK-----LLKLELLLSNLKKKIQKNK--------SL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1578 QSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKeeaekelekwrQKANEALRlrlqaeeiahKKTLA 1657
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ-----------NKIKKQLS----------EKQKE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1658 QEEAEKQKEDAERETrKRTKAEESALRQkdlaeeelEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFR 1737
Cdd:TIGR04523 276 LEQNNKKIKELEKQL-NQLKSEISDLNN--------QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1738 LKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTsEKSKQMLEveaSKLRELAEEAARLRAVSEEAKRQRQ 1817
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL-ESQINDLE---SKIQNQEKLNQQKDEQIKKLQQEKE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1818 LAEEDATRQRAEAERilkekltaiNEATRMRTEAEIALKEKEAENerLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQL 1897
Cdd:TIGR04523 423 LLEKEIERLKETIIK---------NNSEIKDLTNQDSVKELIIKN--LDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1898 KQ--SSENELERQKTIVDETLKhrrVIEEEIRILKINFEKASVGKSDLELEL----QKLKNIADETQKSKEKAEQDAEKQ 1971
Cdd:TIGR04523 492 KSkeKELKKLNEEKKELEEKVK---DLTKKISSLKEKIEKLESEKKEKESKIsdleDELNKDDFELKKENLEKEIDEKNK 568
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 1972 RQLALVEEARRKEAEEKVKKIIAAEQEAgrQRKVALEEVERLKIKADEAKKQKDLAEKEAEK 2033
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELIDQKEK--EKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
160-267 |
6.31e-06 |
|
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: 48.26 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 160 QSEDMTAKEKLLLWSQRMsegYQGLRCDNFTSNWRDGRLFSAIIHRHKPMLI-DMNRVYRQTNLENLDQAFTVAERELGV 238
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 1072265250 239 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 267
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1634-1836 |
6.50e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.18 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1634 RQKANEALRLRLQAEEIAHKKtlAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKlaeetashKLSAEQE 1713
Cdd:COG2268 198 IRDARIAEAEAERETEIAIAQ--ANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETA--------RAEAEAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1714 lirlkAEVdsgeqhrivleedlfrlknevnEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQmleVEAS 1793
Cdd:COG2268 268 -----YEI----------------------AEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKP---AEAE 317
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1072265250 1794 KLRELAEEAARLRAVSEEAKrqrqlAEEDATRQRAEAERILKE 1836
Cdd:COG2268 318 KQAAEAEAEAEAEAIRAKGL-----AEAEGKRALAEAWNKLGD 355
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1399-1555 |
8.35e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.80 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1399 EVTRREVVAV-----DAEQQKKTIQQELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDE 1473
Cdd:COG2268 196 EIIRDARIAEaeaerETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANA 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1474 LRALRARAEEAERQK--KLAQEEAERLRKQVKDEAQKKREAEdelhrKVQAEKDAAREKQKALEDLEKfrlqaeEAERRM 1551
Cdd:COG2268 276 EREVQRQLEIAEREReiELQEKEAEREEAELEADVRKPAEAE-----KQAAEAEAEAEAEAIRAKGLA------EAEGKR 344
|
....
gi 1072265250 1552 KQAE 1555
Cdd:COG2268 345 ALAE 348
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2075-2300 |
8.46e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2075 YDKLKEEAEKAKRAAEEaeRAKIKAEHEAALSRQQAEEAERLKQkaeiEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQA 2154
Cdd:PRK09510 64 YNRQQQQQKSAKRAEEQ--RKKKEQQQAEELQQKQAAEQERLKQ----LEKERLAAQEQKKQAEEAAKQAALKQKQAEEA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2155 ALKLKQMADAEMEKHKQFAEKTVRQKEqvegELTKVKLQLEETDHQKAILDDELgrlkeevtESLRQKKLVEEElfkvKI 2234
Cdd:PRK09510 138 AAKAAAAAKAKAEAEAKRAAAAAKKAA----AEAKKKAEAEAAKKAAAEAKKKA--------EAEAAAKAAAEA----KK 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 2235 QMEELVKLKLRIEQENKMLILKGKDntqqflAEEAEKMKQVAEEAARLSVEAQEAARLRKIAE-DDL 2300
Cdd:PRK09510 202 KAEAEAKKKAAAEAKKKAAAEAKAA------AAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEvDDL 262
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2262-2568 |
9.29e-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: 51.07 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2262 QQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQ 2341
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2342 AKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAE-RLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTE 2420
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDeRILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2421 LSTKEKMTVVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQLRQEtQTLQSTFLTEKQI 2500
Cdd:pfam13868 194 EKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAERE-EEEFERMLRKQAE 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072265250 2501 LIQKEKYIEEEKAKLEKLFDNEVgkaQKLKSEKERQLAQLEEEKRLLQTSMDDAMKKQLDAEDRIRQK 2568
Cdd:pfam13868 273 DEEIEQEEAEKRRMKRLEHRREL---EKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1428-1616 |
9.77e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1428 SETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQ 1507
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1508 -------------------------KKREAEDELHRKVQAEKDAAREKQKALEDLEKfRLQAEEAERRMKQAELEKERQI 1562
Cdd:COG3883 94 alyrsggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKA-ELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 1563 KQAHDVAQQSADAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQ 1616
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2040-2361 |
9.92e-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: 51.95 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2040 DAARLKIDAEEKAYYAAVQQK-EQEMLQTRIQEQSIY----------DKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQ 2108
Cdd:pfam05667 173 KGKTLKNSKELKEFYSEYLPPvTAQPSSRASVVPSLLernaaelaaaQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRI 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2109 QAEEAERLKQKAEIEAQAKGQAQEDAEKV-----RKEAELEAAKRGQ---AEQAALKLKQMADAEMEKHKQFAEKTVRQK 2180
Cdd:pfam05667 253 AEQLRSAALAGTEATSGASRSAQDLAELLssfsgSSTTDTGLTKGSRfthTEKLQFTNEAPAATSSPPTKVETEEELQQQ 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2181 EQVEgeLTKVKLQLEETDHQKAILDDELGRLK---EEVTESLRQKKLVEEEL---FKVKIQMEELVKlklriEQENKMLI 2254
Cdd:pfam05667 333 REEE--LEELQEQLEDLESSIQELEKEIKKLEssiKQVEEELEELKEQNEELekqYKVKKKTLDLLP-----DAEENIAK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2255 LKGKdntqqfLAEEAEKMKQVAEEaarlsveaQEAARlrkiaEDDLNEQRALAEKILKEKMqavqEASRLKAEAEMLQKQ 2334
Cdd:pfam05667 406 LQAL------VDASAQRLVELAGQ--------WEKHR-----VPLIEEYRALKEAKSNKED----ESQRKLEEIKELREK 462
|
330 340
....*....|....*....|....*..
gi 1072265250 2335 KEMAMEQAKKlqedKEQMQQQLAEETE 2361
Cdd:pfam05667 463 IKEVAEEAKQ----KEELYKQLVAEYE 485
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1840-2168 |
1.13e-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: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1840 AINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAaQHKQDIEEKIHQLKQSSENELERQKTIVDETLKH- 1918
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERK-RYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1919 RRVIEEEIRILKINFEKASVGKSDLELELQKLKNiadetQKSKEKAEQDAEKQRQLALVEEarrkeaeekvKKIIAAEQE 1998
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAE-----WKELEKEEEREEDERILEYLKE----------KAEREEERE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1999 AGRQRKVALEEVERLKIKADEAKKQKDLAEKEaEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQsiydKL 2078
Cdd:pfam13868 173 AEREEIEEEKEREIARLRAQQEKAQDEKAERD-ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI----EL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2079 KEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKL 2158
Cdd:pfam13868 248 KERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAER 327
|
330
....*....|
gi 1072265250 2159 KQMADAEMEK 2168
Cdd:pfam13868 328 RERIEEERQK 337
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
40-153 |
1.18e-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: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 40 ERDRVQKKTFTKWVNKHLIKHWraeaqrhVNDLYEDLRDGHNLISLLEV---------LSGETLPREKGRMRfhKLQNVQ 110
Cdd:cd21329 2 EGESSEERTFRNWMNSLGVNPY-------VNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCN 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1072265250 111 IALDFLKLR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 153
Cdd:cd21329 73 YAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1459-1905 |
1.19e-05 |
|
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: 51.75 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1459 QLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDeaqkKREAEDELHRKVQAEK-------------- 1524
Cdd:pfam10174 367 QLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRD----KDKQLAGLKERVKSLQtdssntdtalttle 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1525 DAAREKQKALEDLEKFRlqaeEAERRMKQAELEKERQ----------IKQAHDVAQQSADAELQSKRMSFLEKTTQLEMS 1594
Cdd:pfam10174 443 EALSEKERIIERLKEQR----EREDRERLEELESLKKenkdlkekvsALQPELTEKESSLIDLKEHASSLASSGLKKDSK 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1595 LKQEHITVTHLQEEAERLKKQQLEAETAKEEAekelekwRQKANEALRLRLQAEEIAHKKtlaqEEAEKQKEDAERETrk 1674
Cdd:pfam10174 519 LKSLEIAVEQKKEECSKLENQLKKAHNAEEAV-------RTNPEINDRIRLLEQEVARYK----EESGKAQAEVERLL-- 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1675 rtkaeeSALRqkDLAEEELEKQRKLAEetashklsaeqelirlkaevdsgeqhrivLEEDLFRLKNEVNEAIQRRRGLEE 1754
Cdd:pfam10174 586 ------GILR--EVENEKNDKDKKIAE-----------------------------LESLTLRQMKEQNKKVANIKHGQQ 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1755 ELAKVRAEMeiLLKAKSKAEEDSRSTSEKSKQMLEVEASKLR-ELAEEAARLRAVseeakrQRQLAEEDA--TRQRAEAE 1831
Cdd:pfam10174 629 EMKKKGAQL--LEEARRREDNLADNSQQLQLEELMGALEKTRqELDATKARLSST------QQSLAEKDGhlTNLRAERR 700
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072265250 1832 RILKEKLtaineatRMRTEAEI-ALKEKEAENErlrrLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENEL 1905
Cdd:pfam10174 701 KQLEEIL-------EMKQEALLaAISEKDANIA----LLELSSSKKKKTQEEVMALKREKDRLVHQLKQQTQNRM 764
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1863-2453 |
1.20e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1863 ERLRRLAEDEAYQRKLLEeQAAQHKQDIEEKIHQLkqsseNELERQKTIVDETLKHRRVIEEEIRIlkinfekasvgkSD 1942
Cdd:COG4913 238 ERAHEALEDAREQIELLE-PIRELAERYAAARERL-----AELEYLRAALRLWFAQRRLELLEAEL------------EE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1943 LELELQKLkniadETQKSKEKAEQDAEKQRQLALveearrkeaeekvkkiIAAEQEAGRQRkvaleeVERLKIKADEAKK 2022
Cdd:COG4913 300 LRAELARL-----EAELERLEARLDALREELDEL----------------EAQIRGNGGDR------LEQLEREIERLER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2023 QKDLAEKEAEKQIQLAQDAArLKIDAEEKAYyAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEEaERAKIKAEHE 2102
Cdd:COG4913 353 ELEERERRRARLEALLAALG-LPLPASAEEF-AALRAEAAALLEALEEELEALEEALAEAEAALRDLRR-ELRELEAEIA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2103 AALSRQQAEEAERLKQKAEIeAQAKGQAQED----AE--KVRKEAE-----LEAAKRGQA---------EQAAL------ 2156
Cdd:COG4913 430 SLERRKSNIPARLLALRDAL-AEALGLDEAElpfvGEliEVRPEEErwrgaIERVLGGFAltllvppehYAAALrwvnrl 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2157 KLKQMADAEMEKHKQFAEKTVRQKEQ--VEgeltkvKLQLEETDHQKAiLDDELGR----LKEEVTESLRQ--KKLVEEE 2228
Cdd:COG4913 509 HLRGRLVYERVRTGLPDPERPRLDPDslAG------KLDFKPHPFRAW-LEAELGRrfdyVCVDSPEELRRhpRAITRAG 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2229 LFKVKIQMEELvKLKLRIEQENkmlILkGKDNTQQfLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAE 2308
Cdd:COG4913 582 QVKGNGTRHEK-DDRRRIRSRY---VL-GFDNRAK-LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2309 KI--LKEKMQAVQEASRLKAEAEMLQK---QKEMAMEQAKKLQEDKEQMQQQLaEETEGFQKTLEAERRRqldISAEAER 2383
Cdd:COG4913 656 YSwdEIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEEL-DELKGEIGRLEKELEQ---AEEELDE 731
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2384 LKLQVVEMSKSQAKAeedakkfrkQAEDISEKLHQTELSTKEKmTVVHTLEIQRQHSDKEAEELRKAIAD 2453
Cdd:COG4913 732 LQDRLEAAEDLARLE---------LRALLEERFAAALGDAVER-ELRENLEERIDALRARLNRAEEELER 791
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1635-1807 |
1.22e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1635 QKANEAlrlRLQAEEIAHKKTL-AQEEAEKQKEDAERETRKRT---KAEESALRQKdlaEEELEKQRKLAEETashklsa 1710
Cdd:PRK12704 42 RILEEA---KKEAEAIKKEALLeAKEEIHKLRNEFEKELRERRnelQKLEKRLLQK---EENLDRKLELLEKR------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1711 EQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKvraemEILLKaksKAEEDSRstSEKSKQMLEV 1790
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAK-----EILLE---KVEEEAR--HEAAVLIKEI 178
|
170
....*....|....*..
gi 1072265250 1791 EasklrELAEEAARLRA 1807
Cdd:PRK12704 179 E-----EEAKEEADKKA 190
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1877-2156 |
1.24e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.00 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1877 KLLEEQAAQHKQDiEEKIHQLKQSSENELERQKtivdETLKHRRvIEEEIRILKINFEKASvgksdlelelQKLKNIADE 1956
Cdd:TIGR02794 46 GAVAQQANRIQQQ-KKPAAKKEQERQKKLEQQA----EEAEKQR-AAEQARQKELEQRAAA----------EKAAKQAEQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1957 TQKSKEKAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEAgrqrkvaleEVERLKIKADEAKKQKDLAEKEAEKqiq 2036
Cdd:TIGR02794 110 AAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQA---------EEEAKAKAAAEAKKKAEEAKKKAEA--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2037 laqdAARLKIDAEEKAyyaavqqkeqemlqtriqeqsiydklkeeaeKAKRAAEEAERAKIKAEHEAALSRQQAEEAerl 2116
Cdd:TIGR02794 178 ----EAKAKAEAEAKA-------------------------------KAEEAKAKAEAAKAKAAAEAAAKAEAEAAA--- 219
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1072265250 2117 kqKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAAL 2156
Cdd:TIGR02794 220 --AAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAA 257
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1668-1885 |
1.30e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1668 AERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSgeqhrivLEEDLfrlkNEVNEAIQ 1747
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK-------LQAEI----AEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1748 RRRgleEELAKVRAEM----------EILLKAKSKAEEDSRStsekskQMLEVEASKLRELAEEAARLRAVSEEAKRQRQ 1817
Cdd:COG3883 83 ERR---EELGERARALyrsggsvsylDVLLGSESFSDFLDRL------SALSKIADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072265250 1818 LAEEDATRQRAEAERILKEKLTAINEATRMRteAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQ 1885
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALL--AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3927-3965 |
1.56e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 44.63 E-value: 1.56e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1072265250 3927 FLEGTSCIAGVYVEASKDRYSIYQAMKKGMIRPGTAFEL 3965
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1671-1906 |
1.67e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.84 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1671 ETRKRTKAEESALRQKDLAEEEL---EKQRKLAEETASHKLSAEQELIR-LKAEVDSGEQHRIVLEEDLFRLKNEVNEAI 1746
Cdd:pfam19220 87 ELVARLAKLEAALREAEAAKEELrieLRDKTAQAEALERQLAAETEQNRaLEEENKALREEAQAAEKALQRAEGELATAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1747 QRRRGLEEELAKVRAEMEILLKAKSKAEedsrSTSEKSKQMLEVEASKLRELAEeaarlRAVSEEAKRQRQLAEEDATRQ 1826
Cdd:pfam19220 167 ERLALLEQENRRLQALSEEQAAELAELT----RRLAELETQLDATRARLRALEG-----QLAAEQAERERAEAQLEEAVE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1827 RAEAERI-LKEKLTAIN---EAT-RMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLK--Q 1899
Cdd:pfam19220 238 AHRAERAsLRMKLEALTaraAATeQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQemQ 317
|
....*..
gi 1072265250 1900 SSENELE 1906
Cdd:pfam19220 318 RARAELE 324
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1997-2410 |
1.67e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1997 QEAGRQRKVALEEVERLKIKADE-AKKQKDLAEKEAEKQiQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIY 2075
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEElEELEEELEELEAELE-ELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2076 DKLKEEAEKAKRAAE-EAERAKIKAEHEAALSRQQAEEAERLKQKAE-IEAQAKGQAQEDAEKVRKEAELEAAKrgqaEQ 2153
Cdd:COG4717 153 ERLEELRELEEELEElEAELAELQEELEELLEQLSLATEEELQDLAEeLEELQQRLAELEEELEEAQEELEELE----EE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2154 AALKLKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELFKVK 2233
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2234 IQMEELVKLKLRIEQENKMLILKGKDNTQQF------LAEEAEKMKQVAEEAARLSVEAQEAARlrkiaEDDLNEQRALA 2307
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELlelldrIEELQELLREAEELEEELQLEELEQEI-----AALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2308 EKILKEKMQAVQEASRLKAEAEMLQKQ--KEMAMEQAKKLQEDKEQMQQQLAEEtegfQKTLEAERRRQLDISAEAERLK 2385
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQleELLGELEELLEALDEEELEEELEEL----EEELEELEEELEELREELAELE 459
|
410 420
....*....|....*....|....*
gi 1072265250 2386 LQVVEMSKSQAKAEEDAKKFRKQAE 2410
Cdd:COG4717 460 AELEQLEEDGELAELLQELEELKAE 484
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1105-1558 |
1.72e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1105 KTYEDQLKEVQTVPGDLKELESSKADLKRMRGQVEGHQPLFNGLENDLTKAREVSERMLKVHSERDvdleryrekvqlLL 1184
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP------------LY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1185 ERWQAIVLQIEVRQRELEQLGKQLRYYRESYEWLIRWITEAKKRQEKIQNVPITDSKTVKEQLMEEKKLLEESEKNRGKV 1264
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1265 DECQKYAKQYIEAIKDfEVQLVTYKAQVEPVVSPLKKPKVHSASDNIIqeyVELRTKYSELTTLTSQYIKFITETLRRLE 1344
Cdd:COG4717 212 EEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLLLIAAAL---LALLGLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1345 EEERTAEKLKEQERKKLAEVED-------QLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVA-----VDAEQ 1412
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQAlpaleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEeleeeLQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1413 QKKTIQQELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDElrALRARAEEAERQKKLAQ 1492
Cdd:COG4717 368 LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELE 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072265250 1493 EEAERLRKQVKDEAQKKREAE--DELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEK 1558
Cdd:COG4717 446 EELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1406-1576 |
1.77e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1406 VAVD---AEQQKKTIQQelhQMKNNSETEIKAKVKLIEEA-EYNRKKVEEEIRIIRIQLE--TSQKQKSGAEDELRALRA 1479
Cdd:PRK09510 53 VMVDpgaVVEQYNRQQQ---QQKSAKRAEEQRKKKEQQQAeELQQKQAAEQERLKQLEKErlAAQEQKKQAEEAAKQAAL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1480 RAEEAERQKKLAQEEAerlrkQVKDEAQKKR------EAEDELHRKVQAE--KDAAREKQKALEDLEKFRLQAEEAerrm 1551
Cdd:PRK09510 130 KQKQAEEAAAKAAAAA-----KAKAEAEAKRaaaaakKAAAEAKKKAEAEaaKKAAAEAKKKAEAEAAAKAAAEAK---- 200
|
170 180
....*....|....*....|....*
gi 1072265250 1552 KQAELEKErqiKQAHDVAQQSADAE 1576
Cdd:PRK09510 201 KKAEAEAK---KKAAAEAKKKAAAE 222
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2006-2243 |
1.80e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.98 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2006 ALEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAyyAAVQQKEQEMlqtriqeQSIYDKLKEEAEKa 2085
Cdd:PRK00409 490 AFEIAKRLGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKA--EEAEALLKEA-------EKLKEELEEKKEK- 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2086 kraaeeaerakikaeheaalsrqQAEEAERLKQKAEIEAQAK-GQAQEDAEKVRKE---AELEAAKRGQAEQAALKLKQM 2161
Cdd:PRK00409 560 -----------------------LQEEEDKLLEEAEKEAQQAiKEAKKEADEIIKElrqLQKGGYASVKAHELIEARKRL 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2162 ADAEMEKHKQFAEKTVRQKEQVEGEltKVKLqleETDHQKAILDDELGrlKEEVTeslrqkklVEEELFKVKIQMEELVK 2241
Cdd:PRK00409 617 NKANEKKEKKKKKQKEKQEELKVGD--EVKY---LSLGQKGEVLSIPD--DKEAI--------VQAGIMKMKVPLSDLEK 681
|
..
gi 1072265250 2242 LK 2243
Cdd:PRK00409 682 IQ 683
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3722-3756 |
1.80e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.80e-05
10 20 30
....*....|....*....|....*....|....*
gi 1072265250 3722 LLDAQAATGFIIDPVKNELLTVDEAVRKGVVGPEI 3756
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1659-2265 |
1.94e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.21 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1659 EEAEKQKEDAERETRKRTKAEESAlrQKDLAE-EELEKQRKLAEETASHKLSAEQELIRLKAEVDSGE----QHRIVLEE 1733
Cdd:TIGR01612 1169 EEIEKKIENIVTKIDKKKNIYDEI--KKLLNEiAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEkkksEHMIKAME 1246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1734 DLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKaEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEeAK 1813
Cdd:TIGR01612 1247 AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD-DKDHHIISKKHDENISDIREKSLKIIEDFSEESDIND-IK 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1814 RQRQLAEEDATRQRAEAERILKE-----KLTAINEATRMRTEAEIALKEKEAENERLR-RLAEDEAYQRKLLEE------ 1881
Cdd:TIGR01612 1325 KELQKNLLDAQKHNSDINLYLNEianiyNILKLNKIKKIIDEVKEYTKEIEENNKNIKdELDKSEKLIKKIKDDinleec 1404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1882 ----QAAQHKQDIEEKIHQLKQSsENELERQKTIVDETLKHRRVIEEEIRILKINFEKASV------------GKSDLEL 1945
Cdd:TIGR01612 1405 kskiESTLDDKDIDECIKKIKEL-KNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNksqhilkikkdnATNDHDF 1483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1946 ELQKLKNIADETQKSKEKAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAE-----QEAGRQRKVALEEVERLKIKAD-E 2019
Cdd:TIGR01612 1484 NINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAiknkfAKTKKDSEIIIKEIKDAHKKFIlE 1563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2020 AKKQKDLAEKEAEKQIQLAQDAArlKIDAEEKA---YYAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAE---EAE 2093
Cdd:TIGR01612 1564 AEKSEQKIKEIKKEKFRIEDDAA--KNDKSNKAaidIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSfsiDSQ 1641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2094 RAKIKAEHEAALSRQqaEEAERLK-QKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMADA---EMEKH 2169
Cdd:TIGR01612 1642 DTELKENGDNLNSLQ--EFLESLKdQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIAnkeEIESI 1719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2170 KQFAEKTVrqkEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEELFKVKIQMEELVklKLRIEQE 2249
Cdd:TIGR01612 1720 KELIEPTI---ENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIK--NTRINAQ 1794
|
650
....*....|....*..
gi 1072265250 2250 NKML-ILKGKDNTQQFL 2265
Cdd:TIGR01612 1795 NEFLkIIEIEKKSKSYL 1811
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2289-2556 |
1.96e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2289 AARLRKIAEDDLnEQRALAE--KILKEKMQAVQEasrlkaEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKT 2366
Cdd:PHA02562 149 APARRKLVEDLL-DISVLSEmdKLNKDKIRELNQ------QIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2367 LEAERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQ--TELSTKEKMTVVHTLEIQRQHSDKEA 2444
Cdd:PHA02562 222 YDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQfqKVIKMYEKGGVCPTCTQQISEGPDRI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2445 EELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQlrqetQTLQSTFLTEKQILIQKEKYIEEEKAKLEKL------ 2518
Cdd:PHA02562 302 TKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL-----LELKNKISTNKQSLITLVDKAKKVKAAIEELqaefvd 376
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1072265250 2519 FDNEVGKAQKLKSEKERQLAQLEEEK--RLLQTSM--DDAMK 2556
Cdd:PHA02562 377 NAEELAKLQDELDKIVKTKSELVKEKyhRGIVTDLlkDSGIK 418
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
42-146 |
1.96e-05 |
|
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: 46.88 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 42 DRVQKKTFTKWVNKHLIKhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPREKG--RMRFHKLQNVQIALDFLKLR 119
Cdd:cd21285 8 NGFDKQIYTDWANHYLAK---SGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAK 84
|
90 100
....*....|....*....|....*..
gi 1072265250 120 QVKLVNIRNDDIADGNPKLTLGLIWTI 146
Cdd:cd21285 85 GINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1782-2115 |
2.15e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.45 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1782 EKSK-QMLEVEAsKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILkeklTAINEATRMRTEAEIALKEKEA 1860
Cdd:pfam19220 44 PQAKsRLLELEA-LLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLE----AALREAEAAKEELRIELRDKTA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1861 ENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLkQSSENELerqktivDETLKHRRVIEEEIRILKINFEKASVGK 1940
Cdd:pfam19220 119 QAEALERQLAAETEQNRALEEENKALREEAQAAEKAL-QRAEGEL-------ATARERLALLEQENRRLQALSEEQAAEL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1941 SDLELELQKLKNIADETQKSKEK-----AEQDAEKQRQLALVEEARRKEAEEK----------------VKKIIAAEQEA 1999
Cdd:pfam19220 191 AELTRRLAELETQLDATRARLRAlegqlAAEQAERERAEAQLEEAVEAHRAERaslrmklealtaraaaTEQLLAEARNQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2000 GRQRKVALEEVERlkiKADEAKKQKDLAEK-------EAEKQIQLAQDAARLKIDAEE------KAYYA---AVQQKEQE 2063
Cdd:pfam19220 271 LRDRDEAIRAAER---RLKEASIERDTLERrlagleaDLERRTQQFQEMQRARAELEEraemltKALAAkdaALERAEER 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 2064 M--LQTRIQEQSiydklkeeaekakrAAEEAERAKIKAEHEAALSRQQAEEAER 2115
Cdd:pfam19220 348 IasLSDRIAELT--------------KRFEVERAALEQANRRLKEELQRERAER 387
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
620-710 |
2.23e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.17 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 620 FVAAATKELMWLNDKEEEEVNFDWSDRNTNMTSKKDNYSGLMRELELKEKKIKEIQNTGDRLLRDDHPGKSTIEAFQAAL 699
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEEL 82
|
90
....*....|.
gi 1072265250 700 QTQWSWMLQLC 710
Cdd:smart00150 83 NERWEELKELA 93
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4135-4163 |
2.24e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.24e-05
10 20
....*....|....*....|....*....
gi 1072265250 4135 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4163
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1850-2214 |
2.48e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1850 EAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKtivdETLKHRRVIEEEIRIL 1929
Cdd:pfam13868 10 ELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKE----ERKRYRQELEEQIEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1930 KINFEKASVGKsdLELELQKLKNIADETQKSKEKAEQDAEKQRQLAlveearrkeaeEKVKKIIAaEQEAGRQRKVALEE 2009
Cdd:pfam13868 86 EQKRQEEYEEK--LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLR-----------EEIDEFNE-EQAEWKELEKEEER 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2010 VERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEqsiydklkEEAEKAKRAA 2089
Cdd:pfam13868 152 EEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQE--------EQERKERQKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2090 EEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEaqakgQAQEDAEKV-RKEAELEAAKRGQAEQAALKLKQMADaemEK 2168
Cdd:pfam13868 224 REEAEKKARQRQELQQAREEQIELKERRLAEEAE-----REEEEFERMlRKQAEDEEIEQEEAEKRRMKRLEHRR---EL 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1072265250 2169 HKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEE 2214
Cdd:pfam13868 296 EKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2205-2413 |
2.92e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2205 DDELGRLKEEVTESLRQKKLVEEELFKVKIQMEELVKLKLRIEQENKMLILKgKDNTQQFLAEEAEKMKQVAEEAARLSV 2284
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2285 EAQEAARLRKIAE--------DDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQL 2356
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 2357 AEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDIS 2413
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1358-1515 |
2.96e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1358 RKKLAEVEDQLEKQRQLAEAhAQAKAVAEKEALElrmNMQEEVTRREVVAVDAEQQKKTIQQELHQMKNNseTEIKAKVK 1437
Cdd:COG1579 23 EHRLKELPAELAELEDELAA-LEARLEAAKTELE---DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN--KEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072265250 1438 LIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDE 1515
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2180-2574 |
3.31e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 50.40 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2180 KEQVEGELTKVKLQLEETDH-QKAILDDELGRLKeevTESLRQKKLVEEELfKVKIQMEELVKLKLRIEQENKMLILKGK 2258
Cdd:NF033838 64 ESHLEKILSEIQKSLDKRKHtQNVALNKKLSDIK---TEYLYELNVLKEKS-EAELTSKTKKELDAAFEQFKKDTLEPGK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2259 DNTQ-QFLAEEAEKMKQVAEEAARLSVEAQEAARLR-KIAEDDLNEQRALAEkILKEKMQAVQEASRLK-AEAEMLQKQK 2335
Cdd:NF033838 140 KVAEaTKKVEEAEKKAKDQKEEDRRNYPTNTYKTLElEIAESDVEVKKAELE-LVKEEAKEPRDEEKIKqAKAKVESKKA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2336 EMAmeQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDisEK 2415
Cdd:NF033838 219 EAT--RLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGE--ET 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2416 LHQTELSTKEKMTvvhtleiqrqhsdkEAEelrkaiadlenekeklkkeaellqKKSEEMQK---AQKEQLRQETQTlqS 2492
Cdd:NF033838 295 LPSPSLKPEKKVA--------------EAE------------------------KKVEEAKKkakDQKEEDRRNYPT--N 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2493 TFLTEKQILIQKEKYIEEEKAKLEKLFDNEVGKAQKLKSEKERQLAQLEEEKRLLQTSMD-----DAMKKQLDAEDRIRQ 2567
Cdd:NF033838 335 TYKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDrkkaeEEAKRKAAEEDKVKE 414
|
....*..
gi 1072265250 2568 KQEELQQ 2574
Cdd:NF033838 415 KPAEQPQ 421
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1121-1565 |
3.63e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1121 LKELESSKADLKRMRGQVEGHQPLFNGLEnDLTKAREVSERMLKVHSERDVDLERYREkVQLLLERWQAIVLQIEVRQRE 1200
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1201 LEQLGKQLRYYRESYEWLIRWITEAKKRQEKIQNVPITDSKTVKEQLMEEKKLLEESEKNRGKVDECQKYAKQYIEAIKD 1280
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1281 fEVQLVTYKAQVEPVVSPLKKPKVHSASDNIIqeyVELRTKYSELTTLTSQYIKFITETLRRLEEEERTAEKLKEQERKK 1360
Cdd:COG4717 228 -ELEQLENELEAAALEERLKEARLLLLIAAAL---LALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1361 LAEVED-------QLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVA-----VDAEQQKKTIQQELHQMKNNS 1428
Cdd:COG4717 304 AEELQAlpaleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEeleeeLQLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1429 ETEIKAKVKLIEEaeynRKKVEEEIRIIRIQLEtsqkqksgaedelralrarAEEAERQKKLAQEEAERLRKQVKDEAQK 1508
Cdd:COG4717 384 EEELRAALEQAEE----YQELKEELEELEEQLE-------------------ELLGELEELLEALDEEELEEELEELEEE 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 1509 KREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQA 1565
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1397-1580 |
3.89e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.95 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1397 QEEVTRREVVAVDAEQQKKTIQ---QELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQksgaEDE 1473
Cdd:pfam15709 330 QEKASRDRLRAERAEMRRLEVErkrREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR----QEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1474 LRALRARAEEAERQKKLAQEEA------ERLRKQVKDEAQKkreAEDELHRKVQAEKDAAREKQKALEDLEKFRL----Q 1543
Cdd:pfam15709 406 EERKQRLQLQAAQERARQQQEEfrrklqELQRKKQQEEAER---AEAEKQRQKELEMQLAEEQKRLMEMAEEERLeyqrQ 482
|
170 180 190
....*....|....*....|....*....|....*..
gi 1072265250 1544 AEEAERRMKQAELEKERQIKQAHDVAQQSADAELQSK 1580
Cdd:pfam15709 483 KQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQ 519
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3095-3131 |
4.19e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.19e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1072265250 3095 KLLSAEKAVTGYKDPYTGQALSLFQALKKGLIPKDSG 3131
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1456-1570 |
4.34e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 50.08 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1456 IRIQLETSQKQKSGAEDELRALRARAEEAER-QKKLAQEEAERLRkqvkDEAQKKREAEDELHRKVQAEKDAAREKQKAL 1534
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKeQDEASFERLAELR----DELAELEEELEALKARWEAEKELIEEIQELK 477
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1072265250 1535 EDLEK--FRLQAEEAERRMKQAELEKERQIKQ----AHDVAQ 1570
Cdd:COG0542 478 EELEQryGKIPELEKELAELEEELAELAPLLReevtEEDIAE 519
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1528-1720 |
4.67e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.49 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1528 REKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAhDVAQQSADAELQSKRmsflekttqlemslkqEHITVTHLQE 1607
Cdd:COG2268 180 EDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIA-QANREAEEAELEQER----------------EIETARIAEA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1608 EAERLKKQ---QLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEesalR 1684
Cdd:COG2268 243 EAELAKKKaeeRREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAE----K 318
|
170 180 190
....*....|....*....|....*....|....*.
gi 1072265250 1685 QKDLAEEELEKQRKLAeetashKLSAEQELIRLKAE 1720
Cdd:COG2268 319 QAAEAEAEAEAEAIRA------KGLAEAEGKRALAE 348
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1634-1971 |
4.68e-05 |
|
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: 49.51 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1634 RQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKlaEETASHKLSAEQE 1713
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYK--ELSASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1714 LIRLKAEVDSgeQHRIV-LEEDLFRLKnevneaiQRRRGLEEELAKVRAEMEILLkAKSKAEEDSRSTSEKSKQMLEVEa 1792
Cdd:pfam07888 118 DALLAQRAAH--EARIReLEEDIKTLT-------QRVLERETELERMKERAKKAG-AQRKEEEAERKQLQAKLQQTEEE- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1793 skLRELAEEAARLRAVSEEAKRQRQLAEEDATR--------QRAEAE-RILKEKLTAINEATRMRTEAEIALKEKEAENE 1863
Cdd:pfam07888 187 --LRSLSKEFQELRNSLAQRDTQVLQLQDTITTltqklttaHRKEAEnEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1864 RLRRLAEDEAYQRKL---------------LEEQAAQHKQDIEekihQLKQSSENELERQKTIVDETLK-HRRVIEEEIR 1927
Cdd:pfam07888 265 AQRDRTQAELHQARLqaaqltlqladaslaLREGRARWAQERE----TLQQSAEADKDRIEKLSAELQRlEERLQEERME 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1928 ILKINFEKAS------VGKSDLELELQKLKNIADETQKSKEkaEQDAEKQ 1971
Cdd:pfam07888 341 REKLEVELGRekdcnrVQLSESRRELQELKASLRVAQKEKE--QLQAEKQ 388
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1900-2155 |
4.79e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1900 SSENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLalvee 1979
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1980 arrkeaeekVKKIIAAEQEAG-----------------------------RQRKVALEEVERLKIKADEAKKQkdlAEKE 2030
Cdd:COG3883 88 ---------LGERARALYRSGgsvsyldvllgsesfsdfldrlsalskiaDADADLLEELKADKAELEAKKAE---LEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2031 AEKQIQLAQDAARLKIDAEEkayyaavQQKEQEMLQTRIQEQsiydklKEEAEKAKRAAEEAERAKIKAEHEAALSRQQA 2110
Cdd:COG3883 156 LAELEALKAELEAAKAELEA-------QQAEQEALLAQLSAE------EAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1072265250 2111 EEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAA 2155
Cdd:COG3883 223 AAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGA 267
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1354-2086 |
4.84e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1354 KEQER-----KKLAEVEDQ---LEKQRQLAEAHAQ------------AKAVAEKEALELRMNMQEEVTR--REVVAvDAE 1411
Cdd:PRK04863 304 AEQYRlvemaRELAELNEAesdLEQDYQAASDHLNlvqtalrqqekiERYQADLEELEERLEEQNEVVEeaDEQQE-ENE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1412 QQKKTIQQELHQMKNnseteikakvkliEEAEYNRKKVEEEIRIIRIQ-----LETSQKQKSGAEDELRALRARAEEAER 1486
Cdd:PRK04863 383 ARAEAAEEEVDELKS-------------QLADYQQALDVQQTRAIQYQqavqaLERAKQLCGLPDLTADNAEDWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1487 QKKLAQEEAERLRKQ--VKDEAQKKREAEDELHRKVQAEKDAAREKQKA---LEDLEKFRLQAEEAE-RRMKQAELEKER 1560
Cdd:PRK04863 450 KEQEATEELLSLEQKlsVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVArelLRRLREQRHLAEQLQqLRMRLSELEQRL 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1561 QIKQahDVAQQSADAELQSKRMsfLEKTTQLEMSLKQEHITVTHLQEEAER-------LKKQQLEAETAKEEAEKELEKW 1633
Cdd:PRK04863 530 RQQQ--RAERLLAEFCKRLGKN--LDDEDELEQLQEELEARLESLSESVSEarerrmaLRQQLEQLQARIQRLAARAPAW 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1634 RQkANEAL-RLRLQAEE--------IAHKKTLAQEEAEKQKEDAERETRKRT-KAEESALRQKDLAEeeLEKQRKLAEET 1703
Cdd:PRK04863 606 LA-AQDALaRLREQSGEefedsqdvTEYMQQLLERERELTVERDELAARKQAlDEEIERLSQPGGSE--DPRLNALAERF 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1704 ASHKLSAEQELIRLKaevDSGE--------QHRIV-----------------------LEEDLFRLKNEVNEA------- 1745
Cdd:PRK04863 683 GGVLLSEIYDDVSLE---DAPYfsalygpaRHAIVvpdlsdaaeqlagledcpedlylIEGDPDSFDDSVFSVeelekav 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1746 ----------IQR--------RRGLEEELAKVRAEMEILLKAKSKAEEDSR---STSEKSKQMLEVEASkLRELAEEAAR 1804
Cdd:PRK04863 760 vvkiadrqwrYSRfpevplfgRAAREKRIEQLRAEREELAERYATLSFDVQklqRLHQAFSRFIGSHLA-VAFEADPEAE 838
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1805 LRAVSEE-AKRQRQLAE-EDATRQRAEAERILKEKLTAINeatrmRTEAEIALKEKEAENERLRRLAEdeayQRKLLEEQ 1882
Cdd:PRK04863 839 LRQLNRRrVELERALADhESQEQQQRSQLEQAKEGLSALN-----RLLPRLNLLADETLADRVEEIRE----QLDEAEEA 909
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1883 AA---QHKQDIE--EKIHQLKQSSENELERQKTIVDETLKHRRVIEEEIRILK-INFEKASVGKSDLELELQKLKNIADE 1956
Cdd:PRK04863 910 KRfvqQHGNALAqlEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTeVVQRRAHFSYEDAAEMLAKNSDLNEK 989
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1957 TQKSKEKAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEakkqkDLAEKEAEKQIQ 2036
Cdd:PRK04863 990 LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADS-----GAEERARARRDE 1064
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 2037 LAQD--AARLKIDAEEKAYyaAVQQKEQEMLQTRIQE-QSIYDKLKEEAEKAK 2086
Cdd:PRK04863 1065 LHARlsANRSRRNQLEKQL--TFCEAEMDNLTKKLRKlERDYHEMREQVVNAK 1115
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1952-2138 |
4.92e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.49 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1952 NIADETQKSKEKAEQDAEKQRQLAlveearrkeaEEKVKKIIAAEQEAGRQRKVALE--EVERLKIKADEAKkqkDLAEK 2029
Cdd:COG2268 207 EAERETEIAIAQANREAEEAELEQ----------EREIETARIAEAEAELAKKKAEErrEAETARAEAEAAY---EIAEA 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2030 EAEKQIQLAQDAARLK--IDAEEKAyyaavQQKEQEMLQTRIQEQSIYDKLKEEAE-----KAKRAAEEAERAKIKAEHE 2102
Cdd:COG2268 274 NAEREVQRQLEIAEREreIELQEKE-----AEREEAELEADVRKPAEAEKQAAEAEaeaeaEAIRAKGLAEAEGKRALAE 348
|
170 180 190
....*....|....*....|....*....|....*.
gi 1072265250 2103 AALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVR 2138
Cdd:COG2268 349 AWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
2075-2164 |
5.42e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 49.48 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2075 YDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAeieaqakgqaqeDAEKVRKEAELEAAKRGQAEQA 2154
Cdd:PRK12472 192 AETLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARA------------DAELKRADKALAAAKTDEAKAR 259
|
90
....*....|
gi 1072265250 2155 ALKLKQMADA 2164
Cdd:PRK12472 260 AEERQQKAAQ 269
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1709-1904 |
5.50e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1709 SAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQML 1788
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1789 EV------EASKL------RELAEEAARLRAVSEEAKRQRQLAEEdATRQRAEAERILKEKLTAINEATRMRTEAEIALK 1856
Cdd:COG3883 93 RAlyrsggSVSYLdvllgsESFSDFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1072265250 1857 EKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENE 1904
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4273-4306 |
5.57e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 5.57e-05
10 20 30
....*....|....*....|....*....|....
gi 1072265250 4273 EETGPIAGIVDTDTLEKVSITEAMHRNLVDNITG 4306
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2267-2411 |
5.57e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.18 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2267 EEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEA---EMLQKQKEMAMEQAK 2343
Cdd:pfam15709 366 EQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQELQRKKQQEEAE 445
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072265250 2344 KLQEDKE---QMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQvvEMSKSQAKAEEDAK----KFRKQAED 2411
Cdd:pfam15709 446 RAEAEKQrqkELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARL--EAEERRQKEEEAARlaleEAMKQAQE 518
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1768-2058 |
5.73e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1768 KAKSKAEEDSRSTSEKSKQmlEVEASKLRELAEEAARLrAVSEEAKRQRQLAEEDAtrqRAEAERILKEKLTAINEATRM 1847
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAKA--RFEARQARLEREKAARE-ARHKKAAEARAAKDKDA---VAAALARVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1848 RTEAEIALKEKEAEnERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLK-QSSENELERQKTIVDETLKhrrvieeei 1926
Cdd:PRK05035 509 KAGARPDNSAVIAA-REARKAQARARQAEKQAAAAADPKKAAVAAAIARAKaKKAAQQAANAEAEEEVDPK--------- 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1927 rilkinfeKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLALVEEARRKEAEEKvKKIIAAEQEAGRQRKVA 2006
Cdd:PRK05035 579 --------KAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQ-ANAEPEEPVDPRKAAVA 649
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 2007 LEeVERlkIKADEAKKQKDLAEKEAEKQIQLAQDAARLkidAEEKAYYAAVQ 2058
Cdd:PRK05035 650 AA-IAR--AKARKAAQQQANAEPEEAEDPKKAAVAAAI---ARAKAKKAAQQ 695
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1880-2218 |
6.20e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 49.24 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1880 EEQAAQHKQDIEEKIHQLKQSSENELERQKTI--VDETLKHRRVIEEEIRILKINFEKA-----SVGKSDLELELQKLK- 1951
Cdd:NF033838 53 NESQKEHAKEVESHLEKILSEIQKSLDKRKHTqnVALNKKLSDIKTEYLYELNVLKEKSeaeltSKTKKELDAAFEQFKk 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1952 ------NIADETQKSKEKAEQDAEKQRQLALVEEARRKEAEEKVK------KIIAAEQEAGRQRkvALEEVERLKIKADE 2019
Cdd:NF033838 133 dtlepgKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEiaesdvEVKKAELELVKEE--AKEPRDEEKIKQAK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2020 AKKQKDLAEKEAEKQIQL----AQDAARLKIDAEEKAYYAA-VQQKEQEMLQTRI-----QEQSIYDKlKEEAEKAKRAA 2089
Cdd:NF033838 211 AKVESKKAEATRLEKIKTdrekAEEEAKRRADAKLKEAVEKnVATSEQDKPKRRAkrgvlGEPATPDK-KENDAKSSDSS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2090 ---EEAERAKIKAEHEAAlsrqqaeEAErlKQKAEIEAQAKGQAQED----------------AE---KVrKEAELEAAK 2147
Cdd:NF033838 290 vgeETLPSPSLKPEKKVA-------EAE--KKVEEAKKKAKDQKEEDrrnyptntyktleleiAEsdvKV-KEAELELVK 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072265250 2148 RGQAEQAALKLKQMADAEMEKHKqfAEKTvrqkeQVEGELTKVKlQLEETDHQKAILDDelgRLKEEVTES 2218
Cdd:NF033838 360 EEAKEPRNEEKIKQAKAKVESKK--AEAT-----RLEKIKTDRK-KAEEEAKRKAAEED---KVKEKPAEQ 419
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3463-3499 |
6.46e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 6.46e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1072265250 3463 IRLLEAQVATGGIIDPVHSHRVPIDVAYKRGYFDEAM 3499
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1415-1545 |
6.64e-05 |
|
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: 49.29 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1415 KTIQQELHQM---KNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDEL-------RALRARAEEA 1484
Cdd:pfam05911 684 KRLKEEFEQLkseKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLkcmaesyEDLETRLTEL 763
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 1485 ERQKKLAQEEAERLRKQVKDEAQKKREAEDELHR-KVQAEKDAAREKQKALEDLEKFRLQAE 1545
Cdd:pfam05911 764 EAELNELRQKFEALEVELEEEKNCHEELEAKCLElQEQLERNEKKESSNCDADQEDKKLQQE 825
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1899-2453 |
7.09e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1899 QSSENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQdAEKQRQLALVE 1978
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKT-AESDLSMELEK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1979 EARRKEAEEKVKKIIAAEQEAGRQRKvaleeVERLKIKADEAKKQKDLaeKEAEKQIQLAQDAARLKIDAEEKAYYAAVQ 2058
Cdd:PRK01156 272 NNYYKELEERHMKIINDPVYKNRNYI-----NDYFKYKNDIENKKQIL--SNIDAEINKYHAIIKKLSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2059 QKEQEMLQTRIqeqsiyDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIeaqakgqaqeDAEKVR 2138
Cdd:PRK01156 345 KSRYDDLNNQI------LELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEI----------DPDAIK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2139 KEAELEAAKRGQAEQAALKLKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTES 2218
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREI 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2219 LRQKKLVEEELFKVKIQMEELVKLKLR--IEQENKM----LILKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQEAAR- 2291
Cdd:PRK01156 489 EIEVKDIDEKIVDLKKRKEYLESEEINksINEYNKIesarADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRt 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2292 -----LRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMA---MEQAKKLQEDKEQMQQQLAEETEGF 2363
Cdd:PRK01156 569 swlnaLAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSireIENEANNLNNKYNEIQENKILIEKL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2364 QKTLEAERRRQLDISAEAERLKlqvvEMSKSQAKAEEDAKKFRKQAEDIseKLHQTELSTKEKMTVVHTLEIQRQHSDKE 2443
Cdd:PRK01156 649 RGKIDNYKKQIAEIDSIIPDLK----EITSRINDIEDNLKKSRKALDDA--KANRARLESTIEILRTRINELSDRINDIN 722
|
570
....*....|....*
gi 1072265250 2444 -----AEELRKAIAD 2453
Cdd:PRK01156 723 etlesMKKIKKAIGD 737
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2068-2603 |
7.26e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.97 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2068 RIQEQSIYDKLKEEAekaKRAAEEAERAKIKAEHEA-ALSRQQAEEAERLKQkaeieaqakgqAQEDAEKVRK-EAELEA 2145
Cdd:pfam05557 4 LIESKARLSQLQNEK---KQMELEHKRARIELEKKAsALKRQLDRESDRNQE-----------LQKRIRLLEKrEAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2146 AKRGQAEQAALKLKQMADAEmekhkqfaeKTVRQKEQVEGELTKVKL----QLEETDHQKAILDDELGRLKEEVTESLRQ 2221
Cdd:pfam05557 70 ALREQAELNRLKKKYLEALN---------KKLNEKESQLADAREVISclknELSELRRQIQRAELELQSTNSELEELQER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2222 KKLVEEELFKVKIQMEEL-VKLKLRIEQENKMLILKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQ----EAARLRKIA 2296
Cdd:pfam05557 141 LDLLKAKASEAEQLRQNLeKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELEKELErlreHNKHLNENI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2297 EDDLneqralaekILKEkmqavqEASRLKAEAEmlqkQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKT---------- 2366
Cdd:pfam05557 221 ENKL---------LLKE------EVEDLKRKLE----REEKYREEAATLELEKEKLEQELQSWVKLAQDTglnlrspedl 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2367 ---LEAERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTE-----------LSTKEKMTVVHT 2432
Cdd:pfam05557 282 srrIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKalvrrlqrrvlLLTKERDGYRAI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2433 LE------IQRQHSDKEAEELRKAiADLENEKEKLKKEAELLQKKSEEMQKAQKEQLRQETQTLQSTfltEKQILIQKEK 2506
Cdd:pfam05557 362 LEsydkelTMSNYSPQLLERIEEA-EDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQAL---RQQESLADPS 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2507 YIEEEKAKLEKLFDNEVGKAQKLKSEKERQlaQLEEEKRLLQTSMDDAMKKQLD-----AEDRIRQKQEELQQLDKKrqe 2581
Cdd:pfam05557 438 YSKEEVDSLRRKLETLELERQRLREQKNEL--EMELERRCLQGDYDPKKTKVLHlsmnpAAEAYQQRKNQLEKLQAE--- 512
|
570 580
....*....|....*....|..
gi 1072265250 2582 qerlleeeNRKLRERLEQLEQE 2603
Cdd:pfam05557 513 --------IERLKRLLKKLEDD 526
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1954-2164 |
7.45e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1954 ADETQKSKEKAEQDAEKQRQLALveearrkeaeEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKE-AE 2032
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----------AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2033 KQIQLAQDAARLKIDAEEKAYYAA-------------------VQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEE-- 2091
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVllgsesfsdfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEAlk 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 2092 AERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMADA 2164
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
187-264 |
7.50e-05 |
|
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: 44.60 E-value: 7.50e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072265250 187 DNFTSNWRDGRLFSAIIHRHKPMLIDMNRVYRQTNLENLDQAFTvAERELGVTRLLDPEDVDVPQPDEKSIITYVSSL 264
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1739-1861 |
7.70e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.05 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1739 KNEVNEAIQRRRGLEEELAKVRAEMEILLKaksKAEEDSRSTSEKSKQMLEVEASKLRELAEEA--ARLRAVSEEAKRQR 1816
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLK---EAEKLKEELEEKKEKLQEEEDKLLEEAEKEAqqAIKEAKKEADEIIK 591
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1072265250 1817 QLAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAE 1861
Cdd:PRK00409 592 ELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1350-1565 |
7.77e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.30 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1350 AEKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEvtrrevvavdAEQQKKtiqqelhqmknnse 1429
Cdd:TIGR02794 80 AEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQA----------AEAKAK-------------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1430 TEIKAKVKLIEEAeynRKKVEEEiriiRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEE----AERLRKQVKDE 1505
Cdd:TIGR02794 136 AEAEAERKAKEEA---AKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKAKAAAE 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 1506 AQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEKER---QIKQA 1565
Cdd:TIGR02794 209 AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKyaaIIQQA 271
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3058-3091 |
8.01e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 8.01e-05
10 20 30
....*....|....*....|....*....|....
gi 1072265250 3058 LLEAQAGTGFIIDPVTKELLPVDEAVKAGIVGPE 3091
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2206-2421 |
8.06e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2206 DELGRLKEEVTESLRQKKLVEeelFKVKIQMEELvKLKLRIEQEnkmlilKGKDNTQQFLAEEAEKmKQvAEEAARLSVE 2285
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRK---KKEQQQAEEL-QQKQAAEQE------RLKQLEKERLAAQEQK-KQ-AEEAAKQAAL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2286 AQeaarlrKIAEDDLNEQRALAEKILKEKMQAVQEASRlKAEAEmlQKQKEMAMEQAKKLQEDKEQMQ---QQLAEETEG 2362
Cdd:PRK09510 130 KQ------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAE--AKKKAEAEAAKKAAAEAKKKAEaeaAAKAAAEAK 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1072265250 2363 FQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTEL 2421
Cdd:PRK09510 201 KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2237-2615 |
9.58e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2237 EELVKLKLRIEQenkmlilkgkdnTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEddlnEQRALAEKILKEKMQ 2316
Cdd:pfam01576 12 EELQKVKERQQK------------AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAE----EMRARLAARKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2317 AVQE-ASRLKAEAEMLQKqkemAMEQAKKLQEDKEQMQQQLAEETEGFQK------TLEAERRRQLD-----------IS 2378
Cdd:pfam01576 76 ILHElESRLEEEEERSQQ----LQNEKKKMQQHIQDLEEQLDEEEAARQKlqlekvTTEAKIKKLEEdillledqnskLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2379 AEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAEELRKAIADLENEK 2458
Cdd:pfam01576 152 KERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2459 EKLKKEAellQKKSEEMQKAQkeqLRQETQTLQstflteKQILIQKEKYIEEEKAKLEKLFDNEvgKAQKLKSEKERQla 2538
Cdd:pfam01576 232 AELRAQL---AKKEEELQAAL---ARLEEETAQ------KNNALKKIRELEAQISELQEDLESE--RAARNKAEKQRR-- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2539 QLEEEKRLLQTSMDDAMKKQlDAEDRIRQKQE-ELQQLDKKRQEQERLLEEENRKLRER--------LEQLEQEHR--IA 2607
Cdd:pfam01576 296 DLGEELEALKTELEDTLDTT-AAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQKhtqaleelTEQLEQAKRnkAN 374
|
....*...
gi 1072265250 2608 LEKTREVI 2615
Cdd:pfam01576 375 LEKAKQAL 382
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1646-1822 |
1.02e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1646 QAEEIAHKKTLAQE---EAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAeetashKLSAEQELIRLKAEVD 1722
Cdd:PRK09510 88 QAEELQQKQAAEQErlkQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAA------KAKAEAEAKRAAAAAK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1723 SGEQHRIVLEEDLFRLKNEVN---EAIQRRRGLEEELAKVRAEMEillkAKSKAEEDSRSTSEKSKQMLEVEASKLRELA 1799
Cdd:PRK09510 162 KAAAEAKKKAEAEAAKKAAAEakkKAEAEAAAKAAAEAKKKAEAE----AKKKAAAEAKKKAAAEAKAAAAKAAAEAKAA 237
|
170 180
....*....|....*....|...
gi 1072265250 1800 EEAARLRAVSEEAKRQRQLAEED 1822
Cdd:PRK09510 238 AEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1473-1951 |
1.02e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.58 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1473 ELRALRARAEEAERQKKlaQEEAERLRKQVkdEAQKKREAedeLHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERrmk 1552
Cdd:pfam05557 3 ELIESKARLSQLQNEKK--QMELEHKRARI--ELEKKASA---LKRQLDRESDRNQELQKRIRLLEKREAEAEEALR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1553 qAELEKERQIKQAHDVAQQsadaeLQSKRMSFLEKTTQLEMSLKQEhitVTHLQEEAERLKKQQLEAETAKEEAEKELEK 1632
Cdd:pfam05557 73 -EQAELNRLKKKYLEALNK-----KLNEKESQLADAREVISCLKNE---LSELRRQIQRAELELQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1633 WRQKANEALRLRLQAEeiAHKKTLAqeEAEKQKEDAERETRKR------TKAEESALRQKDLAEEELEKQR---KLAEET 1703
Cdd:pfam05557 144 LKAKASEAEQLRQNLE--KQQSSLA--EAEQRIKELEFEIQSQeqdseiVKNSKSELARIPELEKELERLRehnKHLNEN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1704 ASHKLSAEQELIRLKAEVDSGEQHR---IVLEEDLFRLKNEVNEAIQRRRGLEEELAK---VRAEMEILLKaKSKAEEDS 1777
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLEREEKYReeaATLELEKEKLEQELQSWVKLAQDTGLNLRSpedLSRRIEQLQQ-REIVLKEE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1778 RSTSEKSKQMLEveaSKLRELAEEAARLRAVSEEAKRQRQlaeedatRQRAEAERILKEKLTAINEATRMRTEAEIALKE 1857
Cdd:pfam05557 299 NSSLTSSARQLE---KARRELEQELAQYLKKIEDLNKKLK-------RHKALVRRLQRRVLLLTKERDGYRAILESYDKE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1858 KEAEN------ERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKTIVDETLKHRRVIEEEIRILKI 1931
Cdd:pfam05557 369 LTMSNyspqllERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRR 448
|
490 500
....*....|....*....|
gi 1072265250 1932 NFEkasvgksDLELELQKLK 1951
Cdd:pfam05557 449 KLE-------TLELERQRLR 461
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1775-1973 |
1.03e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.41 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1775 EDSRSTSEKSKQML---EVEASKLRELAEEAARLRAVseEAKRQRQLAEEDATRQRAEAERilKEKLTAINEATRMRTEA 1851
Cdd:pfam15709 312 EEERSEEDPSKALLekrEQEKASRDRLRAERAEMRRL--EVERKRREQEEQRRLQQEQLER--AEKMREELELEQQRRFE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1852 EIALKEKEAENERLRRLAED--EAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENElERQKTIVDEtlkhRRVIEEEIRIL 1929
Cdd:pfam15709 388 EIRLRKQRLEEERQRQEEEErkQRLQLQAAQERARQQQEEFRRKLQELQRKKQQE-EAERAEAEK----QRQKELEMQLA 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1072265250 1930 KinFEKASVGKSDLE-LELQKLKniadetQKSKEKAEQDAEKQRQ 1973
Cdd:pfam15709 463 E--EQKRLMEMAEEErLEYQRQK------QEAEEKARLEAEERRQ 499
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1961-2217 |
1.05e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.06 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1961 KEKAEQDA-----EKQRQLALVEEARRKEAEEKVKKIiaaEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQI 2035
Cdd:NF012221 1564 KERAEADRqrleqEKQQQLAAISGSQSQLESTDQNAL---ETNGQAQRDAILEESRAVTKELTTLAQGLDALDSQATYAG 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2036 QLAQD-----AARLKIDAEEKAYYAA--VQQKEQEMLQTRIQEQSiydKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQ 2108
Cdd:NF012221 1641 ESGDQwrnpfAGGLLDRVQEQLDDAKkiSGKQLADAKQRHVDNQQ---KVKDAVAKSEAGVAQGEQNQANAEQDIDDAKA 1717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2109 QAEeaerlkqKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQ---MADAEMEKHKQfAEKTVRQKEQVEG 2185
Cdd:NF012221 1718 DAE-------KRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKAnqaQADAKGAKQDE-SDKPNRQGAAGSG 1789
|
250 260 270
....*....|....*....|....*....|....*..
gi 1072265250 2186 eLTKVKLQLEETDHQKAILDDEL-----GRLKEEVTE 2217
Cdd:NF012221 1790 -LSGKAYSVEGVAEPGSHINPDSpaaadGRFSEGLTE 1825
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1997-2212 |
1.11e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1997 QEAGRQRKVALEEVERLKIKADEAKKQKDLAEKE---AEKQIQLAQDAARlKIDAEEKAYYAAVQQKEQEMLQTRIQEQS 2073
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQlaaLERRIAALARRIR-ALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2074 IYDKLKEEAEKAKR-----------AAEEAERAKIKAEHEAALSRQQAEEAERLKQ-KAEIEAQAKGQAQEDAEKVRKEA 2141
Cdd:COG4942 102 QKEELAELLRALYRlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRAdLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072265250 2142 ELEAAKRGQAEQAALKLKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLK 2212
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1717-2122 |
1.21e-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: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1717 LKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLR 1796
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1797 ELAEEAARLRAVSEEAK-RQRQLAEEDATrqraeaerILKEKLTAINEATRMRTEAEIALKEKEAENerlrrlAEDEAYQ 1875
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEaRIRELEEDIKT--------LTQRVLERETELERMKERAKKAGAQRKEEE------AERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1876 RKLLEEQAAQHK--QDIEEKIHQLKQSSENELERQKTIVDETLK----HRRVIE-----EEIRILKINFEKASVGKSDLE 1944
Cdd:pfam07888 178 AKLQQTEEELRSlsKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttaHRKEAEneallEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1945 LELQKLKNIADETQKSKEKAE-QDAEKQRQLAlveearRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQ 2023
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARlQAAQLTLQLA------DASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2024 KDLAEKEAEKQ---IQLAQD-------AARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIY-DKLKEEAEKAKRAAEEA 2092
Cdd:pfam07888 332 ERLQEERMEREkleVELGREkdcnrvqLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYiRQLEQRLETVADAKWSE 411
|
410 420 430
....*....|....*....|....*....|
gi 1072265250 2093 ERAKIKAEHEAALSRQQAEEAERLKQKAEI 2122
Cdd:pfam07888 412 AALTSTERPDSPLSDSEDENPEALQPPRPL 441
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1731-1972 |
1.38e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1731 LEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEvEASKLRELAEEA-ARLRAVS 1809
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNE-KVKELKEERDELnEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1810 EEAKRQRQLAEEDATRQ------RAEAERILKEKLTA----------INEATRMRTEAEIALKEKEAENERLRRLAEDEA 1873
Cdd:COG1340 92 EELDELRKELAELNKAGgsidklRKEIERLEWRQQTEvlspeeekelVEKIKELEKELEKAKKALEKNEKLKELRAELKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1874 yqrklLEEQAAQHKQDIEE------KIHQLKQSSENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELEL 1947
Cdd:COG1340 172 -----LRKEAEEIHKKIKElaeeaqELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKEL 246
|
250 260
....*....|....*....|....*
gi 1072265250 1948 QKLKNIADETQKSKEKAEQDAEKQR 1972
Cdd:COG1340 247 KKLRKKQRALKREKEKEELEEKAEE 271
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2693-2731 |
1.39e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 41.93 E-value: 1.39e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1072265250 2693 YLQGKSSIAGLLLKPSNEKMSIYNAMKKKLVTPGTALIL 2731
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1168-1564 |
1.40e-04 |
|
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: 48.51 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1168 ERDVDLERYREKVQLLLERWQAIVLQIEVRQRELEQLGKQLRYYRESYEWLIRWITEAKKRQEKIQNvpitdsktvkeql 1247
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA------------- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1248 meekklleeseknrgKVDECQKYAKQYIEAIKDFEVQLVTYKAQVepvvsplkkpkvhsasdniiqeyvelrtkyseltt 1327
Cdd:TIGR02168 741 ---------------EVEQLEERIAQLSKELTELEAEIEELEERL----------------------------------- 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1328 ltsqyikfitetlrrleeeertaeklkEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEevTRREVva 1407
Cdd:TIGR02168 771 ---------------------------EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL--LNEEA-- 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1408 vdaeqqkktiqQELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQ 1487
Cdd:TIGR02168 820 -----------ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1488 KKLAQEEAERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDL--------EKFRLQAEEAERRMKQAELEK- 1558
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqerlsEEYSLTLEEAEALENKIEDDEe 968
|
....*...
gi 1072265250 1559 --ERQIKQ 1564
Cdd:TIGR02168 969 eaRRRLKR 976
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2260-2577 |
1.46e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2260 NTQQFLAEEAEKMKQVAEE-AARLSVEAQEAARLRKIAEDDlnEQRALAEKILKEKMQAVQEASrlkaeaemLQKQKEMA 2338
Cdd:COG3206 104 NLDEDPLGEEASREAAIERlRKNLTVEPVKGSNVIEISYTS--PDPELAAAVANALAEAYLEQN--------LELRREEA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2339 MEQAKKLQEDKEQMQQQLAEetegFQKTLEAERRRQLDISAEAERLKL--QVVEMSKSQAKAEEDAKKFRKQAEDISEKL 2416
Cdd:COG3206 174 RKALEFLEEQLPELRKELEE----AEAALEEFRQKNGLVDLSEEAKLLlqQLSELESQLAEARAELAEAEARLAALRAQL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2417 HQTELstkekmtvvhtlEIQRQHSDKEAEELRKAIADLENEKEKLKKEAellQKKSEEMQKAQKE------QLRQETQTL 2490
Cdd:COG3206 250 GSGPD------------ALPELLQSPVIQQLRAQLAELEAELAELSARY---TPNHPDVIALRAQiaalraQLQQEAQRI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2491 QSTFLTEKQILIQKEKYIEEEKAKLEKlfdnevgKAQKLkSEKERQLAQLEEEKRLLQTSMDDAMKKQLDAEDRIRQKQE 2570
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEA-------RLAEL-PELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVG 386
|
....*..
gi 1072265250 2571 ELQQLDK 2577
Cdd:COG3206 387 NVRVIDP 393
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2273-2482 |
1.48e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.53 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2273 KQVAEEAARLSVEAQEAARLRKIAEDDLNEQ-RALAEKILKEKMQAVQEASRLKAEAEMLQKQKEmAMEQAKKLQEDKEQ 2351
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQaEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQA-AKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2352 MQQQLAE-----ETEGFQKTLEAERRRqldisAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEK 2426
Cdd:TIGR02794 125 KAKQAAEakakaEAEAERKAKEEAAKQ-----AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1072265250 2427 MTVVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQ 2482
Cdd:TIGR02794 200 AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGA 255
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1429-1755 |
1.51e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1429 ETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQK 1508
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1509 KREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQSKRMSFLEKT 1588
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1589 TQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDA 1668
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1669 ERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQR 1748
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
....*..
gi 1072265250 1749 RRGLEEE 1755
Cdd:COG4372 364 EAGVADG 370
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2335-2603 |
1.54e-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: 48.03 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2335 KEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERR-RQLDISAEAERLKlqvvemsKSQAKAEEDAKKFRKQAEDIS 2413
Cdd:COG5185 227 EIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDlRLEKLGENAESSK-------RLNENANNLIKQFENTKEKIA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2414 EKLHQT--ELSTKEKMTVVHTLEIQRQHSDKEAE---ELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQ-----KEQL 2483
Cdd:COG5185 300 EYTKSIdiKKATESLEEQLAAAEAEQELEESKREtetGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVelsksSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2484 RQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLFDNEVGKAQKLKSEKERQLAQLEEEKRLLQTSMDDAMKKQLDAED 2563
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADE 459
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1072265250 2564 rirqkqEELQQLDKKRQEQERLLEEENRKLRERLEQLEQE 2603
Cdd:COG5185 460 ------ESQSRLEEAYDEINRSVRSKKEDLNEELTQIESR 493
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1997-2179 |
1.71e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.64 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1997 QEAGRQRKVALEEVERL-KIKADEAKKQKDLAEKEAEKQIQLAQDAARlkiDAEEKAYYAAVQQKEQEmlQTRIQEQSIY 2075
Cdd:pfam15709 355 REQEEQRRLQQEQLERAeKMREELELEQQRRFEEIRLRKQRLEEERQR---QEEEERKQRLQLQAAQE--RARQQQEEFR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2076 DKLKEEaeKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEieaqakgqaQEDAEKVRKEAELEAAKRGQAEQAA 2155
Cdd:pfam15709 430 RKLQEL--QRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAE---------EERLEYQRQKQEAEEKARLEAEERR 498
|
170 180
....*....|....*....|....
gi 1072265250 2156 LKLKQMADAEMEKHKQFAEKTVRQ 2179
Cdd:pfam15709 499 QKEEEAARLALEEAMKQAQEQARQ 522
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1459-1830 |
1.71e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.73 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1459 QLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKRE--AEDELHRKVQAEKDAAREKQKALED 1536
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAelAAEAAKKLAEAEKAAAEAEKKAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1537 LEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQ 1616
Cdd:COG3064 97 KAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1617 LEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQ 1696
Cdd:COG3064 177 GAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1697 RKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEED 1776
Cdd:COG3064 257 VGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAAS 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 1777 SRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEA 1830
Cdd:COG3064 337 LEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAG 390
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1470-1539 |
1.74e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 44.35 E-value: 1.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072265250 1470 AEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQK-----KREAEDELHR-KVQAEKDAAREKQKALEDLEK 1539
Cdd:cd06503 42 AEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKikeeiLAEAKEEAERiLEQAKAEIEQEKEKALAELRK 117
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2078-2179 |
1.86e-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: 44.78 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2078 LKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAErlKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRgqaeqaalk 2157
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEAR--AEAAEIIAEARKEAEAIAEEAKAEAEAEAERI--------- 97
|
90 100
....*....|....*....|..
gi 1072265250 2158 lKQMADAEMEKHKQFAEKTVRQ 2179
Cdd:COG0711 98 -IAQAEAEIEQERAKALAELRA 118
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2267-2402 |
1.86e-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: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2267 EEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRalaekilKEKMQAVQEASRL-------------------KAE 2327
Cdd:pfam05262 210 EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQR-------DEVRQKQQEAKNLpkpadtsspkedkqvaenqKRE 282
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 2328 AEMLQKQKEMAMEQAKKLQEDK--EQMQQQLAEETEGFQKTLEAERRRqLDISAEAERLKLQVvemsKSQAKAEEDA 2402
Cdd:pfam05262 283 IEKAQIEIKKNDEEALKAKDHKafDLKQESKASEKEAEDKELEAQKKR-EPVAEDLQKTKPQV----EAQPTSLNED 354
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1449-1907 |
1.98e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.87 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1449 VEEEIRIIRIQLETSQKQKSG----AEDELRALraraeeAERQKKLAQEEAERLRKQVKDEAQ-----KKREAEDELHRK 1519
Cdd:PRK10246 189 VFEQHKSARTELEKLQAQASGvallTPEQVQSL------TASLQVLTDEEKQLLTAQQQQQQSlnwltRLDELQQEASRR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1520 VQAEKDAAREKQKALEDLEKFRLqAEEA-------ERRMKQ-AELEKERQIKQAHDVAQQSADAELQSKRMSFLEKTTQL 1591
Cdd:PRK10246 263 QQALQQALAAEEKAQPQLAALSL-AQPArqlrphwERIQEQsAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1592 EMSLKQehiTVTHLQE-EAERLKKQQLEAetakeeaekelekWR----QKANEALRLRLQAEEIAhkktlaqeeAEKQKE 1666
Cdd:PRK10246 342 QAQQQS---LNTWLAEhDRFRQWNNELAG-------------WRaqfsQQTSDREQLRQWQQQLT---------HAEQKL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1667 DAERETRKRTKAEESA-----------LRQK--DLAEEELEKQRKLAEETASHKlSAEQELIRLKAEVDSGEQHRIVLEE 1733
Cdd:PRK10246 397 NALPAITLTLTADEVAaalaqhaeqrpLRQRlvALHGQIVPQQKRLAQLQVAIQ-NVTQEQTQRNAALNEMRQRYKEKTQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1734 DLFRLKNeVNEAIQRRRGLEEELAKVRAEMEILLKAkskaeedsrSTSE---KSKQMLEVEASKLR---------ELAEE 1801
Cdd:PRK10246 476 QLADVKT-ICEQEARIKDLEAQRAQLQAGQPCPLCG---------STSHpavEAYQALEPGVNQSRldalekevkKLGEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1802 AARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINEATRMRTEAE-IA--LKEKEAENERLRRLAedeayQRKL 1878
Cdd:PRK10246 546 GAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDdIQpwLDAQEEHERQLRLLS-----QRHE 620
|
490 500 510
....*....|....*....|....*....|..
gi 1072265250 1879 LEEQAAQHKQDI---EEKIHQLKQSSENELER 1907
Cdd:PRK10246 621 LQGQIAAHNQQIiqyQQQIEQRQQQLLTALAG 652
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
51-146 |
2.01e-04 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 43.83 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 51 KWVNKHLikhWRAEAQR-HVNDLYEDLRDGHNLISLLEVLSGETLPREKGRM------RFHKLQNVQIALDFLKLRQVkl 123
Cdd:cd21218 17 RWVNYHL---KKAGPTKkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlseedLEKRAEKVLQAAEKLGCKYF-- 91
|
90 100
....*....|....*....|...
gi 1072265250 124 vnIRNDDIADGNPKLTLGLIWTI 146
Cdd:cd21218 92 --LTPEDIVSGNPRLNLAFVATL 112
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
45-157 |
2.07e-04 |
|
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: 44.65 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 45 QKKTFTKWVNKHL-----IKHWrAEAQRHVNDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDF 115
Cdd:cd21323 25 EKVAFVNWINKALegdpdCKHV-VPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNS 103
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1072265250 116 LKLRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 157
Cdd:cd21323 104 ASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1448-1578 |
2.20e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1448 KVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDELH--------RK 1519
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkeyEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1520 VQAEKDAAREKQKALEDLEK-FRLQAEEAERRMKQAELEKErQIKQAHDVAQQSADAELQ 1578
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILeLMERIEELEEELAELEAELA-ELEAELEEKKAELDEELA 152
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1734-1894 |
2.24e-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: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1734 DLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTsEKSKQMLEveaSKLRELAEEAARLRAVSEEAK 1813
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-EKEIKRLE---LEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1814 RQRQLA-----EEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAE-----NERLRRLAEDEAyQRKLLEEQA 1883
Cdd:COG1579 87 NNKEYEalqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekkAELDEELAELEA-ELEELEAER 165
|
170
....*....|.
gi 1072265250 1884 AQHKQDIEEKI 1894
Cdd:COG1579 166 EELAAKIPPEL 176
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1732-1909 |
2.42e-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: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1732 EEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKsKAEEDSRSTSEKSKQMLEVEASKLRE--LAEEAARLRAVS 1809
Cdd:TIGR02794 67 QERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK-QAEQAAKQAEEKQKQAEEAKAKQAAEakAKAEAEAERKAK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1810 EEAKRQRQL-----AEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAA 1884
Cdd:TIGR02794 146 EEAAKQAEEeakakAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEA 225
|
170 180
....*....|....*....|....*
gi 1072265250 1885 QHKQDIEEKIHQLKQSSENELERQK 1909
Cdd:TIGR02794 226 ERKADEAELGDIFGLASGSNAEKQG 250
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2082-2346 |
2.54e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.25 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2082 AEKAKRAAEEAERAKikaeheAALSRQ------------QAEEAERLKQKAEIEAQAKGQAQEDAekvrkEAELEAAKRG 2149
Cdd:PRK05035 433 QAKAEIRAIEQEKKK------AEEAKArfearqarlereKAAREARHKKAAEARAAKDKDAVAAA-----LARVKAKKAA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2150 QAEQAALKLKQMADAEMEKHKQFAEKTVRQKEQVEGELTkvklqlEETDHQKAILDDELGRLKeevteslrQKKLVEEEL 2229
Cdd:PRK05035 502 ATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAA------AAADPKKAAVAAAIARAK--------AKKAAQQAA 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2230 FKVKIQMEELVKLKLrieqENKMLILKGKDNTQQFLAEEAEKM------KQVAEEAARLSVEAQEAARLRKI----AEDD 2299
Cdd:PRK05035 568 NAEAEEEVDPKKAAV----AAAIARAKAKKAAQQAASAEPEEQvaevdpKKAAVAAAIARAKAKKAEQQANAepeePVDP 643
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2300 LNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQK---EMAMEQAKKLQ 2346
Cdd:PRK05035 644 RKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAvaaAIARAKAKKAA 693
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1454-1539 |
2.55e-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: 44.39 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1454 RIIRIqLETSQKQKSGAEDELRALRARAEEA--ERQKKL--AQEEAERLRKQVKDEAQKKRE-----AEDELHRKV-QAE 1523
Cdd:COG0711 24 PILKA-LDERQEKIADGLAEAERAKEEAEAAlaEYEEKLaeARAEAAEIIAEARKEAEAIAEeakaeAEAEAERIIaQAE 102
|
90
....*....|....*.
gi 1072265250 1524 KDAAREKQKALEDLEK 1539
Cdd:COG0711 103 AEIEQERAKALAELRA 118
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3426-3457 |
2.60e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.60e-04
10 20 30
....*....|....*....|....*....|..
gi 1072265250 3426 KLLSAEKAVTGYKDPYSGNTISVFEALQKGLI 3457
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1328-1539 |
2.82e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.79 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1328 LTSQYIKFItetlrrleeeertaEKLKEQERKKLAEVEdqLEKQRQLAEAHaQAKAVAEKEAlelrmnmQEEVTRREVVA 1407
Cdd:COG2268 186 LDALGRRKI--------------AEIIRDARIAEAEAE--RETEIAIAQAN-REAEEAELEQ-------EREIETARIAE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1408 VDAEQQKKTIQQELHQMKNNSETEIKakvklIEEAEYNRKK-VEEEIRIIRIQLET--SQKQKSGAEDELRA-LRARAeE 1483
Cdd:COG2268 242 AEAELAKKKAEERREAETARAEAEAA-----YEIAEANAEReVQRQLEIAEREREIelQEKEAEREEAELEAdVRKPA-E 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 1484 AERQKKLAQE--EAERLRKQVKDEA---QKKREAEDELHRKVQAEK------DAAREKQKALEDLEK 1539
Cdd:COG2268 316 AEKQAAEAEAeaEAEAIRAKGLAEAegkRALAEAWNKLGDAAILLMlieklpEIAEAAAKPLEKIDK 382
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1566-1881 |
2.84e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 47.02 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1566 HDVAQQSADAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQ-EEAERLKKQQLEAETAKEEAEkelekwrQKANEALRLR 1644
Cdd:pfam03528 2 PDEDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYlAKEEDLKRQNAVLQEAQVELD-------ALQNQLALAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1645 LQAEEIAHKKTLaqeeAEKQKEDAERETRKRTKAEESALR---QKDLAEEELEKQRKLAEETA---SHKLSAEQELIRLK 1718
Cdd:pfam03528 75 AEMENIKAVATV----SENTKQEAIDEVKSQWQEEVASLQaimKETVREYEVQFHRRLEQERAqwnQYRESAEREIADLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1719 AEVDSGEQHRIV------LEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSK-------AEEDSRSTSE--- 1782
Cdd:pfam03528 151 RRLSEGQEEENLedemkkAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKelnhyleAEKSCRTDLEmyv 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1783 ----KSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINE--ATRMRTEAEIALK 1856
Cdd:pfam03528 231 avlnTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMESvlTSEQLRQVEEIKK 310
|
330 340
....*....|....*....|....*
gi 1072265250 1857 EKEAENERLRRLAEDEAYQRKLLEE 1881
Cdd:pfam03528 311 KDQEEHKRARTHKEKETLKSDREHT 335
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2768-2799 |
2.87e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.87e-04
10 20 30
....*....|....*....|....*....|..
gi 1072265250 2768 KLLSAERAITGYKDPYTGEKISLFQAMNKDLI 2799
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2124-2351 |
2.92e-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: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2124 AQAKGQAQEDAEKVRK--EAELEAAKR--GQAEQAALKLKQ---MADAEMEkhkqfAEKTVRQKEQVEGELTKVKLQLEE 2196
Cdd:COG3206 163 EQNLELRREEARKALEflEEQLPELRKelEEAEAALEEFRQkngLVDLSEE-----AKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2197 TDHQKAILDDELGRLKEEVTESLRQKKLVEEElfkvkiqmEELVKLKLRIEQENKMLilkGKDN--TQQFLAEEAEKMKQ 2274
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQLR--------AQLAELEAELAELSARY---TPNHpdVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 2275 VAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQ 2351
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2058-2174 |
2.93e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2058 QQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKV 2137
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAA 145
|
90 100 110
....*....|....*....|....*....|....*....
gi 1072265250 2138 RKEAELEaAKRGQ--AEQAALKLKQMADAEMEKhKQFAE 2174
Cdd:PRK09510 146 KAKAEAE-AKRAAaaAKKAAAEAKKKAEAEAAK-KAAAE 182
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2078-2179 |
3.00e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 43.58 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2078 LKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAErlKQKAEIEAQAKGQAQEDAEKVRKEAELEAAkrgqaeqaalK 2157
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEAR--AEAQEIIEEARKEAEKIKEEILAEAKEEAE----------R 95
|
90 100
....*....|....*....|..
gi 1072265250 2158 LKQMADAEMEKHKQFAEKTVRQ 2179
Cdd:cd06503 96 ILEQAKAEIEQEKEKALAELRK 117
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
45-158 |
3.08e-04 |
|
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: 44.28 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 45 QKKTFTKWVNKHLIKHWRAeaqRHV-------NDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIAL 113
Cdd:cd21325 25 EKYAFVNWINKALENDPDC---RHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLAL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1072265250 114 DFLKLRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVT 158
Cdd:cd21325 102 NSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1446-1750 |
3.13e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.78 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1446 RKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDELHRKVQAEKD 1525
Cdd:pfam02029 33 TESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEEN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1526 AAREKQKALEDlEKFRLQAEEAERRMKQaelEKERQIKQAHDVAQQsadaELQSKRMSFLEKTTQLEMSLKQEHITVTHL 1605
Cdd:pfam02029 113 SSWEKEEKRDS-RLGRYKEEETEIREKE---YQENKWSTEVRQAEE----EGEEEEDKSEEAEEVPTENFAKEEVKDEKI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1606 QEEAER-------LKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAhKKTLAQEEAEKQKEDAERETRKRTKA 1678
Cdd:pfam02029 185 KKEKKVkyeskvfLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQERE-EEAEVFLEAEQKLEELRRRRQEKESE 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 1679 EESALRQKDL-AEEELEKQRKLAEEtaSHKLSAEQELIRLKAEvdsgEQHRIVLEEDLFRLKNEvneaIQRRR 1750
Cdd:pfam02029 264 EFEKLRQKQQeAELELEELKKKREE--RRKLLEEEEQRRKQEE----AERKLREEEEKRRMKEE----IERRR 326
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2112-2347 |
3.20e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.79 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2112 EAERLKQKAEIeaqakgqaQEDAEKVRKEAELEAAKrgqaeQAALKLKQMADAEMEKHKQFAEKTVRQKEQvegELTKVK 2191
Cdd:COG2268 187 DALGRRKIAEI--------IRDARIAEAEAERETEI-----AIAQANREAEEAELEQEREIETARIAEAEA---ELAKKK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2192 LQLEETDHQKAILDDELGRLKEEvteslRQKKLVEEELFKVKIQMEELVKLKlRIEQEnkmlilkgkdntqqflAEEAEK 2271
Cdd:COG2268 251 AEERREAETARAEAEAAYEIAEA-----NAEREVQRQLEIAEREREIELQEK-EAERE----------------EAELEA 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072265250 2272 MKQVAEEAARLSVEAQEAARLRKIAEDDLNEqrALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQE 2347
Cdd:COG2268 309 DVRKPAEAEKQAAEAEAEAEAEAIRAKGLAE--AEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDK 382
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3389-3422 |
3.33e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.33e-04
10 20 30
....*....|....*....|....*....|....
gi 1072265250 3389 LLEAQAATGFIIDPVKNQKFYVNEAVKAGIVGPE 3422
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1437-1609 |
3.33e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 46.92 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1437 KLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAED-- 1514
Cdd:pfam05262 185 ALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKpa 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1515 ---ELHRKVQAEKDAAREKQKALEDLEKfrlQAEEAERRMKQAELEKERQIKQAHDVAQQSaDAELQSKRmsfLEKTTQL 1591
Cdd:pfam05262 265 dtsSPKEDKQVAENQKREIEKAQIEIKK---NDEEALKAKDHKAFDLKQESKASEKEAEDK-ELEAQKKR---EPVAEDL 337
|
170
....*....|....*...
gi 1072265250 1592 EMSLKQEHITVTHLQEEA 1609
Cdd:pfam05262 338 QKTKPQVEAQPTSLNEDA 355
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1112-1500 |
3.41e-04 |
|
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: 46.97 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1112 KEVQTVPGDLKELESSKADLKRmrgQVEGHQPLFNGLENDLTKAREVSERMLKVHSERDVDLERYREKVQLLLERWQAIV 1191
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEK---ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1192 LQIEVRQRELEQLGKQLRYYRESYEWLIRWITEAKKRQEKIQNVPITDSKTVKEQLMEEKKLLEESEKNRGKVDECQKYA 1271
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1272 KQYIEAIKDFEVQLVTYKAQVEpvvsplkkpkvhSASDNIIQEYVELRTKYSELTTLTSQYIKFITETLRRLEEEERTAE 1351
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIE------------SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1352 KLKEQERKKLaEVEDQLEKQRQLAEAHAQAKAVAEKEalelRMNMQEEVtrREVVAVDAEqqkktIQQELHQMKNNSETE 1431
Cdd:TIGR02168 902 ELRELESKRS-ELRRELEELREKLAQLELRLEGLEVR----IDNLQERL--SEEYSLTLE-----EAEALENKIEDDEEE 969
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072265250 1432 IKAKVKLIEeaeynrkkvEEEIRIIRIQLEtsqkqksgAEDELRALRARAEEAERQKKLAQEEAERLRK 1500
Cdd:TIGR02168 970 ARRRLKRLE---------NKIKELGPVNLA--------AIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1934-2217 |
3.42e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 46.51 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1934 EKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQlalveearrkeaeekvkkiiAAEQEAGRQRKVALEEVerl 2013
Cdd:PRK07735 45 EKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEE--------------------VTEEEKAKAKAKAAAAA--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2014 KIKADEAKKQKDLAEKEAEKQiqlAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQsiydklkEEAEKAKRAAEEAE 2093
Cdd:PRK07735 102 KAKAAALAKQKREGTEEVTEE---EKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEE-------EETDKEKAKAKAAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2094 RAKIKAeheAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAK----RGQAEQAALKLKQMADAemekh 2169
Cdd:PRK07735 172 AAKAKA---AALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKasqgNGDSGDEDAKAKAIAAA----- 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1072265250 2170 KQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTE 2217
Cdd:PRK07735 244 KAKAAAAARAKTKGAEGKKEEEPKQEEPSVNQPYLNKYVEVIKEKLGE 291
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2058-2423 |
3.47e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2058 QQKEQEMLQTRIQEQSIYDKLKEEAEKAKRAAE----EAERAKIKAEHEAALSRQQAEEAErlKQKAEIEAQAKGQAQED 2133
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWErqrrELESRVAELKEELRQSREKHEELE--EKYKELSASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2134 AEKVRKEAELEAAKRGQAEQAALKLKQMAD--AEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRL 2211
Cdd:pfam07888 118 DALLAQRAAHEARIRELEEDIKTLTQRVLEreTELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2212 KeevtESLRQKKLVEEELFKVKIQMEELVKLKLRIEQENKMLiLKGKDNTQQFLAeeaekMKQVAEEAARLSVEAQEAAR 2291
Cdd:pfam07888 198 R----NSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL-LEELRSLQERLN-----ASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2292 LRKIAEddLNEQRALAEKI---LKEKMQAVQEA-SRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKtL 2367
Cdd:pfam07888 268 DRTQAE--LHQARLQAAQLtlqLADASLALREGrARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREK-L 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 2368 EAERRRQLDIS-AEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELST 2423
Cdd:pfam07888 345 EVELGREKDCNrVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3349-3386 |
3.50e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 3.50e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1072265250 3349 RQYLQGSECIAGVLLEENKQKMNIYQAMKRNLLRPGTA 3386
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1857-2184 |
3.59e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.78 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1857 EKEAENERLRRLAEDEAYQRKlLEEQAAQHKQDIEEKIH-------QLKQSSENELERQKTIVDETLKhrrviEEEIRIL 1929
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKE-EEEPSGQVTESVEPNEHnsyeedsELKPSGQGGLDEEEAFLDRTAK-----REERRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1930 KInfEKASVGKSDLELELQKLKNIADETQKSKEKAE-QDAEKQRQLALVEEARRKEAEEKVKKII-----------AAEQ 1997
Cdd:pfam02029 78 RL--QEALERQKEFDPTIADEKESVAERKENNEEEEnSSWEKEEKRDSRLGRYKEEETEIREKEYqenkwstevrqAEEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1998 EAGRQRKVALEEVERLKIKADE----AKKQKDLAEKEAEKQIqlaqdaarlkIDAEEKAYYAAVQQKEQEMLQTRIQEQS 2073
Cdd:pfam02029 156 GEEEEDKSEEAEEVPTENFAKEevkdEKIKKEKKVKYESKVF----------LDQKRGHPEVKSQNGEEEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2074 IYDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQK---AEIEAQAKGQAQEDAEKVRKEAEleaakrgq 2150
Cdd:pfam02029 226 RQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKqqeAELELEELKKKREERRKLLEEEE-------- 297
|
330 340 350
....*....|....*....|....*....|....
gi 1072265250 2151 aeqaalklKQMADAEMEKHKQFAEKTVRQKEQVE 2184
Cdd:pfam02029 298 --------QRRKQEEAERKLREEEEKRRMKEEIE 323
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1646-2063 |
3.66e-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: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1646 QAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGE 1725
Cdd:COG3064 9 AAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1726 QHRIVLEEDLfRLKNEVNEAIQRRRgleeelAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARL 1805
Cdd:COG3064 89 AEKKAAAEKA-KAAKEAEAAAAAEK------AAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1806 RAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQ 1885
Cdd:COG3064 162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1886 HKQDIEEKIHQLKQSSENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAE 1965
Cdd:COG3064 242 EAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1966 QDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQLAQDAARLK 2045
Cdd:COG3064 322 AAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLL 401
|
410
....*....|....*...
gi 1072265250 2046 IDAEEKAYYAAVQQKEQE 2063
Cdd:COG3064 402 GLRLDLGAALLEAASAVE 419
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1765-1973 |
3.72e-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: 46.30 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1765 ILLKAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLTAINEA 1844
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1845 TRMRTEAEIALKEKEAE-NERLR------------------------RLAEDEAYQRKLLEEQAAQHKQDIEEkIHQLKQ 1899
Cdd:COG4942 89 EKEIAELRAELEAQKEElAELLRalyrlgrqpplalllspedfldavRRLQYLKYLAPARREQAEELRADLAE-LAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 1900 SSENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQ 1973
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1433-1563 |
3.81e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1433 KAKVKLIEEAEynrkKVEEEIRiiriQLETSQKQksgAEDELRALRARAEEAERQKKLAQEEAERLRKQvkdEAQKKREA 1512
Cdd:PRK00409 506 EAKKLIGEDKE----KLNELIA----SLEELERE---LEQKAEEAEALLKEAEKLKEELEEKKEKLQEE---EDKLLEEA 571
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 1513 EDELHRKVQAEKDAAREKQKALEDLEKFRL------QAEEAERRMKQAELEKERQIK 1563
Cdd:PRK00409 572 EKEAQQAIKEAKKEADEIIKELRQLQKGGYasvkahELIEARKRLNKANEKKEKKKK 628
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2392-2611 |
4.05e-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: 46.30 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2392 SKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKK 2471
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2472 SEEMQKAQKEQLRQETQTLQSTFLTE-----------------KQILIQKEKYIEEEKAKLEKLFDNEVgKAQKLKSEKE 2534
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRA-ELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 2535 RQLAQLEEEKRLLQTSMDDAMKKQLDAEDRIRQKQEELQQLDKKRqeqerlleeenRKLRERLEQLEQEHRIALEKT 2611
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-----------EELEALIARLEAEAAAAAERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2296-2559 |
4.20e-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: 46.30 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2296 AEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQL 2375
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2376 DISAEAERLKLQVVEMSKSqakAEEDAKKFRKQAEDISEKLHQTELstkekmtvvhtLEIQRQHSDKEAEELRKAIADle 2455
Cdd:COG4942 98 ELEAQKEELAELLRALYRL---GRQPPLALLLSPEDFLDAVRRLQY-----------LKYLAPARREQAEELRADLAE-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2456 nekeklkkeaELLQKKSEEMQKAQKEQLRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLFDNEVGKAQKLKSEKER 2535
Cdd:COG4942 162 ----------LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250 260
....*....|....*....|....
gi 1072265250 2536 QLAQLEEEKRLLQTSMDDAMKKQL 2559
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALKGKL 255
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3759-3795 |
4.26e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.26e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1072265250 3759 RLLSAERAVTGYRDPYTEQMISIFQAMKKDLIPSDQA 3795
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2092-2418 |
4.28e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2092 AERAKIKAEHEAALSRQQAEEAERLkqkAEIEAQAKGQAQEDAEKVRKEAELEAAKrgQAEQAALKLKQMADAEMEKHKQ 2171
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQL---AEEQYRLVEMARELEELSARESDLEQDY--QAASDHLNLVQTALRQQEKIER 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2172 F----AEKTVRQKEQVEgeltkvklQLEETDHQKAILDDELGRLKEEVtESLR------QKKLveEELFKVKIQMEELVK 2241
Cdd:COG3096 352 YqedlEELTERLEEQEE--------VVEEAAEQLAEAEARLEAAEEEV-DSLKsqladyQQAL--DVQQTRAIQYQQAVQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2242 LKLRIE---QENKMLILKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEddlneqraLAEKILKE--KMQ 2316
Cdd:COG3096 421 ALEKARalcGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE--------LVCKIAGEveRSQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2317 AVQEASRLKAEAEMLQKQKEMAMEQAKKLQE--DKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKS 2394
Cdd:COG3096 493 AWQTARELLRRYRSQQALAQRLQQLRAQLAEleQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQ 572
|
330 340
....*....|....*....|....
gi 1072265250 2395 QAKAEEDAKKFRKQAEDISEKLHQ 2418
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLRARIKE 596
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
45-157 |
4.46e-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: 43.46 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 45 QKKTFTKWVNKHLIKHWRAeaqRHV-------NDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIAL 113
Cdd:cd21324 25 EKYAFVNWINKALENDPDC---KHVipmnpntDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLAL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1072265250 114 DFLKLRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 157
Cdd:cd21324 102 NSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
2070-2157 |
4.83e-04 |
|
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: 42.42 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2070 QEQSIYDKLKEEAEKAKR--AAEEAERAKIKAEHEAALSRQQAEEAERLK-QKAEIEAQAKGQAQEDAEKVRKEAEleaA 2146
Cdd:pfam16999 13 REAALDQQIEAARKEAERevEAAEAEAARILREAEAKAKALQAEYRQELAaETARIREEARARAEAEAQAVRTRAE---G 89
|
90
....*....|.
gi 1072265250 2147 KRGQAEQAALK 2157
Cdd:pfam16999 90 RLQQAVELILR 100
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1607-1931 |
4.94e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.68 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1607 EEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQK 1686
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1687 DLAEEELEKQRKLAEEtashKLSAEQELIRLKAEVDS-GEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVRAEMEI 1765
Cdd:pfam13868 109 RIQEEDQAEAEEKLEK----QRQLREEIDEFNEEQAEwKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKER 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1766 LLKAKSKAEEDSRstsEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLtainEAT 1845
Cdd:pfam13868 185 EIARLRAQQEKAQ---DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAE----EAE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1846 RMRTEAEIALKEKEAENERLRRLAEDeayQRKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKTIvDETLKHRRVIEEE 1925
Cdd:pfam13868 258 REEEEFERMLRKQAEDEEIEQEEAEK---RRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL-REEEAERRERIEE 333
|
....*.
gi 1072265250 1926 IRILKI 1931
Cdd:pfam13868 334 ERQKKL 339
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1949-2164 |
5.01e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1949 KLKNIADETQKSKEKAEQDA-----EKQRQLALVEEARRKEAEEKvKKIIAAEQEAGRQRKVALEEVErlKIKADEAKKQ 2023
Cdd:PRK05035 472 RHKKAAEARAAKDKDAVAAAlarvkAKKAAATQPIVIKAGARPDN-SAVIAAREARKAQARARQAEKQ--AAAAADPKKA 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2024 K---DLAEKEAEKQIQLAQDAARLKIDAEEKAYYAA----VQQKEQEMLQTriQEQSIYDKLKEEAEKAKRAAEEAeRAK 2096
Cdd:PRK05035 549 AvaaAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAaiarAKAKKAAQQAA--SAEPEEQVAEVDPKKAAVAAAIA-RAK 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2097 I-KAEHEAALSRQQAEEAERLKQKAEIE-AQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQMADA 2164
Cdd:PRK05035 626 AkKAEQQANAEPEEPVDPRKAAVAAAIArAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1634-1925 |
5.28e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.01 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1634 RQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKA---EESAL----------RQKDLaEEELEKQRKLA 1700
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGgldEEEAFldrtakreerRQKRL-QEALERQKEFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1701 EETASHKLSaeqelIRLKAEVDSGEQHRIVLEEdlfrlknevnEAIQRRRGLEEELAKVRAEMEILLKAKSKAEED--SR 1778
Cdd:pfam02029 91 PTIADEKES-----VAERKENNEEEENSSWEKE----------EKRDSRLGRYKEEETEIREKEYQENKWSTEVRQaeEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1779 STSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAE-----AERILKEKLTAINEATRMRTEAEI 1853
Cdd:pfam02029 156 GEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEvksqnGEEEVTKLKVTTKRRQGGLSQSQE 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 1854 ALKEKEAENERLRRLaEDEAYQRKLLEEQAAqhkqdieEKIHQLKQSSENELERQKTIVDEtlkHRRVIEEE 1925
Cdd:pfam02029 236 REEEAEVFLEAEQKL-EELRRRRQEKESEEF-------EKLRQKQQEAELELEELKKKREE---RRKLLEEE 296
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1669-2438 |
5.30e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.35 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1669 ERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRivlEEDLFRLKNEVNEAIQR 1748
Cdd:pfam10174 44 ERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVD---GEDKFSTPELTEENFRR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1749 RRGLEEELAKvraemEILLKAKSKAEEDSRSTSEKskQMLEVEASKLRELAEeaarlrAVSEEAKRQRQLAEEDATRQRa 1828
Cdd:pfam10174 121 LQSEHERQAK-----ELFLLRKTLEEMELRIETQK--QTLGARDESIKKLLE------MLQSKGLPKKSGEEDWERTRR- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1829 eaerilkekltaINEATRMRTEAEIALKEKEAENERLRrlaedEAYQRKLlEEQAAQHKQDIEEKIHQLKQSSENELERQ 1908
Cdd:pfam10174 187 ------------IAEAEMQLGHLEVLLDQKEKENIHLR-----EELHRRN-QLQPDPAKTKALQTVIEMKDTKISSLERN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1909 KtivdetlkhrRVIEEEIRILKINfekASVGKSDLELELQKLKNIADETQKSKEKAEQ-DAEKQRQ----LAL-VEEARR 1982
Cdd:pfam10174 249 I----------RDLEDEVQMLKTN---GLLHTEDREEEIKQMEVYKSHSKFMKNKIDQlKQELSKKeselLALqTKLETL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1983 KEAEEKVKKIIAAEQE---AGRQRKVALE-EVERLKIKADE-----AKKQKDLAEKEAEKQiQLAQDAARLKIDAEEKAY 2053
Cdd:pfam10174 316 TNQNSDCKQHIEVLKEsltAKEQRAAILQtEVDALRLRLEEkesflNKKTKQLQDLTEEKS-TLAGEIRDLKDMLDVKER 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2054 YAAVQQKEQEMLQTRIQeqsiyDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEE---AERLKQKAEIEAQAKGQA 2130
Cdd:pfam10174 395 KINVLQKKIENLQEQLR-----DKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKeriIERLKEQREREDRERLEE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2131 QEDAEKVRKEAE--LEAAKRGQAEQ--AALKLKQMADAEmekhKQFAEKTVRQKEQVEGELTKVKLQLE--ETDHQKAIL 2204
Cdd:pfam10174 470 LESLKKENKDLKekVSALQPELTEKesSLIDLKEHASSL----ASSGLKKDSKLKSLEIAVEQKKEECSklENQLKKAHN 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2205 DDELGRLKEEVTESLRqkkLVEEElfkVKIQMEElvKLKLRIEQENKMLILKGKDNtqqflaEEAEKMKQVAEEAARLSV 2284
Cdd:pfam10174 546 AEEAVRTNPEINDRIR---LLEQE---VARYKEE--SGKAQAEVERLLGILREVEN------EKNDKDKKIAELESLTLR 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2285 EAQE----AARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMlqkqkeMAMEQAK-KLQEDKEQMQ--QQLA 2357
Cdd:pfam10174 612 QMKEqnkkVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELM------GALEKTRqELDATKARLSstQQSL 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2358 EETEGFQKTLEAERRRQLD--ISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISeklhqteLSTKEKMTVVHTLEI 2435
Cdd:pfam10174 686 AEKDGHLTNLRAERRKQLEeiLEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVM-------ALKREKDRLVHQLKQ 758
|
...
gi 1072265250 2436 QRQ 2438
Cdd:pfam10174 759 QTQ 761
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1940-2233 |
5.64e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 45.80 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1940 KSDLELELQKLKNIADETQKSKEKAEQD-AEKQRQLALVEEARRKEaeekvkkiiaAEQEAgRQRKVALEEVERLKIKAD 2018
Cdd:pfam15558 19 EEQRMRELQQQAALAWEELRRRDQKRQEtLERERRLLLQQSQEQWQ----------AEKEQ-RKARLGREERRRADRREK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2019 EAKKQKDLAEKEAEKQIQLAQDAARLKI-DAEEKAYYAAVQQKEQEMLQTRIQEQSIYDKLK--EEAEKAKRAAEEAERA 2095
Cdd:pfam15558 88 QVIEKESRWREQAEDQENQRQEKLERARqEAEQRKQCQEQRLKEKEEELQALREQNSLQLQErlEEACHKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2096 KIKAEHEAALSRQQA--------EEAERLKQKAEIEA-----------QAKGQAQEDAEKVRKEAE------LEAAKRGQ 2150
Cdd:pfam15558 168 KVQENNLSELLNHQArkvlvdcqAKAEELLRRLSLEQslqrsqenyeqLVEERHRELREKAQKEEEqfqrakWRAEEKEE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2151 AEQAALK-LKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRlkEEVTESLRQKKLVEEEL 2229
Cdd:pfam15558 248 ERQEHKEaLAELADRKIQQARQVAHKTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHR--EGIKEAIKKKEQRSEQI 325
|
....
gi 1072265250 2230 FKVK 2233
Cdd:pfam15558 326 SREK 329
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1379-1763 |
5.81e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 46.05 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1379 AQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQQKKTIQQELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRI 1458
Cdd:pfam15964 284 AQHEAVLAQTHTNVHMQTIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKS 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1459 QLEtsqKQKSGAEDELRA-LRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDELHRkVQAEKDAA------REKQ 1531
Cdd:pfam15964 364 ELE---RQKERLEKELASqQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEK-VTREKNSLvsqleeAQKQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1532 KALEDLEKFRLQAEE----AERRMKQAELEKE-RQIKQAHDVAQQSADAELQSKRMSFLEKTTQLEMS------LKQEHI 1600
Cdd:pfam15964 440 LASQEMDVTKVCGEMryqlNQTKMKKDEAEKEhREYRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAqqdaarAREECL 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1601 TVTHLQEEAERlkkqQLEAETAKEEAEKelekwRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERET-------- 1672
Cdd:pfam15964 520 KLTELLGESEH----QLHLTRLEKESIQ-----QSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQyslltsqn 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1673 --------------------RKRTKAEESALRQ-KDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVL 1731
Cdd:pfam15964 591 tfiaklkeecctlakkleeiTQKSRSEVEQLSQeKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLDKHCQAT 670
|
410 420 430
....*....|....*....|....*....|..
gi 1072265250 1732 EEDLFRLKNEVNEAIQRRRGLEEELAKVRAEM 1763
Cdd:pfam15964 671 AQQLVQLLSKQNQLFKERQNLTEEVQSLRSQV 702
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
68-147 |
5.95e-04 |
|
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: 42.51 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 68 HVNDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDFLKLRQVKLVNIRNDDIADGNPKLTLGL 142
Cdd:cd21293 29 STNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNSAKAIGCSVVNIGTQDLAEGRPHLVLGL 108
|
....*
gi 1072265250 143 IWTII 147
Cdd:cd21293 109 ISQII 113
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1100-1548 |
6.09e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1100 AEEVVKTYEDQLKEVQTVPGDLKELESSKADLKRMR----GQVEGHQPLFNGLENDLTKARE-----------VSERMLK 1164
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETEREReelaEEVRDLRERLEELEEERDDLLAeaglddadaeaVEARREE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1165 VHSERDV-----------------DLERYREKVQLLLER--------------WQAIVLQIEVRQRELEQLGKQLRYYRE 1213
Cdd:PRK02224 319 LEDRDEElrdrleecrvaaqahneEAESLREDADDLEERaeelreeaaeleseLEEAREAVEDRREEIEELEEEIEELRE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1214 SYEWLIRWITEAKKRQEKIQNVPITDSKTVKEQLMEEKKLLEESEKNR-----GKVDECQKYAKQ--YIEAIKDFEVQLV 1286
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleaGKCPECGQPVEGspHVETIEEDRERVE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1287 TYKAQVEPVVSPlkkpkvHSASDNIIQEYVELRTKYSELTTLTSQyikfitetlrrleeeERTAEKLKEQERKKLAEVED 1366
Cdd:PRK02224 479 ELEAELEDLEEE------VEEVEERLERAEDLVEAEDRIERLEER---------------REDLEELIAERRETIEEKRE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1367 QLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEvtrREVVAvDAEQQKKTIQQELHQMKNNSE--TEIKAKVKLIEEAEY 1444
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAAAEAEEEAEEA---REEVA-ELNSKLAELKERIESLERIRTllAAIADAEDEIERLRE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1445 NRKKVEEEIRIIRIQLETSQKQKSGAEDELRAlrARAEEAeRQKKlaqEEAERLRKQVKDEAQKKREAEDELHRKVQA-- 1522
Cdd:PRK02224 614 KREALAELNDERRERLAEKRERKRELEAEFDE--ARIEEA-REDK---ERAEEYLEQVEEKLDELREERDDLQAEIGAve 687
|
490 500 510
....*....|....*....|....*....|....
gi 1072265250 1523 ----EKDAAREKQKALED----LEKFRLQAEEAE 1548
Cdd:PRK02224 688 neleELEELRERREALENrveaLEALYDEAEELE 721
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1369-1915 |
6.13e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.33 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1369 EKQRQLAEAHAQAKAVAEKEALELRMNMQEE---VTRREVVAVDAeQQKKTIQQELHQMKNNSETEIkAKVKL------- 1438
Cdd:PRK10246 215 PEQVQSLTASLQVLTDEEKQLLTAQQQQQQSlnwLTRLDELQQEA-SRRQQALQQALAAEEKAQPQL-AALSLaqparql 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1439 ------IEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDElrALRARAEEAERQKKLAQ--EEAERLR----------- 1499
Cdd:PRK10246 293 rphwerIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHH--AAKQSAELQAQQQSLNTwlAEHDRFRqwnnelagwra 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1500 ---KQVKDEAQKKREAE--DELHRKVQA-----------EKDAAREKQKALEDLEKfRLQAEEAERRMKQAELEKERQIK 1563
Cdd:PRK10246 371 qfsQQTSDREQLRQWQQqlTHAEQKLNAlpaitltltadEVAAALAQHAEQRPLRQ-RLVALHGQIVPQQKRLAQLQVAI 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1564 QAHDVAQQSADAELQSKRMSFLEKTTQLE--MSLKQEHITVTHLQEEAERLKKQQ--LEAETAKEEAEKELEKWRQKANE 1639
Cdd:PRK10246 450 QNVTQEQTQRNAALNEMRQRYKEKTQQLAdvKTICEQEARIKDLEAQRAQLQAGQpcPLCGSTSHPAVEAYQALEPGVNQ 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1640 ALRLRLQAEeiahKKTLAQEEAE-KQKEDAERETRKRTKAEESALRQKdlaEEELEKQRKLAEETASHKLSAEQELIRLK 1718
Cdd:PRK10246 530 SRLDALEKE----VKKLGEEGAAlRGQLDALTKQLQRDESEAQSLRQE---EQALTQQWQAVCASLNITLQPQDDIQPWL 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1719 AEVDSGEQHRIVLEEDLFrLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKS------KAEEDSRSTSEKSKQMLEVEA 1792
Cdd:PRK10246 603 DAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLATRQQEAQSWQQRQ 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1793 SKLRELAEEAARLRAVSEeakrqrQLAEEDATRqrAEAERILKEKLTAINEATrMRTEAEIALKEKEAENERLR------ 1866
Cdd:PRK10246 682 NELTALQNRIQQLTPLLE------TLPQSDDLP--HSEETVALDNWRQVHEQC-LSLHSQLQTLQQQDVLEAQRlqkaqa 752
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1072265250 1867 ---------RLAEDEAYQRKLLEEQAAQhkqdieeKIHQLKQSSENELERQKTIVDET 1915
Cdd:PRK10246 753 qfdtalqasVFDDQQAFLAALLDEETLT-------QLEQLKQNLENQRQQAQTLVTQT 803
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2067-2237 |
6.27e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 45.76 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2067 TRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQ-AQEDAEKVRKEAElea 2145
Cdd:pfam05262 175 DSISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADfAQDNADKQRDEVR--- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2146 akrgQAEQAALKLKQMADAE--------MEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEvtE 2217
Cdd:pfam05262 252 ----QKQQEAKNLPKPADTSspkedkqvAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKEL--E 325
|
170 180
....*....|....*....|
gi 1072265250 2218 SLRQKKLVEEELFKVKIQME 2237
Cdd:pfam05262 326 AQKKREPVAEDLQKTKPQVE 345
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1480-2102 |
6.37e-04 |
|
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: 45.79 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1480 RAEEAERqKKLAQEEAERLRKQVkdeAQKKREAEDELHRKVQAEKDAAREKqKALEDLEKFRLQAEEAERRMKQ-AELEK 1558
Cdd:pfam05701 30 RIQTVER-RKLVELELEKVQEEI---PEYKKQSEAAEAAKAQVLEELESTK-RLIEELKLNLERAQTEEAQAKQdSELAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1559 ERQIKQAHDVAQQS---ADAELQSKRMSFLEKTTQLEmSLKQEhitVTHLQEEAERLKKQQleaetakeeaekelEKWRQ 1635
Cdd:pfam05701 105 LRVEEMEQGIADEAsvaAKAQLEVAKARHAAAVAELK-SVKEE---LESLRKEYASLVSER--------------DIAIK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1636 KANEAlrlrlqaeeiahkkTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEelekQR---KLAEETASHKLS--- 1709
Cdd:pfam05701 167 RAEEA--------------VSASKEIEKTVEELTIELIATKESLESAHAAHLEAEE----HRigaALAREQDKLNWEkel 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1710 --AEQELIRLKAEVDSGEQhrivleedlfrLKNEVNEAIQRRRGLEEELAkvrAEMEILLKAKSKAEEDSRSTSEKSKQM 1787
Cdd:pfam05701 229 kqAEEELQRLNQQLLSAKD-----------LKSKLETASALLLDLKAELA---AYMESKLKEEADGEGNEKKTSTSIQAA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1788 LeveASKLRELAEEAARLRAVSEEAKRQRQLaeedATRQRAEAERiLKEKLTAINEATRMrteAEIALKEKEAENERLRr 1867
Cdd:pfam05701 295 L---ASAKKELEEVKANIEKAKDEVNCLRVA----AASLRSELEK-EKAELASLRQREGM---ASIAVSSLEAELNRTK- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1868 lAEDEAYQRKllEEQAAQHKQDIEEKIHQLKQssenELERQKTIVdetlkhrRVIEEEIRILKINFEKASVGKSDLELEL 1947
Cdd:pfam05701 363 -SEIALVQAK--EKEAREKMVELPKQLQQAAQ----EAEEAKSLA-------QAAREELRKAKEEAEQAKAAASTVESRL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1948 QKLKNiadETQKSKEKAEqdaekqrqLALVEEARRKEAEEKVKkiiaAEQEAGRQRKVAL--EEVERLKIKADEAKKQKD 2025
Cdd:pfam05701 429 EAVLK---EIEAAKASEK--------LALAAIKALQESESSAE----STNQEDSPRGVTLslEEYYELSKRAHEAEELAN 493
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072265250 2026 LAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTriqeqsiydklkEEAEKAK--RAAEEAERAKIKAEHE 2102
Cdd:pfam05701 494 KRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIAL------------EKAEKAKegKLAAEQELRKWRAEHE 560
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2243-2577 |
6.48e-04 |
|
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: 46.19 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2243 KLRIEQENKMlilKGKDNTQQFLAEEAEKMKQVAEEAArlSVEAQEAARlRKIAEDDLNEQRALAEKiLKEKMQAVQEAS 2322
Cdd:TIGR00606 193 QVRQTQGQKV---QEHQMELKYLKQYKEKACEIRDQIT--SKEAQLESS-REIVKSYENELDPLKNR-LKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2323 RLKAEAEMLQKQKEMAMEQAKKLQEDKEQM----QQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKA 2398
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2399 EEDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEIQRQ-HSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQK 2477
Cdd:TIGR00606 346 LVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2478 AQKEQLRQETQTLQSTFLTEKQILIQKE---KYIEEEKAKLEKLFDNEVGKAQKL-KSEKERQLAQLEEEKRLLQTSMDD 2553
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEILEKKQeelKFVIKELQQLEGSSDRILELDQELrKAERELSKAEKNSLTETLKKEVKS 505
|
330 340
....*....|....*....|....
gi 1072265250 2554 AMKKQLDAEDRIRQKQEELQQLDK 2577
Cdd:TIGR00606 506 LQNEKADLDRKLRKLDQEMEQLNH 529
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
1475-1581 |
6.52e-04 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 45.61 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1475 RALRARAEEAERQKKLAQE-EAERLRKqvKDEAQKKREAEDELHRKVQAEKDAAREKQKAledlekfRLQAEEAERRMKQ 1553
Cdd:PRK00247 321 RAPELHAENAEIKKTRTAEkNEAKARK--KEIAQKRRAAEREINREARQERAAAMARARA-------RRAAVKAKKKGLI 391
|
90 100 110
....*....|....*....|....*....|..
gi 1072265250 1554 AELEKERQIKQAHD----VAQQSADAELQSKR 1581
Cdd:PRK00247 392 DASPNEDTPSENEEskgsPPQVEATTTAEPNR 423
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1990-2125 |
6.66e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1990 KKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKE-AEKQIQLAQDAARLKIDAEEKAYYAAvqQKEQEMLQTR 2068
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEiEEVEARIKKYEEQLGNVRNNKEYEAL--QKEIESLKRR 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 2069 IQ-----EQSIYDKLKE-----EAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQ 2125
Cdd:COG1579 105 ISdledeILELMERIEEleeelAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1738-2038 |
7.13e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1738 LKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSrstsEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQ 1817
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1818 LAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQL 1897
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1898 KQSSENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLALV 1977
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072265250 1978 EEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDLAEKEAEKQIQLA 2038
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1369-1575 |
7.26e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1369 EKQRQLAEAHAQAKAVAEKEAlelrmNMQEEVTRrevvavdAEQQKKTIQQELhqmkNNSETEIKAKVKLIEEAE----Y 1444
Cdd:COG3883 20 AKQKELSELQAELEAAQAELD-----ALQAELEE-------LNEEYNELQAEL----EALQAEIDKLQAEIAEAEaeieE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1445 NRKKVEEEIRIIRIQ----------------------LETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQV 1502
Cdd:COG3883 84 RREELGERARALYRSggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 1503 KDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADA 1575
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1479-1844 |
7.98e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 45.41 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1479 ARAEEAERQKKLAQEEAERLrkqvkdEAQKKREAEdelhRKVQAEkdaaREKQKALEDLEKFRLQAEEAERRMKQAELEK 1558
Cdd:pfam15558 15 ARHKEEQRMRELQQQAALAW------EELRRRDQK----RQETLE----RERRLLLQQSQEQWQAEKEQRKARLGREERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1559 ERQIKQAHDVAQQSADAEL----QSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQleaetakeeaekelekwr 1634
Cdd:pfam15558 81 RADRREKQVIEKESRWREQaedqENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQ------------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1635 qkanEALRLRLQAEEIAHKKTLAQEEAEKQKedaeRETRKRTKAEESALRQkdlaeeELEKQRKlaEETASHKLSAEQEL 1714
Cdd:pfam15558 143 ----NSLQLQERLEEACHKRQLKEREEQKKV----QENNLSELLNHQARKV------LVDCQAK--AEELLRRLSLEQSL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1715 IRlkaevdSGEQHRIVLEEDLFRLKNEV---NEAIQRRRGLEEELAKVRAE-MEILLKAKSKAEEDSRSTSEKSKQ---M 1787
Cdd:pfam15558 207 QR------SQENYEQLVEERHRELREKAqkeEEQFQRAKWRAEEKEEERQEhKEALAELADRKIQQARQVAHKTVQdkaQ 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 1788 LEVEASKLRELAEEAARLRAVSEEAKRQRQLaEEDATRQRAEAERILKEKLTAINEA 1844
Cdd:pfam15558 281 RARELNLEREKNHHILKLKVEKEEKCHREGI-KEAIKKKEQRSEQISREKEATLEEA 336
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1380-2204 |
8.12e-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: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1380 QAKAVAEKEALELRMNMQE-EVTRREVvavDAEQQKKTIQQELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRi 1458
Cdd:pfam07111 11 LVQSPGHQDVLERRLDTQRpTVTMWEQ---DVSGDGQGPGRRGRSLELEGSQALSQQAELISRQLQELRRLEEEVRLLR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1459 qlETSQKQKSGAEDELRALRARAeeaeRQKKLAQEEAERLRKQVkdeaqkkreAEDELHRKVQAEKdaareKQKALEDLE 1538
Cdd:pfam07111 87 --ETSLQQKMRLEAQAMELDALA----VAEKAGQAEAEGLRAAL---------AGAEMVRKNLEEG-----SQRELEEIQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1539 kfrlqaeeaerRMKQAELEkerQIKQAHDVAQQSadaeLQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQle 1618
Cdd:pfam07111 147 -----------RLHQEQLS---SLTQAHEEALSS----LTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQL-- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1619 aetakeeaekelekwrQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETrkrtkaeesalrqkdlaEEELEKQRK 1698
Cdd:pfam07111 207 ----------------SKTQEELEAQVTLVESLRKYVGEQVPPEVHSQTWELER-----------------QELLDTMQH 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1699 LAEETAShkLSAEQELIRLKAEvdsGEQHRIVLEEDlfrlknEVNEAIQRRRGLEEELAK-----VRAEME----ILLKA 1769
Cdd:pfam07111 254 LQEDRAD--LQATVELLQVRVQ---SLTHMLALQEE------ELTRKIQPSDSLEPEFPKkcrslLNRWREkvfaLMVQL 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1770 KSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAkrqrqlAEEDATRQRAEAeriLKEKLTAINEATRmRT 1849
Cdd:pfam07111 323 KAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKA------AEVEVERMSAKG---LQMELSRAQEARR-RQ 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1850 EAEIALKEkeaenERLRRLAEDEAYQRKLLEEQAAQHKQDIEeKIHQLKQSSENELERQKTIvdETLKHRRVIEEEIRIL 1929
Cdd:pfam07111 393 QQQTASAE-----EQLKFVVNAMSSTQIWLETTMTRVEQAVA-RIPSLSNRLSYAVRKVHTI--KGLMARKVALAQLRQE 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1930 KINF-EKASVGKSDLELELQKLKniadetqksKEKAEQDAEKQRQLALVeearrkeaeekvkkiiaaEQEAGRQRKvale 2008
Cdd:pfam07111 465 SCPPpPPAPPVDADLSLELEQLR---------EERNRLDAELQLSAHLI------------------QQEVGRARE---- 513
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2009 everlkikadeakkqkdlaEKEAEKQiQLAQDAarlkidaeekayyaavQQKEQEMLQTRIQEQSIYDKLKEEAEKAKRA 2088
Cdd:pfam07111 514 -------------------QGEAERQ-QLSEVA----------------QQLEQELQRAQESLASVGQQLEVARQGQQES 557
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2089 AEEAerAKIKAEheaaLSRQQAEEAERLKQK-AEIEAQAKGQAQeDAEKVRKEAELEAAKrgqaeqAALKLKQMADAEME 2167
Cdd:pfam07111 558 TEEA--ASLRQE----LTQQQEIYGQALQEKvAEVETRLREQLS-DTKRRLNEARREQAK------AVVSLRQIQHRATQ 624
|
810 820 830
....*....|....*....|....*....|....*..
gi 1072265250 2168 KHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAIL 2204
Cdd:pfam07111 625 EKERNQELRRLQDEARKEEGQRLARRVQELERDKNLM 661
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1463-1571 |
8.14e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1463 SQKQKSGAEDELRALRARAE-EAERQKKL----AQEEAERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDL 1537
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKkEAEAIKKEalleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108
|
90 100 110
....*....|....*....|....*....|....*
gi 1072265250 1538 EKfRLQAEEAERRMKQAELE-KERQIKQAHDVAQQ 1571
Cdd:PRK12704 109 EE-ELEKKEKELEQKQQELEkKEEELEELIEEQLQ 142
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1741-1877 |
8.17e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.25 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1741 EVNEAIQRRRGLEEELAKVRAEmeillKAKSKAEEDSRSTSEKSKQmlEVEASKLRELAEEAARLRAVSEEAKRQRQLAE 1820
Cdd:COG2268 224 EEAELEQEREIETARIAEAEAE-----LAKKKAEERREAETARAEA--EAAYEIAEANAEREVQRQLEIAEREREIELQE 296
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 1821 EDATRQRAEAERILKEKLTAinEATRMRTEAeialkEKEAENERLRRLAEDEAYQRK 1877
Cdd:COG2268 297 KEAEREEAELEADVRKPAEA--EKQAAEAEA-----EAEAEAIRAKGLAEAEGKRAL 346
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1659-2019 |
8.26e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1659 EEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRL 1738
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1739 KNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQ- 1817
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEe 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1818 ---LAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKI 1894
Cdd:COG4372 166 laaLEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1895 HQLKQSSENELERQKTIVDETLKHRRVIEEEIRILKINFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQL 1974
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1072265250 1975 ALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKADE 2019
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2119-2404 |
8.26e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2119 KAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAAlklkqmadaemeKHKQFAEKTVRQKEQ-VEGELTKVKLQLEET 2197
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREA------------RHKKAAEARAAKDKDaVAAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2198 DHQKAILDDELGRLKEEVTEslrqkklveeelfkvkiqmEELVKLKLRIEQENKMlilkgkdntqqflAEEAEKMKQVAE 2277
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAA-------------------REARKAQARARQAEKQ-------------AAAAADPKKAAV 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2278 EAARLSVEAQEAARLRKIAE-----DDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQM 2352
Cdd:PRK05035 551 AAAIARAKAKKAAQQAANAEaeeevDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAE 630
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 2353 QQQLAEETEGfqktlEAERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKK 2404
Cdd:PRK05035 631 QQANAEPEEP-----VDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKK 677
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2300-2418 |
8.65e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.88 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2300 LNEQRALAEKIL---KEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLd 2376
Cdd:cd16269 176 LQSKEAEAEAILqadQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLL- 254
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1072265250 2377 isAEAERLKLqvvemSKSQAKAEEDAKKFRKQAEDISEKLHQ 2418
Cdd:cd16269 255 --KEQERALE-----SKLKEQEALLEEGFKEQAELLQEEIRS 289
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1470-1705 |
8.71e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1470 AEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDELhrkvqaekdaaREKQKALEDLEKfrlQAEEAER 1549
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-----------EALQAEIDKLQA---EIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1550 RMKQAeleKERQIKQAHDVAQQSADAE-----LQSKRMS-FLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAK 1623
Cdd:COG3883 80 EIEER---REELGERARALYRSGGSVSyldvlLGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1624 EEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEET 1703
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
..
gi 1072265250 1704 AS 1705
Cdd:COG3883 237 AA 238
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2477-2618 |
8.82e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2477 KAQKEQLRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLfdnevgKAQKLKSEKERQLAQLEEEKRLLQTSMDDAMK 2556
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY------EEQLGNVRNNKEYEALQKEIESLKRRISDLED 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 2557 KQLDAEDRIRQKQEELQQLDKKRQEQERLLEEENRKLRERLEQLEQEhRIALEKTREVIITK 2618
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE-LEELEAEREELAAK 171
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1464-1561 |
9.07e-04 |
|
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: 42.72 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1464 QKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEdelHRKVQAEKDAAREKQKALEDLEKFRLQ 1543
Cdd:pfam05672 26 QREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEE---ERQRKAEEEAEEREQREQEEQERLQKQ 102
|
90
....*....|....*...
gi 1072265250 1544 AEEAERRMkQAELEKERQ 1561
Cdd:pfam05672 103 KEEAEAKA-REEAERQRQ 119
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1418-1775 |
9.32e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1418 QQELHQMKNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAER 1497
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1498 LRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAEL 1577
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1578 QSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLA 1657
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1658 QEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFR 1737
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
330 340 350
....*....|....*....|....*....|....*...
gi 1072265250 1738 LKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKSKAEE 1775
Cdd:COG4372 332 LAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2262-2441 |
9.47e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.47 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2262 QQFLAEEAEKMKQVAEEAARLSVEAQEAAR---LRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMA 2338
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAkelLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2339 MEQAKKLqedkEQMQQQLAEETEgfqktleaERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEdiseklHQ 2418
Cdd:PRK12705 108 EEREKAL----SARELELEELEK--------QLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIE------EE 169
|
170 180
....*....|....*....|...
gi 1072265250 2419 TELSTKEKMTVVHTLEIQRQHSD 2441
Cdd:PRK12705 170 ADLEAERKAQNILAQAMQRIASE 192
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2222-2567 |
9.93e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2222 KKLVEEELFKVKIQMEELVKLKLRIEQENKMLILKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARlrKIAEddlN 2301
Cdd:COG5185 227 EIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKE--KIAE---Y 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2302 EQRALAEKilkekmqAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAERRrqldisaea 2381
Cdd:COG5185 302 TKSIDIKK-------ATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIEN--------- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2382 erlklqvVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKM-TVVHTLEIQRQHSDKEAEELRKAIADLENEKEK 2460
Cdd:COG5185 366 -------IVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAqEILATLEDTLKAADRQIEELQRQIEQATSSNEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2461 LKKEAELLQK-KSEEMQKAQKEQLRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLFDNEvgkaQKLKSEKERQLAQ 2539
Cdd:COG5185 439 VSKLLNELISeLNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATL----EKLRAKLERQLEG 514
|
330 340
....*....|....*....|....*...
gi 1072265250 2540 LEEEKRLLQTSMDDAMKKQLDAEDRIRQ 2567
Cdd:COG5185 515 VRSKLDQVAESLKDFMRARGYAHILALE 542
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
1806-2229 |
1.00e-03 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 45.24 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1806 RAVSEEAKRQRQLAEEDATRQRAEAERILkekltainEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQ 1885
Cdd:pfam09730 9 KVAADGESREESLLQESASKEAYYAQRIL--------ELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1886 HKQDIEE----KIHQLKQSSENELE-----------RQKTIVDETLKHR-RVIEEEIRILKINFEKASVGKSDLELELQK 1949
Cdd:pfam09730 81 MRDEIKEykvrEARLLQDYSELEEEnislqkqvsvlKQNQVEFEGLKHEiTRKEEETELLNSQLEEAIRLREIAERQLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1950 lkniADETQksKEKAEQDAEKQRQLALVEEARRKEAEEKVKKII-----AAEQEAGRQRKVALEEVERLKIKADEAKKQK 2024
Cdd:pfam09730 161 ----ALETL--KTEREQKNSLRKELSHYMTLNDFDYVSHLSISLdglkfSEDEGAGTEPNNDGEAMDGGENGGGGLKNSG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2025 DLAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTRIQEQSIYDKLKE---EAEKAKRA-AEEAERAKIKAE 2100
Cdd:pfam09730 235 LDNRTSTPRKSEVFPPAPSLVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQEsqkQLEQAKGAlSEQQEKVNRLTE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2101 HEAALSRQQAEEaerlKQKAEIEAQAKGQAQEDA---EKVRKEAELEAAKRGQAEQAALKLKQMADAEMEKHKQFAEKTV 2177
Cdd:pfam09730 315 NLEAMRGLQASK----ERQDALDSEKDRDSHEDGdyyEVDINGPEILECKYRVAVEEAGELREELKALKARYNTLEERYK 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1072265250 2178 RQKEQVEGE---LTKVKLQLEETDHQ----KAILDDELGRLKEEVTESLRQKKLVEEEL 2229
Cdd:pfam09730 391 EEKTRWEAEaqdLAEKIRQLEKASHQdqerIAHLEKELGKTRKVAGESEGSLSVAQDEL 449
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2731-2764 |
1.02e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.02e-03
10 20 30
....*....|....*....|....*....|....
gi 1072265250 2731 LLEAQAASGFITDPVGNKRLTVSEAVKENVIGPE 2764
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
2284-2608 |
1.09e-03 |
|
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: 45.32 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2284 VEAQEAARLRKIAEDDLNEQRAlaeKILKEKMQAVQEASRLKAEAEMLQKQKEMAME------QAKKLQEDKEQMQQQLA 2357
Cdd:pfam15818 10 LEALEELRMRREAETQYEEQIG---KIIVETQELKWQKETLQNQKETLAKQHKEAMAvfkkqlQMKMCALEEEKGKYQLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2358 EET-----EGFQKTLEAerrrqLDISAEAerLKLQVVEMSKS---QAKAEEDakkFRKQAEDIsEKLHQTELStkeKMTV 2429
Cdd:pfam15818 87 TEIkekeiEGLKETLKA-----LQVSKYS--LQKKVSEMEQKlqlHLLAKED---HHKQLNEI-EKYYATITG---QFGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2430 VHTLEIQRQHSDKEAEELRKAIAdlenekeklkkeaeLLQKKSEEMQKAQKEQLRQETQTLQSTFLT------EKQI-LI 2502
Cdd:pfam15818 153 VKENHGKLEQNVQEAIQLNKRLS--------------ALNKKQESEICSLKKELKKVTSDLIKSKVTcqykmgEENInLT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2503 QKEKYIEEEKAKLEklFDNEVGKaqKLKSEkerqLAQLEEEKRLLQTS---MDDAMKKQLDAEDRIrqkQEELQQLDKKR 2579
Cdd:pfam15818 219 IKEQKFQELQERLN--MELELNK--KINEE----ITHIQEEKQDIIISfqhMQQLLQQQTQANTEM---EAELKALKENN 287
|
330 340 350
....*....|....*....|....*....|..
gi 1072265250 2580 QEQERLLEEENRKLRERLEQ---LEQEHRIAL 2608
Cdd:pfam15818 288 QTLERDNELQREKVKENEEKflnLQNEHEKAL 319
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
45-147 |
1.09e-03 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 42.27 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 45 QKKTFTKWVNKHLIKHwraEAQRHV-------NDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIAL 113
Cdd:cd21292 25 EKVAFVNWINKNLGDD---PDCKHLlpmdpntDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLAL 101
|
90 100 110
....*....|....*....|....*....|....
gi 1072265250 114 DFLKLRQVKLVNIRNDDIADGNPKLTLGLIWTII 147
Cdd:cd21292 102 NSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1663-1893 |
1.10e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.60 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1663 KQKEDAERETRKRTKAEESALRQKDLAEE-----ELEKQRKLAEETASHklsAEQELIRLKAEVDSGEQHRIVLEEDLFR 1737
Cdd:NF012221 1541 SQQADAVSKHAKQDDAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEESRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1738 LKNEVNEAIQRRRGLEEElAKVRAEM---------EILLKAKSKAEEDSRSTS----EKSKQMLEVEASKLRELAEEAAR 1804
Cdd:NF012221 1618 VTKELTTLAQGLDALDSQ-ATYAGESgdqwrnpfaGGLLDRVQEQLDDAKKISgkqlADAKQRHVDNQQKVKDAVAKSEA 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1805 LRAVSEEAKRQRQLAEEDAtrqRAEAERILKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQrklLEEQAA 1884
Cdd:NF012221 1697 GVAQGEQNQANAEQDIDDA---KADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQ---AQADAK 1770
|
....*....
gi 1072265250 1885 QHKQDIEEK 1893
Cdd:NF012221 1771 GAKQDESDK 1779
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2076-2208 |
1.20e-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: 41.86 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2076 DKLKEEAEKAKRAAEEAERAKIKAEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAEleaakrgQAEQAA 2155
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQALREELN-------ELKAEI 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 2156 LKLKQMADAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDEL 2208
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQL 126
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1351-1552 |
1.24e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.59 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1351 EKLKEQERKKLAEVEDQLEKQRQLAEAHA-QAKAVAEKEALELRMNMQEEVT-----RREVVAVDAEQQKKTIQQELHQM 1424
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEEARKRLVAKHGAeISKLEEENREKEKALPKNDDMTieeakRRAAAAAKAKAAALAKQKREGTE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1425 KNNSETEIKAKVKLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRAlRARAEEAERQKKLAQEEAERLRKQVKD 1504
Cdd:PRK07735 84 EVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAA-KAKAAALAKQKREGTEEVTEEEEETDK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1072265250 1505 EAQKKREAedelhrKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMK 1552
Cdd:PRK07735 163 EKAKAKAA------AAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAK 204
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2307-2612 |
1.24e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2307 AEKILKEKMQ-AVQEASRLKAEAEMLQKQKEMAMEQAKKL----QEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEA 2381
Cdd:pfam02029 4 EEEAARERRRrAREERRRQKEEEEPSGQVTESVEPNEHNSyeedSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2382 ERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTE---LSTKEKMTVVHTLEIQRQHSdKEAEELRKAIADLENEK 2458
Cdd:pfam02029 84 ERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDsrlGRYKEEETEIREKEYQENKW-STEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2459 EKLKKEAELLQKKSEEMQKAQKEQLRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLFDNEVGKAQKLKSEKERQLA 2538
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEV 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072265250 2539 QLEEEKRLLQTSMDDAMKKQLDAEdRIRQKQEE----LQQLDKKRQEQERLLEEENRKLRErlEQLEQEHRIALEKTR 2612
Cdd:pfam02029 243 FLEAEQKLEELRRRRQEKESEEFE-KLRQKQQEaeleLEELKKKREERRKLLEEEEQRRKQ--EEAERKLREEEEKRR 317
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4278-4309 |
1.36e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 39.23 E-value: 1.36e-03
10 20 30
....*....|....*....|....*....|..
gi 1072265250 4278 IAGIVDTDTLEKVSITEAMHRNLVDNITGQRL 4309
Cdd:pfam00681 8 TGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1414-1574 |
1.58e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1414 KKTIQQELHQMKNNSETEIKAKVKlieEAEYNRKKVEEEIRiiriqlETSQKQKSGAEDELRalRARAEEAERQKKLAQE 1493
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKK---EAEAIKKEALLEAK------EEIHKLRNEFEKELR--ERRNELQKLEKRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1494 EaERLRKqvKDEAQKKREAEdelhrkVQAEKDAAREKQKALEDLEKF----------------RLQAEEAERRM-----K 1552
Cdd:PRK12704 95 E-ENLDR--KLELLEKREEE------LEKKEKELEQKQQELEKKEEEleelieeqlqelerisGLTAEEAKEILlekveE 165
|
170 180
....*....|....*....|..
gi 1072265250 1553 QAELEKERQIKQAHDVAQQSAD 1574
Cdd:PRK12704 166 EARHEAAVLIKEIEEEAKEEAD 187
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1440-1551 |
1.60e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 41.44 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1440 EEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDELHRK 1519
Cdd:pfam20492 9 QELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEA 88
|
90 100 110
....*....|....*....|....*....|..
gi 1072265250 1520 VQAEKDAAREKQKALEDLEKFRLQAEEAERRM 1551
Cdd:pfam20492 89 QEEIARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
103-147 |
1.61e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 41.66 E-value: 1.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1072265250 103 FHKLQNVQIALDFLKLRQVKLVNIRNDDIADGNPKLTLGLIWTII 147
Cdd:cd21294 78 FQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2261-2404 |
1.69e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2261 TQQFLAEEAEKMKQVAEEAARLSVEAQEAarlrkiaeDDLNEQRALAEKILKEkmqavQEASRLKAeaemlQKQKEMAME 2340
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQA--------EELQQKQAAEQERLKQ-----LEKERLAA-----QEQKKQAEE 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 2341 QAKKLQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKlQVVEMSKSQAKAEEDAKK 2404
Cdd:PRK09510 123 AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEA-KKKAEAEAAKKAAAEAKK 185
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1448-1593 |
1.69e-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: 43.13 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1448 KVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKRE--AEDELHRKVQAEKD 1525
Cdd:pfam04012 19 KAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEelAREALAEKKSLEKQ 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072265250 1526 AAREKQ---KALEDLEKFRLQAEEAERRMKQAELEK------ERQIKQAHDVAQQSADAELQSKRMSFLE-KTTQLEM 1593
Cdd:pfam04012 99 AEALETqlaQQRSAVEQLRKQLAALETKIQQLKAKKnllkarLKAAKAQEAVQTSLGSLSTSSATDSFERiEEKIEER 176
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1739-1873 |
1.70e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.62 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1739 KNEVNEAIQRRRGLEEElAKVRAEMEILlKAKSKAEEdSRstseksKQMLEVEASKLRELAEEAARLRAVSE-EAKRQRQ 1817
Cdd:PTZ00491 662 KSQEAAARHQAELLEQE-ARGRLERQKM-HDKAKAEE-QR------TKLLELQAESAAVESSGQSRAEALAEaEARLIEA 732
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1072265250 1818 LAEEDATRQRAEAERILKEkltAINEATRMRTEAEIALKEKEAENE--RLRRLAEDEA 1873
Cdd:PTZ00491 733 EAEVEQAELRAKALRIEAE---AELEKLRKRQELELEYEQAQNELEiaKAKELADIEA 787
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1635-1863 |
1.75e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.20 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1635 QKANEALRLRLQAEEIAHKKTLAQEEAEKQK----------EDAERETRKRTKAEESALRQK------DLAEEELEKQRK 1698
Cdd:PRK07735 16 RRAKEEARKRLVAKHGAEISKLEEENREKEKalpknddmtiEEAKRRAAAAAKAKAAALAKQkregteEVTEEEKAKAKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1699 LAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRG-----------LEEELAKVRAEMEILL 1767
Cdd:PRK07735 96 KAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREgteevteeeeeTDKEKAKAKAAAAAKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1768 KAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSeEAKRQRQLAEEDATRQRAEAERILKEKLTAiNEATRM 1847
Cdd:PRK07735 176 KAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAA-LAKQKASQGNGDSGDEDAKAKAIAAAKAKA-AAAARA 253
|
250
....*....|....*.
gi 1072265250 1848 RTEAEIALKEKEAENE 1863
Cdd:PRK07735 254 KTKGAEGKKEEEPKQE 269
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1736-1930 |
1.79e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1736 FRLKNEVNEAIQRRRGLEEELAKVRAEMEILLKAKS--KAEEDSRSTSEKSKQMLEveasKLRELAEEAARLRAVSEEAK 1813
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQ----QLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1814 RQRQLAEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKE--AENERLRRLAEDEAYQRKLLEEQAAQHKQDIE 1891
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytPNHPDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190
....*....|....*....|....*....|....*....
gi 1072265250 1892 EKIHQLkQSSENELERQKTIVDETLKHRRVIEEEIRILK 1930
Cdd:COG3206 320 AELEAL-QAREASLQAQLAQLEARLAELPELEAELRRLE 357
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1739-1885 |
1.80e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.09 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1739 KNEVNEAIQRRRgleeeLAKVRAEMEIllkAKSKAEEDSRSTSEkskqmlevEASKLRELAE-EAARLRAVSEEAKRQRQ 1817
Cdd:COG2268 182 ENNYLDALGRRK-----IAEIIRDARI---AEAEAERETEIAIA--------QANREAEEAElEQEREIETARIAEAEAE 245
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072265250 1818 LAEEDA-TRQRAEAERILKEKLTAINEATRMRT---EAEIALKEKE---AENERLRRLAEDEAYQRKLLEEQAAQ 1885
Cdd:COG2268 246 LAKKKAeERREAETARAEAEAAYEIAEANAEREvqrQLEIAEREREielQEKEAEREEAELEADVRKPAEAEKQA 320
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1475-1714 |
1.81e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1475 RALRARAEEAERQKKLAQEEAERLRKQVkDEAQKKREA--EDELHRKVQAEKDAAREKQKALED-LEKFRLQAEEAERRM 1551
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL-EEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1552 KQAELEKERQIKQAHDVAQQSADAELQSKRMSFLEKTTQLEMSLKQEHITVTHLQEEAERLKkqqleaetakeeaekele 1631
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR------------------ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1632 kwRQKANEALRLRLQAEeiahkktlAQEEAEKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAE 1711
Cdd:COG3206 305 --AQLQQEAQRILASLE--------AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL 374
|
...
gi 1072265250 1712 QEL 1714
Cdd:COG3206 375 EEA 377
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1856-2058 |
1.84e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.07 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1856 KEKEAENERLRRLAEDEA----YQRKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKTIVDEtlKHRRVIEEEirilki 1931
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAkkeqERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAE--QAAKQAEEK------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1932 nfEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEKQRQLALVEEARRKEAEEKVKKIIAAEQEAGRQRKVALEEve 2011
Cdd:TIGR02794 118 --QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEE-- 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1072265250 2012 rLKIKADEAKKQkdlAEKEAEKQIQLAQdAARLKIDAEEKAYYAAVQ 2058
Cdd:TIGR02794 194 -AKAKAEAAKAK---AAAEAAAKAEAEA-AAAAAAEAERKADEAELG 235
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
2077-2148 |
1.93e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 43.82 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2077 KLKEEAEKAKRAAEEAE----RAKIKAEHEAALSR----QQAEEAERLKQKAEIEAQ---AKGQAQEDAEKVRKEAELEA 2145
Cdd:cd03406 177 KLLIAEQHQKVVEKEAEterkRAVIEAEKDAEVAKiqmqQKIMEKEAEKKISEIEDEmhlAREKARADAEYYRALREAEA 256
|
...
gi 1072265250 2146 AKR 2148
Cdd:cd03406 257 NKL 259
|
|
| PRK09174 |
PRK09174 |
F0F1 ATP synthase subunit B; |
2037-2110 |
1.96e-03 |
|
F0F1 ATP synthase subunit B;
Pssm-ID: 169692 [Multi-domain] Cd Length: 204 Bit Score: 42.86 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2037 LAQD---AARLKIDAEekayyAAVQQKEQEMLQTRIQEQSI----YDKLKEEAEKAKRAAEEAERAKIK-AEHEAALSRQ 2108
Cdd:PRK09174 89 IAQDldqAARLKQEAD-----AAVAAYEQELAQARAKAHSIaqaaREAAKAKAEAERAAIEASLEKKLKeAEARIAAIKA 163
|
..
gi 1072265250 2109 QA 2110
Cdd:PRK09174 164 KA 165
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2094-2316 |
1.99e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2094 RAKIK-AEHEAALSRQQAE-EAERLKQkaEIEAQAKgqaqEDAEKVRKEAELEAAKRgqaeqaalklkqmadaemEKHKQ 2171
Cdd:PRK12704 30 EAKIKeAEEEAKRILEEAKkEAEAIKK--EALLEAK----EEIHKLRNEFEKELRER------------------RNELQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2172 FAEKTVRQKEQvegeltKVKLQLEETDHQKAILDDELGRLKEEvteslrqkklvEEELFKVKIQMEELVKlklriEQENK 2251
Cdd:PRK12704 86 KLEKRLLQKEE------NLDRKLELLEKREEELEKKEKELEQK-----------QQELEKKEEELEELIE-----EQLQE 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 2252 MLILKGkdntqqFLAEEAEKM--KQVAEEAarlsvEAQEAARLRKIAEDDLNEQRALAEKILKEKMQ 2316
Cdd:PRK12704 144 LERISG------LTAEEAKEIllEKVEEEA-----RHEAAVLIKEIEEEAKEEADKKAKEILAQAIQ 199
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1510-1807 |
2.08e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1510 REAEDELHRKVQAEKDAAREKQKAleDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQSKRMSFLEKTT 1589
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARF--EARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIK 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1590 QLEMSLKQEHITvthlQEEAERLKKQQLEAETAKEEAEKElekwRQKANEALRLRLQAeeiahKKTLAQEEAEKQKEDAE 1669
Cdd:PRK05035 510 AGARPDNSAVIA----AREARKAQARARQAEKQAAAAADP----KKAAVAAAIARAKA-----KKAAQQAANAEAEEEVD 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1670 RETRKRTKAEESALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEvdsgeqhrivleedlfrlKNEVNEAIQRR 1749
Cdd:PRK05035 577 PKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAK------------------KAEQQANAEPE 638
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1072265250 1750 RGLEEELAKVRAEMEillKAKSKAEEDSRSTSEKskqmLEVEASKLRELAEEAARLRA 1807
Cdd:PRK05035 639 EPVDPRKAAVAAAIA---RAKARKAAQQQANAEP----EEAEDPKKAAVAAAIARAKA 689
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1847-2151 |
2.09e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.20 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1847 MRTEAEIALKEKEAEnERLRRLAEDEAYQRklLEEQAAQHKQDIEEKIHQLKQSSENELERQKtivdetlkhRRVIEEEi 1926
Cdd:PRK07735 1 MDPEKDLEDLKKEAA-RRAKEEARKRLVAK--HGAEISKLEEENREKEKALPKNDDMTIEEAK---------RRAAAAA- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1927 rilkinfeKASVGksdlELELQKLKNIADETQKSKEKAEQDAEKQRQLALVEEARRKEAEEKVkkiiAAEQEAGRQRKVA 2006
Cdd:PRK07735 68 --------KAKAA----ALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEE----VTEEEKAAAKAKA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2007 LEEVerlKIKADEAKKQKDLAEKEAEKQIQLAQDA-ARLKIDAEEKAYYAAVQQKEQemlqtriQEQSIYDKLKEEAEKA 2085
Cdd:PRK07735 132 AAAA---KAKAAALAKQKREGTEEVTEEEEETDKEkAKAKAAAAAKAKAAALAKQKA-------AEAGEGTEEVTEEEKA 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 2086 KRAAEEAERAKIKAeheAALSRQQAEEA------ERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQA 2151
Cdd:PRK07735 202 KAKAKAAAAAKAKA---AALAKQKASQGngdsgdEDAKAKAIAAAKAKAAAAARAKTKGAEGKKEEEPKQEE 270
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
46-116 |
2.25e-03 |
|
first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409070 Cd Length: 106 Bit Score: 40.72 E-value: 2.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072265250 46 KKTFTKWVNKHLIKhwraeaQR-HVNDLYEDLRDGHNLISLLEVLSGETLPREK----GRMRFHKLQNVQIALDFL 116
Cdd:cd21221 3 VRVLTEWINEELAD------DRiVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1366-1538 |
2.31e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.24 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1366 DQLEKQRQLA--------EAHAQAKAVA-EKEA---LElRMNMQEEVtrrevvavDAEQQKKTIqqeLHQMKNNSETEIK 1433
Cdd:PTZ00491 647 DSLQKSVQLAieittksqEAAARHQAELlEQEArgrLE-RQKMHDKA--------KAEEQRTKL---LELQAESAAVESS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1434 AKVKLIEEAEYNRKKVEEEiriiriqletsqkqksgAEDELRALRARAEEAERQKKLAQEeaerlrkqvkdeaQKKREAE 1513
Cdd:PTZ00491 715 GQSRAEALAEAEARLIEAE-----------------AEVEQAELRAKALRIEAEAELEKL-------------RKRQELE 764
|
170 180
....*....|....*....|....*
gi 1072265250 1514 DElHRKVQAEkdAAREKQKALEDLE 1538
Cdd:PTZ00491 765 LE-YEQAQNE--LEIAKAKELADIE 786
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
2269-2404 |
2.38e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 44.09 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2269 AEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAvqEASRLKAEAEMLQKQKEMA---MEQAK-K 2344
Cdd:PRK12472 182 AEALAAAPARAETLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKL--ERAKARADAELKRADKALAaakTDEAKaR 259
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2345 LQEDKEQMQQQLAEETEgfqktleaerrrQLDISAEAERLKLQVVEMSKSQAKAEEDAKK 2404
Cdd:PRK12472 260 AEERQQKAAQQAAEAAT------------QLDTAKADAEAKRAAAAATKEAAKAAAAKKA 307
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4002-4033 |
2.55e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.55e-03
10 20 30
....*....|....*....|....*....|..
gi 1072265250 4002 KLLSAERAVTGYKDPYSGKIISLFQAMKKGLI 4033
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2019-2127 |
2.58e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 43.43 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2019 EAKKQKDLAEKEAEKQIQlaqdAARLKIDAEEKAyyAAVQQKEQEMLQTRIQEQsiyDKLKEEAEKAKRAAEEAERAKIK 2098
Cdd:pfam02841 190 EAILQTDQALTAKEKAIE----AERAKAEAAEAE--QELLREKQKEEEQMMEAQ---ERSYQEHVKQLIEKMEAEREQLL 260
|
90 100
....*....|....*....|....*....
gi 1072265250 2099 AEHEAALSRQQAEEAERLKQKAEIEAQAK 2127
Cdd:pfam02841 261 AEQERMLEHKLQEQEELLKEGFKTEAESL 289
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1350-1552 |
2.63e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.52 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1350 AEKLKEQERKKLAEVE---DQLEKQRQLAEAHaQAKAVAEKEALELRMNMQEEVTRREVVAV-DAEQQKKTIQQELHQMK 1425
Cdd:pfam19220 53 LEALLAQERAAYGKLRrelAGLTRRLSAAEGE-LEELVARLAKLEAALREAEAAKEELRIELrDKTAQAEALERQLAAET 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1426 NNSETEIKAKVKLIEEAEYNRKKVEEEIRiiriQLETSQKQKSGAEDELRALRARAEE-AERQKKLAQEEAErLRKQVKD 1504
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKALQRAEG----ELATARERLALLEQENRRLQALSEEqAAELAELTRRLAE-LETQLDA 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1072265250 1505 EAQKKREAEDELhrkvqAEKDAAREKQKALEDLEKFRLQAEEAERRMK 1552
Cdd:pfam19220 207 TRARLRALEGQL-----AAEQAERERAEAQLEEAVEAHRAERASLRMK 249
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1841-1970 |
2.66e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1841 INEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQSSENELERQKTIVDETLKH-R 1919
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEaK 583
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 1920 RVIEEEIRILK--INFEKASVGKSDLELELQKLKNIADETQKSKEKAEQDAEK 1970
Cdd:PRK00409 584 KEADEIIKELRqlQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1470-1580 |
2.70e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 41.86 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1470 AEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDElhrkvQAEKDAAREKQKALEDLEKfrlqaeEAER 1549
Cdd:PRK07352 62 AEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAEIEK-----QAIEDMARLKQTAAADLSA------EQER 130
|
90 100 110
....*....|....*....|....*....|..
gi 1072265250 1550 RMKQAELEKERQ-IKQAHDVAQQSADAELQSK 1580
Cdd:PRK07352 131 VIAQLRREAAELaIAKAESQLPGRLDEDAQQR 162
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1349-1686 |
2.74e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1349 TAEKLKEQERKKLAEVEDQLEKQRQLAEAHAQAK-AVAEKealelRMNMQEEvtrrevVAVDAEQQKKTiqqelhqmknn 1427
Cdd:pfam02029 64 FLDRTAKREERRQKRLQEALERQKEFDPTIADEKeSVAER-----KENNEEE------ENSSWEKEEKR----------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1428 seteikakvklieEAEYNRKKVEeeiriiriqlETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKdeaq 1507
Cdd:pfam02029 122 -------------DSRLGRYKEE----------ETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENF---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1508 KKREAEDELHRKVQAEKdaarEKQKALEDLEKFRlqaeeAERRMKQAELEKERqikqaHDVAQQSADAELQSKRMSFLEK 1587
Cdd:pfam02029 175 AKEEVKDEKIKKEKKVK----YESKVFLDQKRGH-----PEVKSQNGEEEVTK-----LKVTTKRRQGGLSQSQEREEEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1588 TTQLEMSLKQEHITVTHLQ---EEAERLKKQQLeAETAKEEAEKELEKWRQKANEALRLRLQAEEiAHKKTLAQEEAEKQ 1664
Cdd:pfam02029 241 EVFLEAEQKLEELRRRRQEkesEEFEKLRQKQQ-EAELELEELKKKREERRKLLEEEEQRRKQEE-AERKLREEEEKRRM 318
|
330 340
....*....|....*....|..
gi 1072265250 1665 KEDAEREtrkrtKAEESALRQK 1686
Cdd:pfam02029 319 KEEIERR-----RAEAAEKRQK 335
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2194-2625 |
2.75e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.74 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2194 LEETDHQKAILDDELGRLKEEVTESLRQKKLVE--EELFKVKIQ-MEELVKLKLRIEQENKMLIL---KGKDNTQQFLAE 2267
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQQARLDelEALIDQWLAeLEQVIALRRAGGLEAALALVrsgEGKALMDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2268 EAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQE 2347
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2348 DKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKM 2427
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2428 TVVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQLRQET---QTLQSTFLTEKQILIQK 2504
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAeveAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2505 EKYIEEEKAKLEKLFDNEVGKAQKLKSEKERQLAQLEEEKRLLQTSMDDAMKKQLDAEDRIRQKQEELQQLDKKRQEQER 2584
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1072265250 2585 LLEEENRKLRERLEQLEQEHRIALEKTREVIITKETVITQT 2625
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALA 518
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1861-2097 |
2.93e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.71 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1861 ENERLRRLAEDEAYQRKlleeQAAQHKQDIEEKIHQ-LKQSSENELERQKtivdetlkhrrvieeEIRILKINFEKASVG 1939
Cdd:COG2268 187 DALGRRKIAEIIRDARI----AEAEAERETEIAIAQaNREAEEAELEQER---------------EIETARIAEAEAELA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1940 KSDLELELqklkniadETQKSKEKAEQDAEKQRQLALveearrkeaeekvKKIIAAEQEAGRQRKVALEEVERLKIKADE 2019
Cdd:COG2268 248 KKKAEERR--------EAETARAEAEAAYEIAEANAE-------------REVQRQLEIAEREREIELQEKEAEREEAEL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2020 AKKQKDLAEKEAEKQIQLAQ---DAARLKIDAEEKAyYAAVQQKEQEMLQTRIQEQsIYDKLKEEAEKAKRAAEEAERAK 2096
Cdd:COG2268 307 EADVRKPAEAEKQAAEAEAEaeaEAIRAKGLAEAEG-KRALAEAWNKLGDAAILLM-LIEKLPEIAEAAAKPLEKIDKIT 384
|
.
gi 1072265250 2097 I 2097
Cdd:COG2268 385 I 385
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1062-1571 |
3.03e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1062 LRSELDVTLHKMEQVHSMSSIYLDKLKTINLVIRNTHGAEEVVKTYEDQLKEVQTVPGDLKELESSKADLKRMRGQVEGH 1141
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1142 QPLFNGLEndltkaREVSERMLKvhserdvDLERYREKVQLLLErwqaivlQIEVRQRELEQLGKQLRyyresyewliRW 1221
Cdd:PRK03918 378 KKRLTGLT------PEKLEKELE-------ELEKAKEEIEEEIS-------KITARIGELKKEIKELK----------KA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1222 ITEAKKRQEK--IQNVPITDSKtvKEQLMEEKKLLEESEKNRGKVDECQ----KYAKQYIEAIKDFEVQLVTYKAQVEPV 1295
Cdd:PRK03918 428 IEELKKAKGKcpVCGRELTEEH--RKELLEEYTAELKRIEKELKEIEEKerklRKELRELEKVLKKESELIKLKELAEQL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1296 VSPLKKPKVHSASdniiqeyvELRTKYSELTTLTSQYIKFitetLRRLEEEERTAEKLKEQErKKLAEVEDQL-EKQRQL 1374
Cdd:PRK03918 506 KELEEKLKKYNLE--------ELEKKAEEYEKLKEKLIKL----KGEIKSLKKELEKLEELK-KKLAELEKKLdELEEEL 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1375 AEAHAQAKAVAEK--EALELRMNMQEEVTRREVVAVDAEQQKKTIQQELHQMKNNseteikakvklIEEAEYNRKKVEEE 1452
Cdd:PRK03918 573 AELLKELEELGFEsvEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEE-----------LDKAFEELAETEKR 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1453 IRIIRIQLEtsQKQKSGAEDELRALRARAEEAERqkklaqeEAERLRKQVKdEAQKKREAEDELHRKVQAEKDAAREKQK 1532
Cdd:PRK03918 642 LEELRKELE--ELEKKYSEEEYEELREEYLELSR-------ELAGLRAELE-ELEKRREEIKKTLEKLKEELEEREKAKK 711
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1072265250 1533 ALEDLEKFRLQAEEAERRMKQAE-LEKERQIKQAHDVAQQ 1571
Cdd:PRK03918 712 ELEKLEKALERVEELREKVKKYKaLLKERALSKVGEIASE 751
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1351-1550 |
3.12e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.78 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1351 EKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQQKKTIQQELHQMKNNSET 1430
Cdd:PRK05035 465 EKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAAD 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1431 EIKAKV-----------------KLIEEAEYNRKKVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQE 1493
Cdd:PRK05035 545 PKKAAVaaaiarakakkaaqqaaNAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARA 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 1494 EAerlRKQVKDEAQKKREAEDELHRKVQAEkdAAREKQKALEDLEKFRLQAEEAERR 1550
Cdd:PRK05035 625 KA---KKAEQQANAEPEEPVDPRKAAVAAA--IARAKARKAAQQQANAEPEEAEDPK 676
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
522-615 |
3.36e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 522 LRYFQDLLAWVEENQKRINTAEWGSDLPSVESQLGSHRGLHQSINEFRAKIERARTDEGQI----PGSRGAYQDYLGKLD 597
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieegHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1072265250 598 LQYAKLLNSSKARLRNLE 615
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4383-4420 |
3.43e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.43e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1072265250 4383 QRFLEVQYLTGGLIEPDVEGRVNLDEALHKGTIDARTA 4420
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1658-2552 |
3.47e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1658 QEEAEKQKEDAERETRKRTKAEESALRQ-----KDLAEEELEKQRKLA--EETASHKLSAEQELI-----RLKAEVdSGE 1725
Cdd:TIGR01612 805 KDEDAKQNYDKSKEYIKTISIKEDEIFKiinemKFMKDDFLNKVDKFInfENNCKEKIDSEHEQFaeltnKIKAEI-SDD 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1726 QHRIVLEE--DLFRLKNEVNEAIQRRRGLEEELAKVRAEMEILlKAKSKAEEDSRSTSEKSKQMLEVEASKLRElaeeaa 1803
Cdd:TIGR01612 884 KLNDYEKKfnDSKSLINEINKSIEEEYQNINTLKKVDEYIKIC-ENTKESIEKFHNKQNILKEILNKNIDTIKE------ 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1804 rlravseeakrqRQLAEEDATRQraeAERILKEKLTAINEATRmrteaEIALKEKEAENERLRRLAEDEAYQRKLLEEQA 1883
Cdd:TIGR01612 957 ------------SNLIEKSYKDK---FDNTLIDKINELDKAFK-----DASLNDYEAKNNELIKYFNDLKANLGKNKENM 1016
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1884 AQHKQDIEEK-IHQLKQSSENELERQKTIvdETLKHRRV--IEEEI-RILKINFEkaSVGKSDLELELQKLKNIADETQK 1959
Cdd:TIGR01612 1017 LYHQFDEKEKaTNDIEQKIEDANKNIPNI--EIAIHTSIynIIDEIeKEIGKNIE--LLNKEILEEAEINITNFNEIKEK 1092
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1960 SKEKAEQDAEKQRQLalveearrkEAEEKVKKIIAAEQEAGRQRKVALEEVERLKIKA----DEAKKQKDLAEKEAEKQI 2035
Cdd:TIGR01612 1093 LKHYNFDDFGKEENI---------KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSenyiDEIKAQINDLEDVADKAI 1163
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2036 QlaqdaarlKIDAEEKayyaavqQKEQEMLQTRI-QEQSIYDKLKE------EAEKAKRAAEEAEraKIKAEHEAALSRQ 2108
Cdd:TIGR01612 1164 S--------NDDPEEI-------EKKIENIVTKIdKKKNIYDEIKKllneiaEIEKDKTSLEEVK--GINLSYGKNLGKL 1226
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2109 QAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAeleaakrgQAEQAALKLKQMADAEME-------KHKQFAEKTVRQKE 2181
Cdd:TIGR01612 1227 FLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKS--------PEIENEMGIEMDIKAEMEtfnishdDDKDHHIISKKHDE 1298
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2182 QVEgELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEE------------ELFKVKIQMEELVKLKLRIEQE 2249
Cdd:TIGR01612 1299 NIS-DIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLylneianiynilKLNKIKKIIDEVKEYTKEIEEN 1377
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2250 NK----------MLILKGKDNTQqfLAEEAEKM-------------KQVAEEAARLSVEAQEAARLRKIAeDDLNEQRAL 2306
Cdd:TIGR01612 1378 NKnikdeldkseKLIKKIKDDIN--LEECKSKIestlddkdideciKKIKELKNHILSEESNIDTYFKNA-DENNENVLL 1454
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2307 -----------AEKILK-EKMQAVQEA----SRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAE 2370
Cdd:TIGR01612 1455 lfkniemadnkSQHILKiKKDNATNDHdfniNELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALA 1534
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2371 RRRQLDISAEAERLKLQVVEMSKSQ-----AKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTVVHTLEiQRQHSDKEAE 2445
Cdd:TIGR01612 1535 IKNKFAKTKKDSEIIIKEIKDAHKKfileaEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLE-NFENKFLKIS 1613
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2446 ELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQLRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEKLFDN---- 2521
Cdd:TIGR01612 1614 DIKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDvdqh 1693
|
970 980 990
....*....|....*....|....*....|....*
gi 1072265250 2522 ----EVGKAQKLKSEKERQLAQLEEEKRLLQTSMD 2552
Cdd:TIGR01612 1694 kknyEIGIIEKIKEIAIANKEEIESIKELIEPTIE 1728
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2272-2613 |
3.65e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2272 MKQVAEEAARLSVEAQEAARLRKIAEDDLNEQ-RALAEKILKEKMQAVQEASRLKAEAEMLQkQKEMAMEQAKKLQEDKE 2350
Cdd:pfam05557 18 KKQMELEHKRARIELEKKASALKRQLDRESDRnQELQKRIRLLEKREAEAEEALREQAELNR-LKKKYLEALNKKLNEKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2351 QMQQQlAEETEGFQKTLEAERRRQldisaeAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTKEKMTV- 2429
Cdd:pfam05557 97 SQLAD-AREVISCLKNELSELRRQ------IQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAe 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2430 --VHTLE--IQRQHSDKEAEELRKAiadlenekeklkkeaelLQKKSEEMQKaQKEQLRQETQTLQSTfltEKQILIQKE 2505
Cdd:pfam05557 170 qrIKELEfeIQSQEQDSEIVKNSKS-----------------ELARIPELEK-ELERLREHNKHLNEN---IENKLLLKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2506 KyIEEEKAKLEKlFDNEVGKAQKLKSEKERQLAQLEEEKRLLQTSMDDaMKKQLDAEDRIrqkqEELQQLDKKRQEQERL 2585
Cdd:pfam05557 229 E-VEDLKRKLER-EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLN-LRSPEDLSRRI----EQLQQREIVLKEENSS 301
|
330 340
....*....|....*....|....*...
gi 1072265250 2586 LEEENRKLRERLEQLEQEHRIALEKTRE 2613
Cdd:pfam05557 302 LTSSARQLEKARRELEQELAQYLKKIED 329
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
2150-2346 |
3.95e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 42.38 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2150 QAEQAALKLK-QMADAE----MEKHKQFAEKTVRQKEQVEG-ELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKK 2223
Cdd:pfam15294 71 QAEKWHLKLQaDISELEnrelLEQIAEFEEREFTSSNKKPNfELNKPKLEPLNEGGGSALLHMEIERLKEENEKLKERLK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2224 LVEEELFKVKiqmEELVKLKLRIEQenKMLILKGKDNTQQFLAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDL--- 2300
Cdd:pfam15294 151 TLESQATQAL---DEKSKLEKALKD--LQKEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTLNASTALQKSLEEDLast 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 2301 -------NEQRALAEKILKEKmqaVQEASRLKAEAEMLQKQKEMAMEQAKKLQ 2346
Cdd:pfam15294 226 khellkvQEQLEMAEKELEKK---FQQTAAYRNMKEMLTKKNEQIKELRKRLS 275
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1989-2613 |
4.00e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1989 VKKIIAAEQEAGRQRKVALEEVERLKIKADEAKKQKDlAEKEAEKQIQLAQDAARLKIDAEEKAYYAAVQQKEQEMLQTR 2068
Cdd:COG3096 284 SERALELRRELFGARRQLAEEQYRLVEMARELEELSA-RESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2069 IQEQS-----IYDKLKEEAEKAKRAAEEAERAK---------IKAEHEAALSRQQA----EEAERLKQKAEIEAQAKGQA 2130
Cdd:COG3096 363 LEEQEevveeAAEQLAEAEARLEAAEEEVDSLKsqladyqqaLDVQQTRAIQYQQAvqalEKARALCGLPDLTPENAEDY 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2131 QEDAEkvrkeaeleaAKRGQAEQAALKLKQ-MADAEMEkHKQFaEKTVRQKEQVEGELTKvklqleETDHQKAilddelg 2209
Cdd:COG3096 443 LAAFR----------AKEQQATEEVLELEQkLSVADAA-RRQF-EKAYELVCKIAGEVER------SQAWQTA------- 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2210 rlkEEVTESLRQKKLVEEELFKVKIQMEELVKlklRIEQENkmlilkgkdNTQQFLAEEAEKMKQVAEEAARLSVEAQEA 2289
Cdd:COG3096 498 ---RELLRRYRSQQALAQRLQQLRAQLAELEQ---RLRQQQ---------NAERLLEEFCQRIGQQLDAAEELEELLAEL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2290 ARLRKIAEDDLNEQRALAEKILKEKMQAVQEASRLKAEA-------EMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETE- 2361
Cdd:COG3096 563 EAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawlaaqDALERLREQSGEALADSQEVTAAMQQLLEREREa 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2362 GFQKTLEAERRRQLDISAE----------------AERL----------------------------------------- 2384
Cdd:COG3096 643 TVERDELAARKQALESQIErlsqpggaedprllalAERLggvllseiyddvtledapyfsalygparhaivvpdlsavke 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2385 KLQ---------------------------------VVEMSKSQ--------------AKAEEDAKKFRKQAEDISEKLH 2417
Cdd:COG3096 723 QLAgledcpedlyliegdpdsfddsvfdaeeledavVVKLSDRQwrysrfpevplfgrAAREKRLEELRAERDELAEQYA 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2418 QTELSTKEkmtvvhtleIQRQH----------------SDKEAE--ELRKAIADLENEKEKlkkeaellQKKSEEMQKAQ 2479
Cdd:COG3096 803 KASFDVQK---------LQRLHqafsqfvgghlavafaPDPEAElaALRQRRSELERELAQ--------HRAQEQQLRQQ 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2480 KEQLRQETQTLQ----STFLTEKQILIQKEKYIEEEKAKLEKlfdnevgkAQKLKSEKERQLAQLEEEKRLLQTsmDDAM 2555
Cdd:COG3096 866 LDQLKEQLQLLNkllpQANLLADETLADRLEELREELDAAQE--------AQAFIQQHGKALAQLEPLVAVLQS--DPEQ 935
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 2556 KKQLDAE-DRIRQKQEELQQ----LD-----------KKRQEQERLLEEENRKLRERLEQLEQEHRIALEKTRE 2613
Cdd:COG3096 936 FEQLQADyLQAKEQQRRLKQqifaLSevvqrrphfsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQ 1009
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2242-2545 |
4.04e-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: 43.67 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2242 LKLRIEQENKMLILKGKDNTQqflaeeaeKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEKilkekmqavqea 2321
Cdd:NF012221 1505 LKLTAKAGSNRLEFKGTGHND--------GLGYILDNVVATSESSQQADAVSKHAKQDDAAQNALADK------------ 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2322 srLKAEAEmlqKQKemaMEQAKklqedkeqmQQQLAEeTEGFQKTLEAERRRQLD---------ISAEAERLKLQVVEMS 2392
Cdd:NF012221 1565 --ERAEAD---RQR---LEQEK---------QQQLAA-ISGSQSQLESTDQNALEtngqaqrdaILEESRAVTKELTTLA 1626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2393 K------SQAK-AEEDAKKFRKQ-----AEDISEKLHQTELSTKEKMTVVHTLEIQRQHSDKEAeeLRKAIADLENEKEK 2460
Cdd:NF012221 1627 QgldaldSQATyAGESGDQWRNPfagglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDA--VAKSEAGVAQGEQN 1704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2461 LKKEAELLQKKSEEMQKAQKEQLRQETQTLQStfltekqiliQKEKYIEEEKAKLEKLFDNEVGKAQKLKSEKERQLAQL 2540
Cdd:NF012221 1705 QANAEQDIDDAKADAEKRKDDALAKQNEAQQA----------ESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQ 1774
|
....*
gi 1072265250 2541 EEEKR 2545
Cdd:NF012221 1775 DESDK 1779
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1471-1564 |
4.04e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1471 EDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDELHrKVQAEKDAAREK--QKALEDLEKFRLQAEEAE 1548
Cdd:PRK11448 148 QQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQ-ELEAQLEQLQEKaaETSQERKQKRKEITDQAA 226
|
90
....*....|....*.
gi 1072265250 1549 RRMKQAELEKERQIKQ 1564
Cdd:PRK11448 227 KRLELSEEETRILIDQ 242
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
2077-2148 |
4.18e-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: 42.55 E-value: 4.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 2077 KLKEEA-EKAKRAAEEAERAKIKAEHEaalsrQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKR 2148
Cdd:pfam07946 253 KLRPEAlKKAKKTREEEIEKIKKAAEE-----ERAEEAQEKKEEAKKKEREEKLAKLSPEEQRKYEEKERKKE 320
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2039-2148 |
4.21e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.93 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2039 QDAARLKIDAEekayyAAVQQKEQEMLQTRIQEQSIYDKLKEEAEKakraaeEAERAKIKAEHEAALSRQQAE---EAER 2115
Cdd:COG0711 41 AEAERAKEEAE-----AALAEYEEKLAEARAEAAEIIAEARKEAEA------IAEEAKAEAEAEAERIIAQAEaeiEQER 109
|
90 100 110
....*....|....*....|....*....|....
gi 1072265250 2116 LKQKAEIEAQAKGQAQEDAEKV-RKEAELEAAKR 2148
Cdd:COG0711 110 AKALAELRAEVADLAVAIAEKIlGKELDAAAQAA 143
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1351-1557 |
4.25e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1351 EKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRREVVAVDAEQQKKTIQQELHQMKNNSET 1430
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1431 EIKAKVKLIEEAEYNRKKVEEeiriiRIQLETSQKqksgaedelralrarAEEAERQKKLAQEEAERLRKQVKDEAQKKr 1510
Cdd:pfam05262 264 ADTSSPKEDKQVAENQKREIE-----KAQIEIKKN---------------DEEALKAKDHKAFDLKQESKASEKEAEDK- 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1072265250 1511 eaedelhrkvqaEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELE 1557
Cdd:pfam05262 323 ------------ELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAID 357
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2221-2412 |
4.38e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.91 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2221 QKKLVEEELFKVKIQMEELVKLKLRIEQENKMLILKGKDntqQFLAEEAEKMKQVAEEAARlsveaQEAARLRKIAEDDL 2300
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAA---EKAAKQAEQAAKQAEEKQK-----QAEEAKAKQAAEAK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2301 NEQRALAEKILKEKMQAVQEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEEtEGFQKTLEAERRRQLDISAE 2380
Cdd:TIGR02794 134 AKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE-EAKAKAEAAKAKAAAEAAAK 212
|
170 180 190
....*....|....*....|....*....|..
gi 1072265250 2381 AERLKlqvvemsKSQAKAEEDAKKFRKQAEDI 2412
Cdd:TIGR02794 213 AEAEA-------AAAAAAEAERKADEAELGDI 237
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1785-1970 |
4.84e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1785 KQMLEVEASKLRELAE---EAARLRAvsEEAKRQRQL-AEEDATRQRAEAERILKEKLTAINEATRMRTEAEIALKEKEA 1860
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKEA--EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1861 ENERLRRLAEDEAYQRKLLEEQAAQHKQDIEEKIHQLKQssenELERqktIVDETlkhrrviEEEIRilKINFEKAsvgK 1940
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELER---ISGLT-------AEEAK--EILLEKV---E 164
|
170 180 190
....*....|....*....|....*....|
gi 1072265250 1941 SDLELELQKLknIADETQKSKEKAEQDAEK 1970
Cdd:PRK12704 165 EEARHEAAVL--IKEIEEEAKEEADKKAKE 192
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2398-2656 |
4.87e-03 |
|
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: 43.13 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2398 AEEDAKKfrkqaEDISEKLHQTELSTKEKMTVvhtLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQK 2477
Cdd:TIGR02169 166 AEFDRKK-----EKALEELEEVEENIERLDLI---IDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2478 aQKEQLRQETQTLqstfltekqiliqkEKYIEEEKAKLEKLFDNEVGKAQKLKSEKERQLAQLEEEKRLLQTSMDDAMKK 2557
Cdd:TIGR02169 238 -QKEAIERQLASL--------------EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2558 QLDAEDRIRQKQEELQQLDKKRQEQERLLeeenRKLRERLEQLEQEhrIALEKTREVIITKETVITQTKTMPNGRDAADG 2637
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEI----DKLLAEIEELERE--IEEERKRRDKLTEEYAELKEELEDLRAELEEV 376
|
250
....*....|....*....
gi 1072265250 2638 SAQNGELLNAFDGLRQKIS 2656
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLE 395
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2265-2486 |
5.06e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2265 LAEEAEKMKQVAEEAARLSVEAQEAARLRKIAEDDLNEQRALAEkilkekmQAVQEASRLKAEAEMLQKQKEMAMEQAKK 2344
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-------ALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2345 LQEDKEQMQQQLAEETEGFQKTLEAERRRQLDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQTELSTK 2424
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 2425 EKMTVVHTLEIQRQHSDKEAEELRKAIADLENEKEKLKKEAELLQKKSEEMQKAQKEQLRQE 2486
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1038-1555 |
5.20e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1038 NLDKVNDKTR-KVLAQPDLGDSGPLLRSELDVTLHKMEQVHSMSSIYLDKLKTINLVIRNTHGAEEVVKTYEDQLKEVQT 1116
Cdd:PRK01156 184 NIDYLEEKLKsSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAES 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1117 -----------VPG---DLKELESSKADLKRMR--------GQVEGHQPLFNGLENDLTKAREVSERMLKVHSERDVDLE 1174
Cdd:PRK01156 264 dlsmeleknnyYKEleeRHMKIINDPVYKNRNYindyfkykNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1175 RYREKVQL--LLERWQAIVLQIEVRQRELEQLGKQLRYYRESYEWLIRWITEAKKRQEKIQNVPITDSKTVKEQLMEEKk 1252
Cdd:PRK01156 344 KKSRYDDLnnQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1253 lleeseknrGKVDECQKYAKQYIEAIKDFEVQLVTYKAQ-VEPVV-SPLKKPKvhsaSDNIIQEYVELRTKYSELTTLTS 1330
Cdd:PRK01156 423 ---------SKVSSLNQRIRALRENLDELSRNMEMLNGQsVCPVCgTTLGEEK----SNHIINHYNEKKSRLEEKIREIE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1331 QYIKFItetlrrleeeertaeklkEQERKKLAEVEDQLEKQrQLAEAHAQAKAVAEKEA-LELRMNMQEEVTRREVVAVD 1409
Cdd:PRK01156 490 IEVKDI------------------DEKIVDLKKRKEYLESE-EINKSINEYNKIESARAdLEDIKIKINELKDKHDKYEE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1410 AEQQKKTIQQELHQMKNNSETEIKAKVKLIEeAEYNRKKVEEeiriIRIQLETSQKQKSGAEDELRALRARAEEAERQkk 1489
Cdd:PRK01156 551 IKNRYKSLKLEDLDSKRTSWLNALAVISLID-IETNRSRSNE----IKKQLNDLESRLQEIEIGFPDDKSYIDKSIRE-- 623
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072265250 1490 lAQEEAERLRKQVKdEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAE 1555
Cdd:PRK01156 624 -IENEANNLNNKYN-EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSR 687
|
|
| 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 ... |
2078-2180 |
5.41e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 39.99 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2078 LKEEAEKAKRAAEEAERAKIKAEheaalsrQQAEEAERLKQKAEIEAQA-KGQAQEDAEKVRKEAEleaakrGQAEQAAL 2156
Cdd:pfam00430 28 LDKRRELIADEIAEAEERRKDAA-------AALAEAEQQLKEARAEAQEiIENAKKRAEKLKEEIV------AAAEAEAE 94
|
90 100
....*....|....*....|....
gi 1072265250 2157 KLKQMADAEMEKHKQFAEKTVRQK 2180
Cdd:pfam00430 95 RIIEQAAAEIEQEKDRALAELRQQ 118
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2110-2374 |
5.44e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.53 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2110 AEEAERLKQKaeiEAQAKGQAQEDAEKVRKEAElEAAKRGQAEQAALK-LKQMADAemEKHKQFAEKTVRQKEQVEGELT 2188
Cdd:TIGR02794 49 AQQANRIQQQ---KKPAAKKEQERQKKLEQQAE-EAEKQRAAEQARQKeLEQRAAA--EKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2189 KVKLQLEETDHQKAilddelgrlkeevtESLRQKKLVEEelfkvkiqmeelvkLKLRIEQENKmlilkgkdntqqflAEE 2268
Cdd:TIGR02794 123 EAKAKQAAEAKAKA--------------EAEAERKAKEE--------------AAKQAEEEAK--------------AKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2269 AEKMKQVAEEAarlsvEAQEAARLRKIAEddlneqraLAEKILKEKMQAVQEASRLKAEAEmlQKQKEMAMEQAKKLQED 2348
Cdd:TIGR02794 161 AAEAKKKAEEA-----KKKAEAEAKAKAE--------AEAKAKAEEAKAKAEAAKAKAAAE--AAAKAEAEAAAAAAAEA 225
|
250 260
....*....|....*....|....*.
gi 1072265250 2349 KEQMQQQLAEETEGFQKTLEAERRRQ 2374
Cdd:TIGR02794 226 ERKADEAELGDIFGLASGSNAEKQGG 251
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
40-153 |
5.59e-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: 39.97 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 40 ERDRVQKKTFTKWVNKhlikhwrAEAQRHVNDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQ 110
Cdd:cd21330 9 EGETREERTFRNWMNS-------LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCN 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1072265250 111 IALDFLKLR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 153
Cdd:cd21330 80 YAVELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1683-1832 |
5.68e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1683 LRQKDLAEEELEKQRK-LAEETAShklsAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKVR- 1760
Cdd:COG1579 12 LQELDSELDRLEHRLKeLPAELAE----LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1761 --------AEMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAvsEEAKRQRQLAEEDATRQRAEAER 1832
Cdd:COG1579 88 nkeyealqKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE--KKAELDEELAELEAELEELEAER 165
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
36-264 |
5.80e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 43.01 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 36 DAEDERdrvQKKTFTKWVNKHLIKHwraeaqrHVNDLYEDLRDGHNLISLLEVLSGE---TLPREKGR-------MRFHK 105
Cdd:COG5069 374 DAEGEF---EARVFTFWLNSLDVSP-------EITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKA 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 106 LQNVQIALDFLKLRQVKLVNIRNDDIADGNpKLTLGLIWTIILHFQISDIQVTGQSEDMTAKEKLLLWSQRMSEGY---Q 182
Cdd:COG5069 444 FENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGdkeE 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 183 GLRCDNFTSNWRDGRLFSAIIHRHKPMLIDMNRVyRQTNLENLD----QAFTVAE---RELGVTRLLDPEDVDVPQPdEK 255
Cdd:COG5069 523 GIRSFGDPAGSVSGVFYLDVLKGIHSELVDYDLV-TRGFTEFDDiadaRSLAISSkilRSLGAIIKFLPEDINGVRP-RL 600
|
....*....
gi 1072265250 256 SIITYVSSL 264
Cdd:COG5069 601 DVLTFIESL 609
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1309-1561 |
6.12e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1309 DNIIQEYVELRTKYSELTTLTSQYIKFITETLRRLEEEERTAEKLKEQERKKLAEV----EDQLEKQRQLAEAHAQAKAV 1384
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkelkEERDELNEKLNELREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1385 AEKEALELRMNMQEEVTRREVVAVDAEQQKKTIQQELhqmknnsETEIKAKVKLIEEAEYNRKKVEE---EIRIIRIQLE 1461
Cdd:COG1340 98 RKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEE-------EKELVEKIKELEKELEKAKKALEkneKLKELRAELK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1462 TSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKD---EAQKKREAEDELHRKVQAEKDAAREKQKALEDLE 1538
Cdd:COG1340 171 ELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADElhkEIVEAQEKADELHEEIIELQKELRELRKELKKLR 250
|
250 260
....*....|....*....|...
gi 1072265250 1539 KfrlQAEEAERRMKQAELEKERQ 1561
Cdd:COG1340 251 K---KQRALKREKEKEELEEKAE 270
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1531-1886 |
6.16e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.92 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1531 QKALEDLEKFRLQAEEAERRMKQAELEK-----ERQIKQAHDVAQQSADAELQSKRMSFLEKTTQ----LEMSLKQEHIT 1601
Cdd:COG3899 729 ERALELLPPDPEEEYRLALLLELAEALYlagrfEEAEALLERALAARALAALAALRHGNPPASARayanLGLLLLGDYEE 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1602 VTHLQEEAERL--KKQQLEAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRtkae 1679
Cdd:COG3899 809 AYEFGELALALaeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAA---- 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1680 esALRQKDLAEEELEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLknevNEAIQRRRGLEEELAKV 1759
Cdd:COG3899 885 --ALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAA----AAALAAAAAAAALAAAL 958
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1760 RAEMEILLKAKSKAEEDSRstsekskqmLEVEASKLRELAEEAARLRAVSEEAKRQRQLAEEDATRQRAEAERILKEKLT 1839
Cdd:COG3899 959 ALAAAAAAAAAAALAAAAA---------AAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAA 1029
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1072265250 1840 AINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAAQH 1886
Cdd:COG3899 1030 AAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAA 1076
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1474-1565 |
6.18e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.11 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1474 LRALRARAE-------EAERQKKLAQE---EAERLRKQVKDEAQKKREaedelhrkvQAEKDAAREKQKALEDLEkfrlq 1543
Cdd:cd06503 25 LKALDEREEkiaesleEAEKAKEEAEEllaEYEEKLAEARAEAQEIIE---------EARKEAEKIKEEILAEAK----- 90
|
90 100
....*....|....*....|..
gi 1072265250 1544 aEEAERRMKQAELEKERQIKQA 1565
Cdd:cd06503 91 -EEAERILEQAKAEIEQEKEKA 111
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1350-1579 |
6.35e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1350 AEKLKEQERKKLAEVEDQLEK-QRQLAEAHAQAKAVAEK--EALELRMNMQEEV--TRREVVAVDAE--QQKKTIQQELH 1422
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAaQAELDALQAELEELNEEynELQAELEALQAEIdkLQAEIAEAEAEieERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1423 QMKNNSETEIKAKV--------KLIEEAEYNRKKVEEEIRIIRIQLETSQK---QKSGAEDELRALRARAEEAERQKKLA 1491
Cdd:COG3883 94 ALYRSGGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAEleaKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1492 QEEAERLRKQVKDEAQKKREAEDELHRKVQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQ 1571
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAG 253
|
....*...
gi 1072265250 1572 SADAELQS 1579
Cdd:COG3883 254 AAGAAAGS 261
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2100-2208 |
6.42e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2100 EHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEkvrKEAELEAAKRGQAEQAALKLKQMAdAEMEKHKQFAEKTVRQ 2179
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAE---AQQQELVALEGLAAELEEKQQELE-AQLEQLQEKAAETSQE 213
|
90 100 110
....*....|....*....|....*....|..
gi 1072265250 2180 KEQVEGELTKV---KLQLEETDhQKAILDDEL 2208
Cdd:PRK11448 214 RKQKRKEITDQaakRLELSEEE-TRILIDQQL 244
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1474-1615 |
6.57e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1474 LRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKREAEDElhrkvQAEKDAAREKQKALEDLEKFRLQAEEAERRMKQ 1553
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERN-----QQRQEARREREELQREEERLVQKEEQLDARAEK 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072265250 1554 AELEKERQIKQAHDVAQQSAD-AELQSKRMSFLEKTTQLEMSLKQEHItVTHLQEEAERLKKQ 1615
Cdd:PRK12705 100 LDNLENQLEEREKALSARELElEELEKQLDNELYRVAGLTPEQARKLL-LKLLDAELEEEKAQ 161
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2292-2418 |
6.63e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2292 LRKIAEDDLNEQRALAEKILKEkmqavqeasrlkAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEETEGFQKTLEAER 2371
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEE------------AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLL 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1072265250 2372 RRQLDISAEAERLKLQVVEMSKSQAKAEEDAKKFRKQAEDISEKLHQ 2418
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2315-2453 |
6.69e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2315 MQAVQEASRlkaeaEMLQKQKEMAMEQAKKLQEDKEQMQQQLAE-------ETEGFQKTLEAERRRQLDISAEAERLKLQ 2387
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAIEITTKSQEAAARHQAELLEqeargrlERQKMHDKAKAEEQRTKLLELQAESAAVE 712
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072265250 2388 VVEMSKSQAKAEEDAKKFRKQAEdisekLHQTELSTK-EKMTVVHTLEIQRQHSDKEAEElRKAIAD 2453
Cdd:PTZ00491 713 SSGQSRAEALAEAEARLIEAEAE-----VEQAELRAKaLRIEAEAELEKLRKRQELELEY-EQAQNE 773
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1520-1796 |
6.73e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1520 VQAEKDAAREKQKALEDLEKfrlQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQskrmsflEKTTQLEMSLKQEH 1599
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQ---EIAELEKELAALKKEEKALLKQLAALERRIAALARR-------IRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1600 ITVthLQEEAERLKKQQleAETAKEEAEKELEKWRQKANEALRLRLQAEEIAHKKTLAQEEAEKQKEDAERETRKRTKAE 1679
Cdd:COG4942 85 LAE--LEKEIAELRAEL--EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1680 EsalrqkdlaeeeLEKQRKLAEETASHKLSAEQELIRLKAEVDSGEQHRIVLEEDLFRLKNEVNEAIQRRRGLEEELAKV 1759
Cdd:COG4942 161 E------------LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 1072265250 1760 RAEMEILLKAKSKAEEDSRSTSEKSKQMLEVEASKLR 1796
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFAALKGKLPWPVSGRVVR 265
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1352-1576 |
6.82e-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: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1352 KLKEQERKKLAEVEDQLEKQR-QLAEAHAQAKAVAEKEALELRMNMQeevtrrevvavDAEQQKKTIQQELHQMKNNSET 1430
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDlQQALSLLDKIDASKQRAAAYQKALD-----------DAPAELRELRQELAALQAKAEA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1431 EIKAKVKLIEEAEynrkkVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKR 1510
Cdd:pfam12795 70 APKEILASLSLEE-----LEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1511 EAEDELHRKVQAEKDAAREKQKALE-----------------DLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSA 1573
Cdd:pfam12795 145 PLSEAQRWALQAELAALKAQIDMLEqellsnnnrqdllkarrDLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQ 224
|
...
gi 1072265250 1574 DAE 1576
Cdd:pfam12795 225 LAE 227
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1371-1526 |
7.16e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1371 QRQLAEAHAQAKAV---AEKEAlelrmnmqeEVTRREVVaVDAEQQKKTIQQELHQMKNNSETEIKAKVKLIEEAEYNRK 1447
Cdd:PRK12704 30 EAKIKEAEEEAKRIleeAKKEA---------EAIKKEAL-LEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1448 KVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKK--------LAQEEA-ERLRKQVKDEAQKK-----REAE 1513
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLqelerisgLTAEEAkEILLEKVEEEARHEaavliKEIE 179
|
170
....*....|...
gi 1072265250 1514 DELhrKVQAEKDA 1526
Cdd:PRK12704 180 EEA--KEEADKKA 190
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1950-2155 |
7.28e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1950 LKNIAdetQKSKEKAEQDAEKqrqlaLVEEARRKEAEEKVKKIIAAEqeagrqrkvalEEVERLKIKADEAKKQKDLAEK 2029
Cdd:PRK12704 25 RKKIA---EAKIKEAEEEAKR-----ILEEAKKEAEAIKKEALLEAK-----------EEIHKLRNEFEKELRERRNELQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2030 EAEKQIQLAQDAARLKIDAEEKayyaavqqKEQEMLqtriQEQSIYDKLKEEAEKAKRAAEEAERAKIKA-EHEAALSRQ 2108
Cdd:PRK12704 86 KLEKRLLQKEENLDRKLELLEK--------REEELE----KKEKELEQKQQELEKKEEELEELIEEQLQElERISGLTAE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1072265250 2109 QAEEA--ERLKQKAEIEA-----QAKGQAQEDAEKVRKEAELEAAKRGQAEQAA 2155
Cdd:PRK12704 154 EAKEIllEKVEEEARHEAavlikEIEEEAKEEADKKAKEILAQAIQRCAADHVA 207
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1361-1460 |
7.47e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1361 LAEVEDQLEKQRQLAEAHAQAKAVAEKEALElrmnMQEEVTRREVVAVDAEQQKKTIQQELHQM-KNNSETEIKAKVKLI 1439
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALAEA----QQQELVALEGLAAELEEKQQELEAQLEQLqEKAAETSQERKQKRK 219
|
90 100
....*....|....*....|....*
gi 1072265250 1440 EEAEYNRKKV---EEEIR-IIRIQL 1460
Cdd:PRK11448 220 EITDQAAKRLelsEEETRiLIDQQL 244
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1350-1560 |
7.50e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1350 AEKLKEQERKKLAEVEDQLEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRRevvavdaeqQKKTIQQELHQMKNNsE 1429
Cdd:COG5185 287 LIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQN---------LTAEIEQGQESLTEN-L 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1430 TEIKAKVKLIeEAEYNRKKVEEEIRIIRIQLETS--------QKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQ 1501
Cdd:COG5185 357 EAIKEEIENI-VGEVELSKSSEELDSFKDTIESTkesldeipQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSS 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072265250 1502 VKDEAQKKREAEDELHRKV------------QAEKDAAREKQKALEDLEKFRLQAEEAERRMKqAELEKER 1560
Cdd:COG5185 436 NEEVSKLLNELISELNKVMreadeesqsrleEAYDEINRSVRSKKEDLNEELTQIESRVSTLK-ATLEKLR 505
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
2163-2342 |
8.03e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 42.35 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2163 DAEMEKHKQFAEKTVRQKEQVEGELTKVKLQLEETDHQKAILDDELGRLKEEVTESLRQKKLVEEE--------LFKVKI 2234
Cdd:pfam05911 2 DDLVKQHAKVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQLRNVKEEqeqkihdvVLKKTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2235 QMEelvklKLRIEQENKMlilkgkDNTQQFLAEeaekmkqVAEEAARLSVEAQEAARLRKiaedDLNEQRALAE---KIL 2311
Cdd:pfam05911 82 EWE-----KIKAELEAKL------VETEQELLR-------AAAENDALSRSLQERENLLM----KLSEEKSQAEaeiEAL 139
|
170 180 190
....*....|....*....|....*....|....*....
gi 1072265250 2312 KEKMQAVQ-EASRLKAEAEMLQKQ-------KEMAMEQA 2342
Cdd:pfam05911 140 KSRLESCEkEINSLKYELHVLSKEleirneeKNMSRRSA 178
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
2470-2611 |
8.30e-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: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2470 KKSEEMQKAQKEQLRQETQTLQSTFLTEKQILIQKEKYIEEEKAKLEklfdNEVGKAQKLKSEKERQLAQLEEEKRLLQT 2549
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAK----EKLKKLLQEIMIKVKKLEELEEELQELES 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072265250 2550 SMDDAMKKQLDAEDRIrqkqeelQQLDKKRQEQERLLEEENRKLRERLEQLEQEHRIALEKT 2611
Cdd:smart00787 240 KIEDLTNKKSELNTEI-------AEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLTGWKITKL 294
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1175-1512 |
8.34e-03 |
|
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: 42.36 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1175 RYREKVQLLLERWQAIVLQIEVRQRELEQLGKQLRYYRESYEWLIRWITEAKKRQEKIQNvpitDSKTVKEQLMEEKKLL 1254
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ----EEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1255 EESEKNRGKVDECQKyakQYIEAIKDFEVQLVTYKAQVEPvvspLKKPKVHSASDNIIQEYVELRTKYSELTTLTSQyik 1334
Cdd:TIGR02169 747 SSLEQEIENVKSELK---ELEARIEELEEDLHKLEEALND----LEARLSHSRIPEIQAELSKLEEEVSRIEARLRE--- 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1335 fITETLRRLEEEERTAEKLKEQERKKLAEVEDQ----------LEKQRQLAEAHAQAKAVAEKEALELRMNMQEEVTRRE 1404
Cdd:TIGR02169 817 -IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQiksiekeienLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1405 VVAVDAEQQKKTIQQELHQMKNN-SETEIKAKVKLIEEAEYNRKKVE-EEIRIIRIQLETSQKQKSGAEDELRAL----- 1477
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRlSELKAKLEALEEELSEIEDPKGEdEEIPEEELSLEDVQAELQRVEEEIRALepvnm 975
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1072265250 1478 ---------RARAEEAERQKKLAQEEAERLRKQVKDEAQKKREA 1512
Cdd:TIGR02169 976 laiqeyeevLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1465-1578 |
8.66e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.02 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1465 KQKSGAEDELRALRARAE---------EAERQKKLAQEEAERLRKqvkdEAQKKREAEDELHRKVQAEKDAAREKQKALE 1535
Cdd:pfam05672 1 KPSAGTTDAEEAARILAEkrrqareqrEREEQERLEKEEEERLRK----EELRRRAEEERARREEEARRLEEERRREEEE 76
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1072265250 1536 DLEKFRLQAEEAERRMKQAELEKERQIKQAHDVAQQSADAELQ 1578
Cdd:pfam05672 77 RQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQ 119
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2131-2407 |
8.85e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2131 QEDAEKVRKEAELEAAKRGQAEQAALKLKQMADAEMEKHKQFAEKTVRQKEQVEG---ELTKVKLQLEETDHQKAILDDE 2207
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDElneKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2208 LGRLKEEVtESLRQKKLVEEELFKvkiQMEELVK----LKLRIEQENKmLILKGKDntqqfLAEEAEKMKQVAEEAARLS 2283
Cdd:COG1340 94 LDELRKEL-AELNKAGGSIDKLRK---EIERLEWrqqtEVLSPEEEKE-LVEKIKE-----LEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2284 VEAQEAARLRKIAEDDLNEQRALAEKI--LKEKMQAV-QEASRLKAEAEMLQKQKEMAMEQAKKLQEDKEQMQQQLAEet 2360
Cdd:COG1340 164 ELRAELKELRKEAEEIHKKIKELAEEAqeLHEEMIELyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE-- 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1072265250 2361 egFQKTLEAERRRQLDISAEAERlklqvvemSKSQAKAEEDAKKFRK 2407
Cdd:COG1340 242 --LRKELKKLRKKQRALKREKEK--------EELEEKAEEIFEKLKK 278
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
185-266 |
8.93e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 39.20 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 185 RCDNFTSNWRDGRLFSAIIHRHKP-------MLIDMNRVYRQTNLENLDQAFtvaeRELGVTRLLDPEDVdVpQPDEKSI 257
Cdd:cd21218 32 RVTNFSSDLKDGEVYALLLHSLAPelcdkelVLEVLSEEDLEKRAEKVLQAA----EKLGCKYFLTPEDI-V-SGNPRLN 105
|
....*....
gi 1072265250 258 ITYVSSLYD 266
Cdd:cd21218 106 LAFVATLFN 114
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2072-2158 |
9.06e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2072 QSIYDKLKEEAEKAKRAAEEAERAKikaEHEAALSRQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEA-----ELEAA 2146
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREK---AQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAaetsqERKQK 217
|
90
....*....|..
gi 1072265250 2147 KRGQAEQAALKL 2158
Cdd:PRK11448 218 RKEITDQAAKRL 229
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1739-1893 |
9.26e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.20 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1739 KNEVNEAIQRRRGLEEELAKVRAEMEillKAKSKAEEDSRSTSEKSKQMLEVEASKLRELAEEAARLRAVSEEAKRQRQL 1818
Cdd:PRK12678 48 KGELIAAIKEARGGGAAAAAATPAAP---AAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEA 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072265250 1819 AEEDATRQRAEAERiLKEKLTAINEATRMRTEAEIALKEKEAENERLRRLAEDEAYQRKllEEQAAQHKQDIEEK 1893
Cdd:PRK12678 125 AQARERRERGEAAR-RGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQ--AEAERGERGRREER 196
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1470-1972 |
9.30e-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: 41.98 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1470 AEDELRALRARAEEAERQKKLAQEEaerlRKQVKDEAQKKREAEDELHRKVQAEKDAAR---EKQKALEDL--EKFRLQA 1544
Cdd:pfam05622 5 AQEEKDELAQRCHELDQQVSLLQEE----KNSLQQENKKLQERLDQLESGDDSGTPGGKkylLLQKQLEQLqeENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1545 EEAERRMKQAELEKERQIKQAHDVAQQSADAELQskrmsflekttqlemSLKQEhitVTHLQEEAERLKKQQleaetake 1624
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQ---------------ALKDE---MDILRESSDKVKKLE-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1625 eaeKELEKWRQKANEALRLRLQAeeiahkktlaqeeaeKQKEDAERETRKRTKAEESALRQKDLAEEELEKQRKLAEETa 1704
Cdd:pfam05622 135 ---ATVETYKKKLEDLGDLRRQV---------------KLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQEL- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1705 SHKLSAEQ--------ELIRLKAEVDS--GEQHRIVLEEDLFRLKNevneaiqrrrgleEELAKVRAEMEILLKAKSKAE 1774
Cdd:pfam05622 196 HGKLSEESkkadklefEYKKLEEKLEAlqKEKERLIIERDTLRETN-------------EELRCAQLQQAELSQADALLS 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1775 EDSRSTSEKSKQMLEVE-ASKLRELAEEAARLRAVSEEAKRQRQLAE----EDATRQRAEAERILKEKLTAINEATRMRT 1849
Cdd:pfam05622 263 PSSDPGDNLAAEIMPAEiREKLIRLQHENKMLRLGQEGSYRERLTELqqllEDANRRKNELETQNRLANQRILELQQQVE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1850 EAEIALKEKEAENERLRRLAED-EAYQRKLLEEQAaqHKQDIEEKIHQLKQSSENELERQKTIVDETLKHRrviEEEIRI 1928
Cdd:pfam05622 343 ELQKALQEQGSKAEDSSLLKQKlEEHLEKLHEAQS--ELQKKKEQIEELEPKQDSNLAQKIDELQEALRKK---DEDMKA 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1072265250 1929 L----KINFEKA-SVGKS-------DLELELQKLKNIADETQKSKEKAEQDAEKQR 1972
Cdd:pfam05622 418 MeeryKKYVEKAkSVIKTldpkqnpASPPEIQALKNQLLEKDKKIEHLERDFEKSK 473
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2077-2291 |
9.46e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2077 KLKEEAEKAKRAAEEAERAKikaeheaalsrQQAEEAERLKQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQaal 2156
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAE-----------KMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQ--- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2157 klkqmadaemekhkqfaEKTVRQKEQVEGELTKVKLQLEETDHQKAilddelgrlkeeVTESLRQKKLveeelfkvKIQM 2236
Cdd:pfam15709 419 -----------------ERARQQQEEFRRKLQELQRKKQQEEAERA------------EAEKQRQKEL--------EMQL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2237 EELVKLKLRIEQENKMLILKGKDNTQQFLAEEAEKMKQVAEEAARLSVE-----AQEAAR 2291
Cdd:pfam15709 462 AEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEeamkqAQEQAR 521
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
2053-2162 |
9.58e-03 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 41.55 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2053 YYAAVQQKE--------QEMLQTR--IQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEHEAA---LSRQQAEEAERLKQK 2119
Cdd:PRK10476 84 YELTVAQAQadlaladaQIMTTQRsvDAERSNAASANEQVERARANAKLATRTLERLEPLLAkgyVSAQQVDQARTAQRD 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1072265250 2120 AEIE-AQAKGQAQEDAEKVRKEAELEAAKRgqAEQAALKLKQMA 2162
Cdd:PRK10476 164 AEVSlNQALLQAQAAAAAVGGVDALVAQRA--AREAALAIAELH 205
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1448-1570 |
9.68e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 1448 KVEEEIRIIRIQLETSQKQKSGAEDELRALRARAEEAERQKKLAQEEAERLRKQVKDEAQKKRE--AEDELHRKVQAEKD 1525
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREdlAREALERKAELEAQ 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1072265250 1526 AAREKQ---KALEDLEKFRLQAEEAERRMKQAELEKErQIKQAHDVAQ 1570
Cdd:COG1842 100 AEALEAqlaQLEEQVEKLKEALRQLESKLEELKAKKD-TLKARAKAAK 146
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
2034-2197 |
9.87e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.64 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2034 QIQLAQ-DAARLKIDAEEKAYYAAVQQKeQEMLQTRIQEQSIYDKLKEEAEKAKRAAEEAERAKIKAEHEAA-------- 2104
Cdd:pfam00529 57 QAALDSaEAQLAKAQAQVARLQAELDRL-QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLArrrvlapi 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072265250 2105 --LSRQQAEEAERL--KQKAEIEAQAKGQAQEDAEKVRKEAELEAAKRGQAEQAALKLKQmADAEMEKHKQFAEKTVRqK 2180
Cdd:pfam00529 136 ggISRESLVTAGALvaQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAE-AEAELKLAKLDLERTEI-R 213
|
170
....*....|....*..
gi 1072265250 2181 EQVEGELTKVKLQLEET 2197
Cdd:pfam00529 214 APVDGTVAFLSVTVDGG 230
|
|
| |
