|
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 ... |
34-150 |
4.00e-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: 236.91 E-value: 4.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 34 DRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERdlvrnvrlprekGRMRFHKLQNVQIALD 113
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNVQTALD 68
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655220527 114 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 150
Cdd:cd21188 69 FLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
20-159 |
1.60e-71 |
|
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: 236.03 E-value: 1.60e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 20 QAYENVREKYKDERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlpreKGR 99
Cdd:cd21236 1 QAYENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE------------KGR 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 100 MRFHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 159
Cdd:cd21236 69 MRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
31-161 |
7.83e-70 |
|
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: 231.07 E-value: 7.83e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 31 DERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlpreKGRMRFHKLQNVQI 110
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE------------KGRMRFHKLQNVQI 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 111 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSD 161
Cdd:cd21235 69 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
163-268 |
7.13e-66 |
|
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: 219.12 E-value: 7.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 242
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1655220527 243 PEDVDVAHPDEKSIITYVSSLYDVMP 268
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
164-268 |
3.50e-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: 214.18 E-value: 3.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 243
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1655220527 244 EDVDVAHPDEKSIITYVSSLYDVMP 268
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
31-160 |
4.64e-60 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 202.96 E-value: 4.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 31 DERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGetlprerdlvrnVRLPREKGRMRFHKLQNVQI 110
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSG------------VKLPREKGRMRFHRLQNVQI 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1655220527 111 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 160
Cdd:cd21237 69 ALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
164-268 |
2.18e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 194.82 E-value: 2.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAEReLGVTRLLDP 243
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1655220527 244 EDVDVAHPDEKSIITYVSSLYDVMP 268
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
162-268 |
4.00e-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: 176.77 E-value: 4.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 162 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAEReLGVTRLL 241
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1655220527 242 DPEDVDVAHPDEKSIITYVSSLYDVMP 268
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
36-151 |
5.27e-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: 165.25 E-value: 5.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 36 VQKKTFTKWVNKHLMKAQR-HITDLYEDLRDGHNLISLLEVLSGEtlprerdlvrnvRLPREKGRMRFHKLQNVQIALDF 114
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGK------------KLKPEKGRMRVHHLNNVNRALQV 69
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655220527 115 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21186 70 LEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
22-147 |
9.03e-47 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 164.85 E-value: 9.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 22 YENVREK-YKDERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlprEKGRM 100
Cdd:cd21246 1 FERSRIKaLADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKP-----------TKGKM 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1655220527 101 RFHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21246 70 RIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
164-264 |
5.58e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 162.20 E-value: 5.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 243
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1655220527 244 EDVDVAHPDEKSIITYVSSLY 264
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
164-264 |
5.66e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 156.40 E-value: 5.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 243
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1655220527 244 EDVDVAHPDEKSIITYVSSLY 264
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
22-147 |
5.84e-43 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 153.99 E-value: 5.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 22 YENVR-EKYKDERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlprEKGRM 100
Cdd:cd21193 1 FEKGRiRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKP-----------NRGRL 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1655220527 101 RFHKLQNVQIALDFLkHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21193 70 RVQKIENVNKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
32-151 |
4.08e-42 |
|
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: 151.37 E-value: 4.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 32 ERDRVQKKTFTKWVNKHLMKAQR--HITDLYEDLRDGHNLISLLEVLSGEtlprerdlvrnvRLPREKGRM--RFHKLQN 107
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGE------------KLPCEKGRRlkRVHFLSN 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655220527 108 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21241 69 INTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
35-264 |
1.32e-40 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 162.03 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 35 RVQKKTFTKWVNKHLMKA-QRHITDLYEDLRDGHNLISLLEVLSGEtlprerDLVRNVRLPRekgrMRFHKLQNVQIALD 113
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKD------NAGEYNETPE----TRIHVMENVSGRLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 114 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvngQSDDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSW 192
Cdd:COG5069 78 FIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSW 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 193 RDGKLFNAIIHKHRPALLDMSQVYRQSNQE--NLEQAFSVAERELGVTRLLDPEDV-DVAHPDEKSIITYVSSLY 264
Cdd:COG5069 155 RDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
14-147 |
2.46e-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: 147.48 E-value: 2.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 14 EEQHYVQAYENVREK-YKDERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvr 92
Cdd:cd21318 15 EPAATAKLFECSRIKaLADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKP-------- 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 93 lprEKGRMRFHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21318 87 ---TRGRMRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1787-2656 |
1.34e-39 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 164.16 E-value: 1.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1787 EMDALLQMKIQAEKVSQSNTEKSKQllETEALKMKQLAEEAARLRSV--------AEEAKKQRQLAEDEAARQRAEAEKI 1858
Cdd:PTZ00121 1089 ADEATEEAFGKAEEAKKTETGKAEE--ARKAEEAKKKAEDARKAEEArkaedarkAEEARKAEDAKRVEIARKAEDARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1859 ---LKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKN 1935
Cdd:PTZ00121 1167 eeaRKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1936 IVEETLRQKKVVEEEI-HIIRINFERASKEKSDLEvELKKlkgiADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKV 2014
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMaHFARRQAAIKAEEARKAD-ELKK----AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2015 KKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKqvilaKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKL 2094
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-----AEAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2095 RDEFENAKKLAQAAETAKEKAEKEAALlRQKAEE---AEKLKKAAEdEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAA 2171
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEA-KKKAEEkkkADEAKKKAE-EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2172 LKQKQEADAEMAKHKKEAEQALKQKSQVEKElglvklqldETDKQKAlmdEELQRVKAqvndavKQKAQvENELSKVKMQ 2251
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKKA---------AEAKKKA---DEAKKAEE------AKKAD-EAKKAEEAKK 1535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2252 MDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKmkslAEEAARLSVEAEETARQrkTAEAELAEQRALAEKMLKEKM 2331
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK----AEEDKNMALRKAEEAKK--AEEARIEEVMKLYEEEKKMKA 1609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2332 QAIQEATKLKAEAEELQKQknqaqEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQ 2411
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2412 AKAEEEATRFKKQADEAKvRLQETEKQTTEtvvqklETQRLQSTREADDLKKAIAE-LEKEREKLKRDAQELQNKSKETA 2490
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAK-KAEELKKKEAE------EKKKAEELKKAEEENKIKAEeAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2491 SAQQEQMEQQKAmlQQTFLTEKELLLKRERDVEDEKKKLQ--KHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEA 2568
Cdd:PTZ00121 1758 KIAHLKKEEEKK--AEEIRKEKEAVIEEELDEEDEKRRMEvdKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEV 1835
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2569 V-------------------KKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREklESLEVTSKQAASKTKEIE 2629
Cdd:PTZ00121 1836 AdsknmqleeadafekhkfnKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDK--DDIEREIPNNNMAGKNND 1913
|
890 900
....*....|....*....|....*..
gi 1655220527 2630 VQTDKVPEEQLVSMTTVETTKKVFNGS 2656
Cdd:PTZ00121 1914 IIDDKLDKDEYIKRDAEETREEIIKIS 1940
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
30-147 |
2.22e-39 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 144.43 E-value: 2.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 30 KDERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlprEKGRMRFHKLQNVQ 109
Cdd:cd21317 25 ADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKP-----------TKGRMRIHCLENVD 93
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655220527 110 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21317 94 KALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
164-264 |
3.06e-39 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 143.22 E-value: 3.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 243
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
|
90 100
....*....|....*....|.
gi 1655220527 244 EDVDVAHPDEKSIITYVSSLY 264
Cdd:cd21319 85 EDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
163-268 |
4.07e-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: 142.46 E-value: 4.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 242
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1655220527 243 PEDVDVAHPDEKSIITYVSSLYDVMP 268
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
151-264 |
9.24e-39 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 141.73 E-value: 9.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 151 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 230
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220527 231 AERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 264
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYY 111
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
905-982 |
1.01e-38 |
|
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: 140.43 E-value: 1.01e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 905 LSWQYLMRDIHMIKTWNITMFKTLRVEEYRLALRNLEQHYQDFLRDSQDSQMFGAEDRMQVESNYNRANQHYNTMVSS 982
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
32-151 |
1.65e-38 |
|
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: 141.17 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 32 ERDRVQKKTFTKWVNKHLMKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPRERDLVRNvrlprekgrmRFHKLQNVQ 109
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQpiVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQ----------RAHKLSNIR 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655220527 110 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21190 71 NALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
34-147 |
2.59e-37 |
|
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: 137.14 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 34 DRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerdlvrnvrlPREKGRMRFHKLQNVQIALD 113
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLP-----------KPERGKMRFHKIANVNKALD 71
|
90 100 110
....*....|....*....|....*....|....
gi 1655220527 114 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21214 72 FIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
163-264 |
4.51e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 136.92 E-value: 4.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 242
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1655220527 243 PEDVDVAHPDEKSIITYVSSLY 264
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
160-264 |
6.83e-37 |
|
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: 136.73 E-value: 6.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 160 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTR 239
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1655220527 240 LLDPEDVDVAHPDEKSIITYVSSLY 264
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
167-268 |
1.04e-36 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 135.63 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 167 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 245
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1655220527 246 VDVAHPDEKSIITYVSSLYDVMP 268
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
36-149 |
1.40e-36 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 135.22 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 36 VQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERdlvrnvrlprEKGRMRFHKLQNVQIALDFL 115
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYN----------KNPKMRVQKLENVNKALEFI 73
|
90 100 110
....*....|....*....|....*....|....
gi 1655220527 116 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21215 74 KSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
32-151 |
1.65e-35 |
|
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: 132.26 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 32 ERDRVQKKTFTKWVNKHLMKAQ--RHITDLYEDLRDGHNLISLLEVLSGEtlprerdlvrnvRLPREKGRMRFHKLQNVQ 109
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQ------------QLPREKGHNVFQCRSNIE 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655220527 110 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21242 69 TALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1799-2602 |
5.57e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 148.75 E-value: 5.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1799 EKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSV---AEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTE 1875
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAkkkAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1876 AEVALKAKEAENERLKRQAED--EAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEihi 1953
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEA--- 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1954 irinfERASKEKSDLEVELKKLKGIADETQKskakaeeeaeklkklAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQD 2033
Cdd:PTZ00121 1243 -----KKAEEERNNEEIRKFEEARMAHFARR---------------QAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2034 EVERLKQKAAEANKLKDKAEKelekqvilAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKE 2113
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKK--------AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2114 KAEKEAALLRQKAEE---AEKLKKAAEDEAAKQAKAQKDAERlrkeaeaeaakraaaeaaalKQKQEADAEMAKHKKEAE 2190
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADELKKAAAA--------------------KKKADEAKKKAEEKKKAD 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2191 QAlKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAqvnDAVKQKAQVenelskvKMQMDELlklKVRIEEENLRLM 2270
Cdd:PTZ00121 1435 EA-KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA---DEAKKKAEE-------AKKADEA---KKKAEEAKKKAD 1500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2271 QKNKDNTQKLLAEEAEKmkslAEEAaRLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQ 2350
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKK----AEEA-KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2351 KNQAQEKAKKL--LEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAE----AEKLKLRVKELSSAQAKAEEEATRFKKQ 2424
Cdd:PTZ00121 1576 KNMALRKAEEAkkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelkkAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2425 ADEAKVRLQETEKQTTEtvvqkletqrlqSTREADDLKKAIAELEKEREKLKRDAQElqnKSKETASAQQEQMEQQKAml 2504
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEE------------DKKKAEEAKKAEEDEKKAAEALKKEAEE---AKKAEELKKKEAEEKKKA-- 1718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2505 qqtfltekELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQqrqqklmdEEKKKLQAIMDEAVKKQKEAEAEMKNKQK 2584
Cdd:PTZ00121 1719 --------EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE--------EEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
810 820
....*....|....*....|
gi 1655220527 2585 E--MEALEKKRLEQEKLLAD 2602
Cdd:PTZ00121 1783 EelDEEDEKRRMEVDKKIKD 1802
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
148-264 |
1.93e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 130.17 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 148 HFQISDIQVNGQSDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQA 227
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655220527 228 FSVAERELGVTRLLDPEDVDVAHPDEKSIITYVSSLY 264
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
163-261 |
3.51e-34 |
|
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: 128.31 E-value: 3.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 242
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1655220527 243 PEDVDVAHPDEKSIITYVS 261
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
164-264 |
6.72e-34 |
|
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: 127.91 E-value: 6.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 243
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1655220527 244 EDVDVAHPDEKSIITYVSSLY 264
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
31-151 |
7.19e-33 |
|
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: 125.04 E-value: 7.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 31 DERDRVQKKTFTKWVNKHLMKAQR-HITDLYEDLRDGHNLISLLEVLSGEtlprerdlvrnvRLPREKGRMRFHKLQNVQ 109
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQ------------KLVKEKGSTRVHALNNVN 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655220527 110 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21231 69 KALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
167-269 |
9.49e-33 |
|
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: 124.66 E-value: 9.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 167 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ-ENLEQAFSVAERELGVTRLLDPE 244
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1655220527 245 DVDVAHPDEKSIITYVSSLYDVMPR 269
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
163-261 |
1.72e-32 |
|
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: 123.79 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 163 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 242
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1655220527 243 PEDVDVAHPDEKSIITYVS 261
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1510-2485 |
2.01e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 140.28 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1510 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEE-EKVRQ 1588
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEaRKAED 1138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1589 IKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEE--EANKAREQAEKELETWRLKANEAL 1666
Cdd:PTZ00121 1139 ARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEAR 1218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1667 RLRLRAEEEAQRKSlaqEEAEKQKTEAERDAKkkakaeeaalkqkenaEKELEKQRTFAEqiaqqklsaeqeyirlkADF 1746
Cdd:PTZ00121 1219 KAEDAKKAEAVKKA---EEAKKDAEEAKKAEE----------------ERNNEEIRKFEE-----------------ARM 1262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1747 EHAEQQRGLLDNELQRLKNEVNAAEKQRRQleDELAKvrsemdallqmkiqAEKVSQSNTEKSKQLLETEALKMKQLAEE 1826
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKA--DEAKK--------------AEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1827 AAR----LRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAEN--ERLKRQAEDEAYQ 1900
Cdd:PTZ00121 1327 AKKkadaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkaDEAKKKAEEDKKK 1406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1901 RKLLEDQAAQHKhdiqekitqlqssSVSELDRQKNIVEETLRQKKVVEEeihiirinferasKEKSDlevELKKLkgiAD 1980
Cdd:PTZ00121 1407 ADELKKAAAAKK-------------KADEAKKKAEEKKKADEAKKKAEE-------------AKKAD---EAKKK---AE 1454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1981 ETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEverlKQKAAEANKLKDKAEKELEKQV 2060
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA----KKKADEAKKAEEAKKADEAKKA 1530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2061 ILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRdeFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEA 2140
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK--AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2141 AKQAKaqKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKelglvklQLDETDKQKAlm 2220
Cdd:PTZ00121 1609 AEEAK--KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA-------KKAEEDKKKA-- 1677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2221 dEELQRVKAQVNDAVKQKAQVENELSKVKmqmdellKLKVRIEEENLRLMQKNKDNTQKLLaeEAEKMKSLAEEAARLSV 2300
Cdd:PTZ00121 1678 -EEAKKAEEDEKKAAEALKKEAEEAKKAE-------ELKKKEAEEKKKAEELKKAEEENKI--KAEEAKKEAEEDKKKAE 1747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2301 EAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKlkaeaEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQ 2380
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD-----EEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIN 1822
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2381 KSLEAE----------RKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETeKQTTETVVQKLETQ 2450
Cdd:PTZ00121 1823 DSKEMEdsaikevadsKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA-DEIEKIDKDDIERE 1901
|
970 980 990
....*....|....*....|....*....|....*
gi 1655220527 2451 RLQSTREADDLKKAIAELEKErEKLKRDAQELQNK 2485
Cdd:PTZ00121 1902 IPNNNMAGKNNDIIDDKLDKD-EYIKRDAEETREE 1935
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1520-2563 |
2.17e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 140.28 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1520 EEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKT 1599
Cdd:PTZ00121 1027 EKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKT 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1600 aatqlqamsfseKTTKLEESLKKEQGtvlqlQEEAEKLRKQeEEANKAREQaeKELETWRlKANEALRLRL-RAEEEAQR 1678
Cdd:PTZ00121 1107 ------------ETGKAEEARKAEEA-----KKKAEDARKA-EEARKAEDA--RKAEEAR-KAEDAKRVEIaRKAEDARK 1165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1679 KSLAQEEAEKQKTEAERdaKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEyirlkadfEHAEQQRGLldN 1758
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAAR--KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA--------KKAEAVKKA--E 1233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1759 ELQRLKNEVNAAEKQRRQLE-DELAKVRSEMDALLQMKIQAEKvsqsnTEKSKQLLETEALKMKQLAEEAARLRSVAEEA 1837
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEiRKFEEARMAHFARRQAAIKAEE-----ARKADELKKAEEKKKADEAKKAEEKKKADEAK 1308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1838 KKQRQLAEDEAARQRAEAEKilkeklaaiNEATRLKTEAEVALKAKEAenerlkRQAEDEAYQRKLledQAAQHKHDIQE 1917
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAK---------KKADAAKKKAEEAKKAAEA------AKAEAEAAADEA---EAAEEKAEAAE 1370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1918 KITQLQSSSVSELDRQKNIVEETLRQKKVVEEEihiirinferasKEKSDlevELKKL---KGIADETQKskakaeeeae 1994
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEED------------KKKAD---ELKKAaaaKKKADEAKK---------- 1425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1995 klkklaaeeerkrreAEEKVKKIAAAEEEAARQRKAaqdevERLKQKAAEANKLKDKAEKELEKQvilAKEAAQKSTAAE 2074
Cdd:PTZ00121 1426 ---------------KAEEKKKADEAKKKAEEAKKA-----DEAKKKAEEAKKAEEAKKKAEEAK---KADEAKKKAEEA 1482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2075 QKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKekaekeaallRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLR 2154
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE----------AKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2155 KEAEAEAAKRAAAEAAalKQKQEADAEMAKHKKEaeqALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKA-QVND 2233
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEE--AKKAEEDKNMALRKAE---EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeELKK 1627
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2234 AVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQ-KNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTA 2312
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEeAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2313 EAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKnqaqEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLE 2392
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA----EEAKKDEEEKKKIAHLKKEE----EKKAEEIRKEKEA 1779
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2393 ISAEaeklklrvkELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQrLQSTREADDLKKAIAELEKER 2472
Cdd:PTZ00121 1780 VIEE---------ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME-DSAIKEVADSKNMQLEEADAF 1849
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2473 EKLKRDAQELQNKSKETASaqqeqmeqqkamlqqTFLTEKELLLKRERDVE--DEKKKLQKH-LEDEV-NKAKALKDEQQ 2548
Cdd:PTZ00121 1850 EKHKFNKNNENGEDGNKEA---------------DFNKEKDLKEDDEEEIEeaDEIEKIDKDdIEREIpNNNMAGKNNDI 1914
|
1050
....*....|....*
gi 1655220527 2549 RQQKLMDEEKKKLQA 2563
Cdd:PTZ00121 1915 IDDKLDKDEYIKRDA 1929
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
31-147 |
7.41e-32 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 123.62 E-value: 7.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 31 DERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlprEKGRMRFHKLQNVQI 110
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKP-----------TKGRMRIHCLENVDK 116
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655220527 111 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 147
Cdd:cd21316 117 ALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
151-264 |
7.69e-32 |
|
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: 122.25 E-value: 7.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 151 ISDIQVNGqsddMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 230
Cdd:cd21291 1 IADINEEG----LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220527 231 AERELGVTRLLDPEDV-DVAHPDEKSIITYVSSLY 264
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYF 111
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1377-2590 |
1.34e-31 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 137.26 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1377 SEKLKEDEKKRMAEIQAQleTQKQLAEgHAKSVAK--AELEAqelklkmkEDASQRQGLAVDAEKQKQNIQLELT----- 1449
Cdd:NF041483 85 ADQLRADAERELRDARAQ--TQRILQE-HAEHQARlqAELHT--------EAVQRRQQLDQELAERRQTVESHVNenvaw 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1450 --QLKNLSEQEIRsknQQLEEaqvSRRKLEEEIHLIRIQ---LQTTIKQKSTADDELQKlrdqaAEAEKVRKAAQEEAER 1524
Cdd:NF041483 154 aeQLRARTESQAR---RLLDE---SRAEAEQALAAARAEaerLAEEARQRLGSEAESAR-----AEAEAILRRARKDAER 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1525 LRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQ-AE--------EAERRLKQAEEEKVRQIKVVEEV 1595
Cdd:NF041483 223 LLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQeAEealrearaEAEKVVAEAKEAAAKQLASAESA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1596 -AQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQ-LQEEAEKLRKqeEEANKAREQAEKELETWRLK-ANEALRLRLRA 1672
Cdd:NF041483 303 nEQRTRTAKEEIARLVGEATKEAEALKAEAEQALAdARAEAEKLVA--EAAEKARTVAAEDTAAQLAKaARTAEEVLTKA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1673 EEEAQRKS-LAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQ---RTFAEQIAQQKLSAEQEYIRLKADFEh 1748
Cdd:NF041483 381 SEDAKATTrAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKEyraKTVELQEEARRLRGEAEQLRAEAVAE- 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1749 AEQQRGlldnelQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQ-MKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEA 1827
Cdd:NF041483 460 GERIRG------EARREAVQQIEEAARTAEELLTKAKADADELRStATAESERVRTEAIERATTLRRQAEETLERTRAEA 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1828 ARLRSVAEE-AKKQRQLAEDEAARQRAEAEKILKEKLA-AINEATRLKTEAEVALKAKE-------AENERLKRQAEDEA 1898
Cdd:NF041483 534 ERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEERLTAAEealadarAEAERIRREAAEET 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1899 YQrklLEDQAAqhkhdiqEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIhiirinferASKEKSDLEVELKKLKGI 1978
Cdd:NF041483 614 ER---LRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAARAEGENV---------AVRLRSEAAAEAERLKSE 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1979 ADETqKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKA----AEANKLKDKAEK 2054
Cdd:NF041483 675 AQES-ADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSeellASARKRVEEAQA 753
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2055 ELEKqviLAKEAAQKST----AAEQKAQDVlsknkedllsqeklRDEFENAKKLAQAAETAkekaekeaalLRQKAEE-A 2129
Cdd:NF041483 754 EAQR---LVEEADRRATelvsAAEQTAQQV--------------RDSVAGLQEQAEEEIAG----------LRSAAEHaA 806
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2130 EKLKKAAEDEA--------AKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKqkqEADAEMAKHKKEAEQaLKQKSQVEK 2201
Cdd:NF041483 807 ERTRTEAQEEAdrvrsdayAERERASEDANRLRREAQEETEAAKALAERTVS---EAIAEAERLRSDASE-YAQRVRTEA 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2202 ELGLVKLQLDETdKQKALMDEELQRVK----AQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLR--------- 2268
Cdd:NF041483 883 SDTLASAEQDAA-RTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRadaaaqaeq 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2269 LMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEET-ARQRKTAEAELAEQRALAEKMLKEkmqAIQEATKLKAE-AEE 2346
Cdd:NF041483 962 LIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVkAEAAAEAERLRTEAREEADRTLDE---ARKDANKRRSEaAEQ 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2347 LQKQKNQAQEKAKKLLEDKQEIQQR--LDKETQGfQKSLEAERKRQLEISAEA--------EKLKLRVKELSSAqakAEE 2416
Cdd:NF041483 1039 ADTLITEAAAEADQLTAKAQEEALRttTEAEAQA-DTMVGAARKEAERIVAEAtvegnslvEKARTDADELLVG---ARR 1114
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2417 EATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAElekEREKLKRDAQELQNKSKETASAqqeq 2496
Cdd:NF041483 1115 DATAIRERAEELRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEE---QLAEAEAKAKELVSDANSEASK---- 1187
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2497 meqqkamLQQTFLTEKELLLKrerdvEDEKKKlqkhlEDEVNKAKALKDEQQRQQKLMDEEKKKLqaiMDEAVKKQKEAE 2576
Cdd:NF041483 1188 -------VRIAAVKKAEGLLK-----EAEQKK-----AELVREAEKIKAEAEAEAKRTVEEGKRE---LDVLVRRREDIN 1247
|
1290
....*....|....
gi 1655220527 2577 AEMKNKQKEMEALE 2590
Cdd:NF041483 1248 AEISRVQDVLEALE 1261
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1428-1976 |
1.36e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 136.61 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1428 SQRQGLAVDAEKQK--QNIQLELTQLknlseqEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLR 1505
Cdd:COG1196 200 RQLEPLERQAEKAEryRELKEELKEL------EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1506 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEK 1585
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1586 VRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWR--LKAN 1663
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEeaLAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1664 EALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLK 1743
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1744 ADFEHAEQQRGLLDNELQ---------------RLKNEVNAAEKQRRQLEDELAKVRSEMDALLQM-KIQAEKVSQSNTE 1807
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGveaayeaaleaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLdKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1808 KSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRA----EAEKILKEKLAAINEATRLKTEAEVALKAK 1883
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAvtlaGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1884 EAENERLKRQAEDEAYQ------RKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRIN 1957
Cdd:COG1196 674 LLEAEAELEELAERLAEeeleleEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
570 580
....*....|....*....|
gi 1655220527 1958 FERASKEK-SDLEVELKKLK 1976
Cdd:COG1196 754 EELPEPPDlEELERELERLE 773
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
35-152 |
4.65e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 120.25 E-value: 4.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 35 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlpREKGRMRFHKLQNVQIALDF 114
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKF----------NKRPTFRSQKLENVSVALKF 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655220527 115 LKHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21311 84 LEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1453-2287 |
5.19e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 135.65 E-value: 5.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1453 NLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKvRKAAQEEAERLRKQvnEE 1532
Cdd:PTZ00121 1056 HEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARK-AEEAKKKAEDARKA--EE 1132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1533 TQKKKNAedelkRKSEAEKEAARQKQKALDELQKHKMQAEEAER--RLKQAEE-EKVRQIKVVEEVAQKTAATQLQAMSF 1609
Cdd:PTZ00121 1133 ARKAEDA-----RKAEEARKAEDAKRVEIARKAEDARKAEEARKaeDAKKAEAaRKAEEVRKAEELRKAEDARKAEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1610 SEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQE-EAEK 1688
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElKKAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1689 QKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVN 1768
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1769 AAEKQRRQLE---DELAKVRSEMDALLQMKIQAEKVSQSNTE-KSKQLLETEALKMKQLAEE---AARLRSVAEEAKKQR 1841
Cdd:PTZ00121 1368 AAEKKKEEAKkkaDAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEkkkADEAKKKAEEAKKAD 1447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1842 QLAEDEAARQRAEAekiLKEKLAAINEATRLKTEAEVALKAKEAEN--ERLKRQAED----EAYQRKLLEDQAAQHKHDI 1915
Cdd:PTZ00121 1448 EAKKKAEEAKKAEE---AKKKAEEAKKADEAKKKAEEAKKADEAKKkaEEAKKKADEakkaAEAKKKADEAKKAEEAKKA 1524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1916 QEKITQLQSSSVSELDRQKNIVE-ETLRQKKVVEEEIHIIRInfERASKEKSDLEVELKKlkgiADETQKSKAKAEEEAE 1994
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKaDELKKAEELKKAEEKKKA--EEAKKAEEDKNMALRK----AEEAKKAEEARIEEVM 1598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1995 KLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKaaqdEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAE 2074
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK----KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2075 QKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALlrQKAEE-----AEKLKKAAEDEAAKQAKAQKD 2149
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL--KKAEEenkikAEEAKKEAEEDKKKAEEAKKD 1752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2150 AErlrkeaeaeaakrAAAEAAALKQKQEADAEMAKHKKEA--EQALKQKSqvEKELGLVKLQLDETDKQKALMDEELQRV 2227
Cdd:PTZ00121 1753 EE-------------EKKKIAHLKKEEEKKAEEIRKEKEAviEEELDEED--EKRRMEVDKKIKDIFDNFANIIEGGKEG 1817
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 2228 KAQVNDA----VKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKD-NTQKLLAEEAEK 2287
Cdd:PTZ00121 1818 NLVINDSkemeDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADfNKEKDLKEDDEE 1882
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1340-1951 |
5.36e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 134.68 E-value: 5.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1340 QEYVTLRTRYSELS-TLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQE 1418
Cdd:COG1196 213 ERYRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1419 LKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTAD 1498
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1499 DELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRL 1578
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1579 KQAEEEKVRQIKVVEEVAQKTAATQLQamsfsekttkleeslkkeqgtVLQLQEEAEKLRKQEEEANKAREQAEKELETW 1658
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAA---------------------LAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1659 RLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTF----------AEQI 1728
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpldkiraraALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1729 AQQKLSAEQEYIRLKADFEHAEQQRGLLDNEL---QRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmkiqaekvSQSN 1805
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLlgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA--------GGSL 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1806 TEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEA 1885
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 1886 ENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQS---SSVSELDRQKNIVEETLRQKKVVEEEI 1951
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnlLAIEEYEELEERYDFLSEQREDLEEAR 811
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1566-2153 |
1.50e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 133.52 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1566 KHKMQAEEAERRLKQAEE----------EKVRQIKVVEEvaQKTAATQLQAMSFSEKTTKLEESLKKEQgtvlQLQEEAE 1635
Cdd:COG1196 169 KYKERKEEAERKLEATEEnlerledilgELERQLEPLER--QAEKAERYRELKEELKELEAELLLLKLR----ELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1636 KLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAE 1715
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1716 KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMK 1795
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1796 IQAEKVSQSNTEKSKQLLETEAlkmkQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTE 1875
Cdd:COG1196 403 EELEEAEEALLERLERLEEELE----ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1876 AEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQ-----------------------LQSSSVSELDR 1932
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGavavligveaayeaaleaalaaaLQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1933 QKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEE 2012
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2013 KVKKIAAAEEEAARQRKAAQD-EVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQ 2091
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGgSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 2092 EKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEaAKQAKAQKDAERL 2153
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE-RELERLEREIEAL 779
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
36-151 |
3.73e-30 |
|
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: 117.00 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 36 VQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRerdLVRNVRlprekgrMRFHKLQNVQIALDFL 115
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGR---VIKKPL-------NQHQKLENVTLALKAM 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 1655220527 116 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21227 74 AEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1501-2103 |
6.61e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 131.21 E-value: 6.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1501 LQKLRDQAAEAEKVRKAAQEEAERlrkQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQ 1580
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELKEL---EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1581 AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRL 1660
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1661 KANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYI 1740
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1741 RLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALlqmkiQAEKVSQSNTEKSKQLLETEALKM 1820
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-----AARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1821 KQLAEEAARLRSVAEEAkkQRQLAEDEAARQRAEAekilkekLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQ 1900
Cdd:COG1196 514 LLLAGLRGLAGAVAVLI--GVEAAYEAALEAALAA-------ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1901 RKLLEDQAAQHKhdIQEKITQLQSSSVSELDRQKNIVEETLrqkkvveeEIHIIRINFERASKEKSDLEVELKKLKGIAD 1980
Cdd:COG1196 585 RAALAAALARGA--IGAAVDLVASDLREADARYYVLGDTLL--------GRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1981 EtqkSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQV 2060
Cdd:COG1196 655 G---GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1655220527 2061 ILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKK 2103
Cdd:COG1196 732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
167-268 |
6.69e-30 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 116.21 E-value: 6.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 167 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 245
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1655220527 246 VDVAHPDEKSIITYVSSLYDVMP 268
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1364-1967 |
9.41e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 131.80 E-value: 9.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1364 LETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQN 1443
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1444 IQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEihliRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAE 1523
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA----KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1524 RLRKQVNEETQK---KKNAEdELKRKSEAEKEAARQKQKAlDELQKHKMQAEEAERRLKQAEE-EKVRQIKVVEEVAQKT 1599
Cdd:PTZ00121 1382 AAKKKAEEKKKAdeaKKKAE-EDKKKADELKKAAAAKKKA-DEAKKKAEEKKKADEAKKKAEEaKKADEAKKKAEEAKKA 1459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1600 AATQLQAmsfsEKTTKLEESLKK--EQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETwrLKANEALRL-RLRAEEEA 1676
Cdd:PTZ00121 1460 EEAKKKA----EEAKKADEAKKKaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA--KKAEEAKKAdEAKKAEEA 1533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1677 QRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLL 1756
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1757 DNELQRLKNE-VNAAEKQRRQLEDELAKVRSEMDALLQMKiQAEKVSQSNTEKSKQLLETEalkmKQLAEEAARlrsvAE 1835
Cdd:PTZ00121 1614 KAEEAKIKAEeLKKAEEEKKKVEQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEED----KKKAEEAKK----AE 1684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1836 EAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEValkaKEAENERLKRQAEDEayqrkllEDQAAQHKHDI 1915
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE----NKIKAEEAKKEAEED-------KKKAEEAKKDE 1753
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 1916 QEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSD 1967
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
169-264 |
9.96e-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: 115.52 E-value: 9.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 169 LLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED-VD 247
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1655220527 248 VAHPDEKSIITYVSSLY 264
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
167-266 |
2.93e-29 |
|
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: 114.30 E-value: 2.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 167 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED- 245
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1655220527 246 VDVAHPDEKSIITYVSSLYDV 266
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
32-153 |
3.22e-29 |
|
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: 114.60 E-value: 3.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 32 ERDRVQKKTFTKWVNKHLMKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPRERDLVRNvrlprekgrmRFHKLQNVQ 109
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSH----------RIFRLNNIA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655220527 110 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 153
Cdd:cd21191 71 KALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
36-151 |
7.01e-29 |
|
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: 113.18 E-value: 7.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 36 VQKKTFTKWVNKHLMKAQR-HITDLYEDLRDGHNLISLLEVLSGETLPRERdlvrnvrlprekGRMRFHKLQNVQIALDF 114
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKER------------GSTRVHALNNVNRVLQV 69
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655220527 115 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21232 70 LHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
35-149 |
8.34e-29 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 113.34 E-value: 8.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 35 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDlvrnvrlprEKGRMRFHKLQNVQIALDF 114
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYN---------RRPAFQQHYLENVSTALKF 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220527 115 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21183 74 IEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1464-2339 |
3.60e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 125.94 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1464 QQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADdELQKLRDQAAEAEK-----VRKAAQEEAERLRKQVNEETQKKKN 1538
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAE-RYKELKAELRELELallvlRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1539 AEDELK-----------RKSEAEKEAARQkQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAm 1607
Cdd:TIGR02168 258 LTAELQeleekleelrlEVSELEEEIEEL-QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1608 sfSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALR--LRLRAEEEAQRKSLAQEE 1685
Cdd:TIGR02168 336 --AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELqiASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1686 AEKQKTEAERdakkKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKN 1765
Cdd:TIGR02168 414 DRRERLQQEI----EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1766 EVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALkmkqLAEEAARLRSVAEEAKKQRQ--L 1843
Cdd:TIGR02168 490 RLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA----LGGRLQAVVVENLNAAKKAIafL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1844 AEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAEnerlkrQAEDEAyqRKLLE------------DQAA-- 1909
Cdd:TIGR02168 566 KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV------KFDPKL--RKALSyllggvlvvddlDNALel 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1910 QHKHDIQEKITQLQSSSV---------------SELDRQKNIvEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKK 1974
Cdd:TIGR02168 638 AKKLRPGYRIVTLDGDLVrpggvitggsaktnsSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1975 LKGIADETQKskakaeeeaeklkklaaeeerKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEK 2054
Cdd:TIGR02168 717 LRKELEELSR---------------------QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2055 ELekqvilaKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKK 2134
Cdd:TIGR02168 776 EL-------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2135 AAEDEAAKQAKAQKDAErlrkeaeaeaakraaaeaaalkqkqeadAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETD 2214
Cdd:TIGR02168 849 ELSEDIESLAAEIEELE----------------------------ELIEELESELEALLNERASLEEALALLRSELEELS 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2215 KQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKlkvRIEEE---NLRLMQKNKDNTQKLLAEEAEKMKSL 2291
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE---RLSEEyslTLEEAEALENKIEDDEEEARRRLKRL 977
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 2292 AEEAARL---SVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATK 2339
Cdd:TIGR02168 978 ENKIKELgpvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1364-2087 |
4.15e-28 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 126.02 E-value: 4.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1364 LETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAEleaqelKLKMKEDASQrqglaVDAEKQKQN 1443
Cdd:PTZ00121 1142 AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAE------ELRKAEDARK-----AEAARKAEE 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1444 IQleltQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQ-EEA 1522
Cdd:PTZ00121 1211 ER----KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElKKA 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1523 ERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAAT 1602
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1603 QLQAMSFSEKTTKLEESLKK--EQGTVLQLQEEAEKLRKQEEEANKArEQAEKELETWRLKANE---ALRLRLRAEEEAQ 1677
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKaeEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAEEkkkADEAKKKAEEAKK 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1678 RKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEK--ELEKQRTFAEQIAQQKLSAEQEyiRLKAD----FEHAEQ 1751
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEA--KKKADeakkAEEAKK 1523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1752 QRGLLDNELQRLKNEVNAAEKQRRQleDELAKVRSEMDAllQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLR 1831
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKA--DELKKAEELKKA--EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1832 SVAEEAK-KQRQLAEDEAARQRAE----AEKILKEKLAAINEATRLKTEAEVALKAKEAEN---ERLKRQAEDEayQRKL 1903
Cdd:PTZ00121 1600 LYEEEKKmKAEEAKKAEEAKIKAEelkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaAEEAKKAEED--KKKA 1677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1904 LEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKgiADETQ 1983
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK--KDEEE 1755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1984 KSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEA----NKLKDKAEKELEKQ 2059
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGnlviNDSKEMEDSAIKEV 1835
|
730 740
....*....|....*....|....*...
gi 1655220527 2060 VILAKEAAQKSTAAEQKAQDVLSKNKED 2087
Cdd:PTZ00121 1836 ADSKNMQLEEADAFEKHKFNKNNENGED 1863
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1623-2486 |
8.38e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 124.78 E-value: 8.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1623 EQGTVLQLQE-EAEKLRKQEEEA------NKAREQAEKELEtwrlKANEAL-RLR-LRAEEEAQRKSLaqeeaEKQKTEA 1693
Cdd:TIGR02168 142 EQGKISEIIEaKPEERRAIFEEAagiskyKERRKETERKLE----RTRENLdRLEdILNELERQLKSL-----ERQAEKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1694 ERdakkkakaeeaaLKQKENAEKELEKqrtfaEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQ 1773
Cdd:TIGR02168 213 ER------------YKELKAELRELEL-----ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1774 RRQLEDELAKVRSEMDAL------LQMKIQAEKVSQSNTEKSKQLLETEALKMKQ----LAEEAARLRSVAEEAKKQRQL 1843
Cdd:TIGR02168 276 VSELEEEIEELQKELYALaneisrLEQQKQILRERLANLERQLEELEAQLEELESkldeLAEELAELEEKLEELKEELES 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1844 AE---DEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKIT 1920
Cdd:TIGR02168 356 LEaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1921 QLQSSSVSELDRQKNIVEETLRQkkvVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLA 2000
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELER---LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2001 AEEERKRREAEEKVKKIAAAEEEAA---------------RQRKAAQDEVERLKQKAA------EANKLKDKAEKELEKQ 2059
Cdd:TIGR02168 513 KNQSGLSGILGVLSELISVDEGYEAaieaalggrlqavvvENLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDRE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2060 VILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALL----------------- 2122
Cdd:TIGR02168 593 ILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssi 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2123 ---RQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQV 2199
Cdd:TIGR02168 673 lerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2200 EKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDElLKLKVRIEEENLRLMQKNKDNTQK 2279
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-LRAELTLLNEEAANLRERLESLER 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2280 LLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAK 2359
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2360 KLLEDKQEIQQRLDKETQGFQKsLEAERKRQLEISAEAEKLKLR-VKELSSAQAKAEEEATRFKKQADEAKVRL------ 2432
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENKIKELgpvnla 990
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2433 QETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKS 2486
Cdd:TIGR02168 991 AIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNEN 1044
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1711-2599 |
3.86e-27 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 122.39 E-value: 3.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1711 KENAEKELEKQRTFAEQIAQQKLSAEQEYIRLK----ADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRS 1786
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1787 EMDAlLQMKIQAEKVSQSNTEKSKQLLETEAlkmKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAI 1866
Cdd:pfam02463 259 EIEK-EEEKLAQVLKENKEEEKEKKLQEEEL---KLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1867 NEATRLKTEAEVALKAKEAENErlkrqAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRqkkv 1946
Cdd:pfam02463 335 EEIEELEKELKELEIKREAEEE-----EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK---- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1947 veeeihIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAeekvkkiaaaeeeaar 2026
Cdd:pfam02463 406 ------EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD---------------- 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2027 qrkaaQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQ 2106
Cdd:pfam02463 464 -----ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2107 AAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAE-RLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKH 2185
Cdd:pfam02463 539 ENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLiPKLKLPLKSIAVLEIDPILNLAQLDKATLEADED 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2186 KKEAEQALKQKSQVE--KELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIE 2263
Cdd:pfam02463 619 DKRAKVVEGILKDTEltKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2264 EENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSveAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAE 2343
Cdd:pfam02463 699 LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI--NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2344 AEELQKQKNQAQEKAKKLLEDKQEiqqrldketqgfqkslEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKK 2423
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQE----------------EELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAL 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2424 QADEAKVRLQETEKQTTEtvVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAM 2503
Cdd:pfam02463 841 ELKEEQKLEKLAEEELER--LEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2504 LQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQR-QQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNK 2582
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRlLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
890
....*....|....*..
gi 1655220527 2583 QKEMEALEKKRLEQEKL 2599
Cdd:pfam02463 999 RLEEEKKKLIRAIIEET 1015
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1121-1875 |
4.78e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 122.56 E-value: 4.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1121 IRNTKDAEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEaEADQATFDRLQDELKAATSV--SDKMTRLHSERDA 1198
Cdd:PTZ00121 1130 AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE-DAKKAEAARKAEEVRKAEELrkAEDARKAEAARKA 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1199 ElehyrqlagsllerwqavfaqiDLRQRElsllgrhmnsykqsyewliqwlrEARLRQEKIEAAPVwdskalkeQLTQEK 1278
Cdd:PTZ00121 1209 E----------------------EERKAE-----------------------EARKAEDAKKAEAV--------KKAEEA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1279 KLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDPIASPLKKPKMESASDNIIQeyvtlrtryselstltSQ 1358
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK----------------AE 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1359 YIKFILETQRRLEDDEKASE--KLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKA--ELEAQELKLKMKEDASQRQGLA 1434
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEakKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAadEAEAAEEKAEAAEKKKEEAKKK 1379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1435 VDAEKQKQNIQLELTQLKNLSEqEIRSKNQQLEEAQVSRRKLEEeihliriqLQTTIKQKSTAdDELQKLRDQAAEAEKV 1514
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAE-EDKKKADELKKAAAAKKKADE--------AKKKAEEKKKA-DEAKKKAEEAKKADEA 1449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1515 RKAAQE--EAERLRKQVNEetqkkKNAEDELKRKSEAEKEAARQKQKAlDELQKHKMQAEEAERRLKQAEE-EKVRQIKV 1591
Cdd:PTZ00121 1450 KKKAEEakKAEEAKKKAEE-----AKKADEAKKKAEEAKKADEAKKKA-EEAKKKADEAKKAAEAKKKADEaKKAEEAKK 1523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1592 VEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLrlr 1671
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL--- 1600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1672 AEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEkELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQ 1751
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE-EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1752 QRGllDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLR 1831
Cdd:PTZ00121 1680 AKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1655220527 1832 SVAEEAKKQRQLAEDeaarQRAEAEKILKEKLAAINEATRLKTE 1875
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1811-2635 |
1.09e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 120.93 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1811 QLLETEALKMKQLAEEAA---RLRSVAEEAkkQRQLAEDEAARQRAEAekILKEKLAAINeatRLKTEAEVALKAKEAEN 1887
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAgisKYKERRKET--ERKLERTRENLDRLED--ILNELERQLK---SLERQAEKAERYKELKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1888 ErlKRQAEDEAYQRKLleDQAAQHKHDIQEKITQLQSSsVSELDRQKNIVEETLRQKKV----VEEEIHIIRINFERASK 1963
Cdd:TIGR02168 221 E--LRELELALLVLRL--EELREELEELQEELKEAEEE-LEELTAELQELEEKLEELRLevseLEEEIEELQKELYALAN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1964 EKSDLEVELKKLKGIADETQKSKakaeeeaeklkklaaeeerkrreaeekvKKIAAAEEEAARQRKAAQDEVERLKQKAA 2043
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQL----------------------------EELEAQLEELESKLDELAEELAELEEKLE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2044 EANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLR 2123
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2124 QKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQK----SQV 2199
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfSEG 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2200 EKELGLVKLQLD----------ETDKQ-----KALMDEELQRVKAQVNDAVKQ--KAQVENELSKVKMQmdELLKLKVRI 2262
Cdd:TIGR02168 508 VKALLKNQSGLSgilgvlseliSVDEGyeaaiEAALGGRLQAVVVENLNAAKKaiAFLKQNELGRVTFL--PLDSIKGTE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2263 EEENLRLMQKNKDNTQKLLAEEAEKMKSLA----------------EEAARLSVEAEETAR------QRKTAEAELAEQR 2320
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddlDNALELAKKLRPGYRivtldgDLVRPGGVITGGS 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2321 ALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKL 2400
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2401 KLRVKELSSAQAKAEEEATRFKKQADEAkvrlqETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQ 2480
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEA-----EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2481 ELQNKsKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKhLEDEVNKAKALKDEQQRQQKLMDEEKKK 2560
Cdd:TIGR02168 821 NLRER-LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-LESELEALLNERASLEEALALLRSELEE 898
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 2561 LQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLE-SLEVTSKQAASKTKEIEVQTDKV 2635
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRL 974
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
149-264 |
3.69e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 106.32 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 149 FQISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAF 228
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655220527 229 SVAERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 264
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFY 114
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
35-149 |
3.80e-26 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 105.65 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 35 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDlvrnvrlprEKGRMRFHKLQNVQIALDF 114
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYN---------KRPTFRQMKLENVSVALEF 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220527 115 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21228 74 LERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1835-2663 |
6.67e-26 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 118.54 E-value: 6.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1835 EEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQhKHD 1914
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD-EQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1915 IQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAE 1994
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1995 KLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAE 2074
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2075 QKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLR 2154
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2155 KEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQ--VN 2232
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVraLT 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2233 DAVKQKAQVENELSKVKMQMDELLKLKV-------RIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARL------- 2298
Cdd:pfam02463 572 ELPLGARKLRLLIPKLKLPLKSIAVLEIdpilnlaQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKesglrkg 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2299 -SVEAEETARQRKTAEAELAEQRALAEKMLKEKM--------QAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQ 2369
Cdd:pfam02463 652 vSLEEGLAEKSEVKASLSELTKELLEIQELQEKAeselakeeILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2370 QRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLET 2449
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2450 QRLQSTREADDLKKaiAELEKEREKLKRDAQELQNKSKETASAQQEQmEQQKAMLQQTFLTEKELLLKRERDVEDEKKKL 2529
Cdd:pfam02463 812 EEAELLEEEQLLIE--QEEKIKEEELEELALELKEEQKLEKLAEEEL-ERLEEEITKEELLQELLLKEEELEEQKLKDEL 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2530 QKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQK-----------EAEAEMKNKQKEMEALEKKRLEQEK 2598
Cdd:pfam02463 889 ESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKyeeepeellleEADEKEKEENNKEEEEERNKRLLLA 968
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 2599 LLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVSMTTVETTKKVFNGSVEAVKKD 2663
Cdd:pfam02463 969 KEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGW 1033
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
28-151 |
1.57e-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: 104.45 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 28 KYKDERDRVQKKTFTKWVNKHLMKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlprEKGRMRFHKL 105
Cdd:cd21247 12 KLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRP-----------SRGKMRVHFL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1655220527 106 QNVQIALDFLKHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21247 81 ENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1648-2377 |
2.05e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 116.57 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1648 REQAEKELEtwRLKANEAlRLRLRAEE-EAQRKSLaQEEAEK-------QKTEAERDAKKKAKAEEAALKQKENAEKELE 1719
Cdd:COG1196 174 KEEAERKLE--ATEENLE-RLEDILGElERQLEPL-ERQAEKaeryrelKEELKELEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1720 KqrtfaeqiaqqklsAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAE 1799
Cdd:COG1196 250 E--------------LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1800 KVSQSNTEKSKQLLETEALKMKQLAEEAARLRSvAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVA 1879
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEE-AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1880 LKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEihiirinfE 1959
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL--------A 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1960 RASKEKSDLEVELKKLKGIADEtqkskakaeeeaeklkklaaeeerkrreaeekvkkiaaaeeeaARQRKAAQDEVERLK 2039
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAE-------------------------------------------AAARLLLLLEAEADY 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2040 QKAAEANKLKDKAEKELEKQVILAkEAAQKSTAAEQKAQDVLSknkedLLSQEKLRDEFENAKKLAQaaetakekAEKEA 2119
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVA-VLIGVEAAYEAALEAALA-----AALQNIVVEDDEVAAAAIE--------YLKAA 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2120 ALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQV 2199
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2200 EKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKvRIEEENLRLMQKNKDNTQK 2279
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL-AEAEEERLEEELEEEALEE 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2280 LLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEK----MQAIQEATKLKAEAEELQKQKNQAq 2355
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnLLAIEEYEELEERYDFLSEQREDL- 807
|
730 740
....*....|....*....|..
gi 1655220527 2356 EKAKKLLEdkqEIQQRLDKETQ 2377
Cdd:COG1196 808 EEARETLE---EAIEEIDRETR 826
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
35-152 |
2.22e-25 |
|
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: 103.96 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 35 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDlvrnvrlPREKgrMRFHKLQNVQIALDF 114
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYH-------PRPN--FRQMKLENVSVALEF 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655220527 115 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21310 86 LDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
169-264 |
2.46e-25 |
|
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: 103.00 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 169 LLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED-VD 247
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1655220527 248 VAHPDEKSIITYVSSLY 264
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1716-2567 |
4.21e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 115.92 E-value: 4.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1716 KELEKQrtfAEQIAQQKLSAEQeYIRLKADFEHAeqQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALlQMK 1795
Cdd:TIGR02168 196 NELERQ---LKSLERQAEKAER-YKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQEL-EEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1796 IQAEKVSQSNTEKSKQLLETEalkMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTE 1875
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKE---LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1876 AEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHK------HDIQEKITQLQSSsVSELDRQKNIVEETLRQKKVVEE 1949
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrskvAQLELQIASLNNE-IERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1950 EIhiiriNFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRK 2029
Cdd:TIGR02168 425 EL-----LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2030 AAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKED-------LLSQEKLRDEF---- 2098
Cdd:TIGR02168 500 NLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAakkaiafLKQNELGRVTFlpld 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2099 -ENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAE------------DEAAKQAKAQKDAERLRKEAEAEAAKRA 2165
Cdd:TIGR02168 580 sIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2166 AAEAAALKQKQ---EADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVE 2242
Cdd:TIGR02168 660 VITGGSAKTNSsilERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2243 NELSKVKMQMDELlklkvrieeenlrlmqknkdntQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAeqral 2322
Cdd:TIGR02168 740 AEVEQLEERIAQL----------------------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE----- 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2323 aekmlkekmQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLEISAEAEKLKL 2402
Cdd:TIGR02168 793 ---------QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT----ERRLEDLEEQIEELSEDIESLAA 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2403 RVKELSSAQAKAEEEATRFKKQADEAKVRLQE--TEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQ 2480
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALlrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2481 ELQnkskETASAQQEqmeqqkaMLQQTFLTEKELLLKRERDVEDEKKKLQKHLED--EVNKA--KALKDEQQRQQKL--- 2553
Cdd:TIGR02168 940 NLQ----ERLSEEYS-------LTLEEAEALENKIEDDEEEARRRLKRLENKIKElgPVNLAaiEEYEELKERYDFLtaq 1008
|
890
....*....|....*..
gi 1655220527 2554 ---MDEEKKKLQAIMDE 2567
Cdd:TIGR02168 1009 kedLTEAKETLEEAIEE 1025
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
151-264 |
5.46e-25 |
|
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: 102.86 E-value: 5.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 151 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 230
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220527 231 AERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 264
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFY 111
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
164-264 |
6.06e-25 |
|
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: 102.12 E-value: 6.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 243
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 1655220527 244 ED-VDVAHPDEKSIITYVSSLY 264
Cdd:cd21198 80 ADmVLLSVPDKLSVMTYLHQIR 101
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
164-268 |
6.75e-25 |
|
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: 101.79 E-value: 6.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 243
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1655220527 244 EDVDVAHPDEKSIITYVSSLYDVMP 268
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
165-264 |
7.40e-25 |
|
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: 101.87 E-value: 7.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 165 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPE 244
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1655220527 245 D-VDVAHPDEKSIITYVSSLY 264
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1457-2379 |
1.02e-24 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 114.68 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1457 QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKK 1536
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1537 KNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAatqlqamsfSEKTTKL 1616
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD---------EEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1617 EESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwrlkanEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERD 1696
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE-------ELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1697 AKkkakaeeaalkqkENAEKELEKQRTFAEQIaqqklsaeqeyirlkadfEHAEQQRGLLDNELQRLKNEVNAAEKQRRQ 1776
Cdd:pfam02463 393 KE-------------EELELKSEEEKEAQLLL------------------ELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1777 LEDELAKVRSEMDALLQMKIQAEKVSqsntEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAE 1856
Cdd:pfam02463 442 KQGKLTEEKEELEKQELKLLKDELEL----KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1857 KILKEKL-AAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKN 1935
Cdd:pfam02463 518 DGVGGRIiSAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1936 IVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKL----KGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAE 2011
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLkesaKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2012 EKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEanKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQ 2091
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIKKKEQREKE--ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2092 EKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLrkeaeaeaaKRAAAEAAA 2171
Cdd:pfam02463 756 RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL---------EEEQLLIEQ 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2172 LKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELskvkmQ 2251
Cdd:pfam02463 827 EEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKK-----E 901
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2252 MDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEaelAEQRALAEKMLKEKM 2331
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK---RLLLAKEELGKVNLM 978
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1655220527 2332 QAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGF 2379
Cdd:pfam02463 979 AIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELF 1026
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
163-269 |
2.47e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 100.44 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 163 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ--ENLEQAFSVAERELGVTR 239
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDklENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1655220527 240 -LLDPEdvDVAHPDEKSIITYVSSLYDVMPR 269
Cdd:pfam00307 81 vLIEPE--DLVEGDNKSVLTYLASLFRRFQA 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2041-2615 |
3.50e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.72 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2041 KAAEAN--KLKDKAEkELEKQV-ILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEK 2117
Cdd:COG1196 182 EATEENleRLEDILG-ELERQLePLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2118 EaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLrkeaeaeaakraaaeaaaLKQKQEADAEMAKHKKEAEQALKQKS 2197
Cdd:COG1196 261 E---LAELEAELEELRLELEELELELEEAQAEEYEL------------------LAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2198 QVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKnKDNT 2277
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2278 QKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEK 2357
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2358 AKKLLEDKQEIQQRLD------KETQGFQKSLEAERK---------------------RQLEISAEAEKLKLRVKELSSA 2410
Cdd:COG1196 479 LAELLEELAEAAARLLllleaeADYEGFLEGVKAALLlaglrglagavavligveaayEAALEAALAAALQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2411 QAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAE-----------LEKEREKLKRDA 2479
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYyvlgdtllgrtLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2480 QELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKK 2559
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 2560 KLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADEN------KKLREKLESLE 2615
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEelerelERLEREIEALG 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2282-2641 |
3.59e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.72 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2282 AEEAEKMKSLAEEAARLsvEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKL 2361
Cdd:COG1196 209 AEKAERYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2362 LEDKQEIQQRLDKETQgfQKSLEAERKRQLEISAEaeklklrvkelssaQAKAEEEATRFKKQADEAKVRLQETEKQTTE 2441
Cdd:COG1196 287 QAEEYELLAELARLEQ--DIARLEERRRELEERLE--------------ELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2442 TVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAmlqqtfltEKELLLKRERD 2521
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA--------LLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2522 VEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLmDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLA 2601
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1655220527 2602 DENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLV 2641
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
167-267 |
1.82e-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: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 167 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPEDV 246
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1655220527 247 DVAHPDEKSIITYVSSLYDVM 267
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
39-148 |
3.17e-23 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 97.00 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 39 KTFTKWVNKHLMKA-QRHITDLYEDLRDGHNLISLLEVLSGETLPrerdlVRNVRlpreKGRMRFHKLQNVQIALDFLKH 117
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVD-----KKKVA----ASLSRFKKIENINLALSFAEK 71
|
90 100 110
....*....|....*....|....*....|.
gi 1655220527 118 RQVKLVNIRNDDIADGnPKLTLGLIWTIILH 148
Cdd:smart00033 72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
804-870 |
4.26e-23 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 95.41 E-value: 4.26e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220527 804 QLKPRNpaTPIKSKLPIQAVCDFKQMEITVHRGDECALLNNSQPYKWRVLNDKGSEASVPSICFLVP 870
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
151-264 |
6.00e-23 |
|
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: 97.10 E-value: 6.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 151 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 230
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220527 231 AERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 264
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFY 111
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1363-2286 |
1.67e-22 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 107.36 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1363 ILETQRRLEDDEKASEKLKEDEKKrmAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQ 1442
Cdd:pfam02463 185 LAELIIDLEELKLQELKLKEQAKK--ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1443 NIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEeihliRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEA 1522
Cdd:pfam02463 263 EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL-----KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1523 ERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQktaat 1602
Cdd:pfam02463 338 EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE----- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1603 qlqamsfsekttkleeslkkeqgtvlqlqeeaekLRKQEEEANKAREQAEKEletwrlKANEALRLRLRAEEEAQRKSLA 1682
Cdd:pfam02463 413 ----------------------------------LARQLEDLLKEEKKEELE------ILEEEEESIELKQGKLTEEKEE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1683 QEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQR 1762
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1763 LKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQ 1842
Cdd:pfam02463 533 DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKAT 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1843 LAEDEAARQRAEAEKILKEKlaainEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQL 1922
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDT-----ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAES 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1923 QSSSVSELDRQKNIVEETLRQKKVVE---EEIHIIRINFERASKEKSDLEVELKKLKgIADETQKSKAKAEEEAEKLKKL 1999
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKklkLEAEELLADRVQEAQDKINEELKLLKQK-IDEEEEEEEKSRLKKEEKEEEK 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2000 AAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERlkqkaAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQD 2079
Cdd:pfam02463 767 SELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR-----ALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2080 VLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEA 2159
Cdd:pfam02463 842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2160 EAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKqksQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKA 2239
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE---EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1655220527 2240 QVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAE 2286
Cdd:pfam02463 999 RLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGS 1045
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1125-1931 |
4.94e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 105.99 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1125 KDAEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELkaatsvsdkmtRLHSERDAELEHYR 1204
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEI-----------RKFEEARMAHFARR 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1205 QLAGSLLERWQAVfaqiDLRQRELSllgRHMNSYKQSYEwlIQWLREARLRQEKIEAApvwdsKALKEQLTQEKKLLEEI 1284
Cdd:PTZ00121 1269 QAAIKAEEARKAD----ELKKAEEK---KKADEAKKAEE--KKKADEAKKKAEEAKKA-----DEAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1285 EKNKDQIENCQKDAKAYIDSLKDYefqilAYRALQDPIASPLKKPKMESASDNIIQEyvtlrtryselstltSQYIKFIL 1364
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADE-----AEAAEEKAEAAEKKKEEAKKKADAAKKK---------------AEEKKKAD 1394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1365 ETQRRLEDDEKASEKLK--EDEKKRMAEIQAQLETQKQLAEghAKSVAKAELEAQELKlKMKEDASQRQGLAVDAEKQKQ 1442
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADE--AKKKAEEAKKADEAK-KKAEEAKKAEEAKKKAEEAKK 1471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1443 NIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEihliriqlqttiKQKStadDELQKlRDQAAEAEKVRKAAQ-EE 1521
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA------------KKKA---DEAKK-AEEAKKADEAKKAEEaKK 1535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1522 AERLRKQvnEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAerrlKQAEEEKVRQIKVVEEVAQKTAA 1601
Cdd:PTZ00121 1536 ADEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA----KKAEEARIEEVMKLYEEEKKMKA 1609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1602 TQL----QAMSFSEKTTKLEESLKKEQGTVLQLQEE---AEKLRKQEEEANKAREQAEKELETWRLKANEAlrlrlRAEE 1674
Cdd:PTZ00121 1610 EEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA-----KKAE 1684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1675 EAQRKSlaqEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIaqqKLSAEQEyirlKADFEHAEQQRG 1754
Cdd:PTZ00121 1685 EDEKKA---AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA---KKEAEED----KKKAEEAKKDEE 1754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1755 LLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQ---------AEKVSQSNTEKSKQLLETEALKMKQLAE 1825
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDkkikdifdnFANIIEGGKEGNLVINDSKEMEDSAIKE 1834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1826 EAARLRSVAEEAK--------KQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDE 1897
Cdd:PTZ00121 1835 VADSKNMQLEEADafekhkfnKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDI 1914
|
810 820 830
....*....|....*....|....*....|....
gi 1655220527 1898 AYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELD 1931
Cdd:PTZ00121 1915 IDDKLDKDEYIKRDAEETREEIIKISKKDMCIND 1948
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1212-1791 |
5.16e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.40 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1212 ERWQAVfaQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAApvwdSKALKEQLTQEKKLLEEIEknkDQI 1291
Cdd:COG1196 213 ERYREL--KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELE---LEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1292 ENCQKDAKAYIDSLKDYEFQILAYRALQdpiasplkkpkmESASDNIIQEYVTLRTRYSELSTLTSQyIKFILETQRRLE 1371
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERR------------RELEERLEELEEELAELEEELEELEEE-LEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1372 DDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQL 1451
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1452 KNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRI--QLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQV 1529
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELlaELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1530 NEETQKKKNAE-----------DELKRKSEAEKEAARQKQKALDELQkhkmQAEEAERRLKQAEEEKVRQIKVVEEVAQK 1598
Cdd:COG1196 511 KAALLLAGLRGlagavavligvEAAYEAALEAALAAALQNIVVEDDE----VAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1599 TAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQR 1678
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1679 KSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDN 1758
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
570 580 590
....*....|....*....|....*....|...
gi 1655220527 1759 ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAL 1791
Cdd:COG1196 747 LLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
36-151 |
5.57e-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: 93.51 E-value: 5.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 36 VQKKTFTKWVNKHLMKAQRH--ITDLYEDLRDGHNLISLLEVLSGETLPrerdlvrnvrlPREKGRMRFHKLQNVQIALD 113
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVD-----------KKKLNKSEFDKLENINLALD 70
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655220527 114 FLKHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:pfam00307 71 VAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2026-2567 |
1.13e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.25 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2026 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLA 2105
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2106 QAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKH 2185
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2186 KKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEE 2265
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2266 NLRLMQ--------KNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEA 2337
Cdd:COG1196 500 EADYEGflegvkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2338 TKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQ--KSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAE 2415
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLlgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2416 EEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQE 2495
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2496 QMEQQKAMLQQTFLTEKELLLKRErDVEDEKKKLQKHLE----------DEVNKAKALKDEQQRQQKLMDEEKKKLQAIM 2565
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLE-ELERELERLEREIEalgpvnllaiEEYEELEERYDFLSEQREDLEEARETLEEAI 818
|
..
gi 1655220527 2566 DE 2567
Cdd:COG1196 819 EE 820
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1365-2257 |
1.19e-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: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1365 ETQRRLEDDEKASEKLkEDEKKRMAEIQAQLETQKQLAEG-HAKSVAKAELEAQELKLKMKEdasqrqglAVDAEKQKQN 1443
Cdd:TIGR02168 176 ETERKLERTRENLDRL-EDILNELERQLKSLERQAEKAERyKELKAELRELELALLVLRLEE--------LREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1444 IQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAE 1523
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1524 RLRkqvneetQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEkvrqikvVEEVAQKTAATQ 1603
Cdd:TIGR02168 327 ELE-------SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1604 LQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQ 1683
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1684 EEAEKQKTEAErdakkkakaEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQ---------EYIRLKADFEHAeqqrg 1754
Cdd:TIGR02168 473 AEQALDAAERE---------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAA----- 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1755 lLDNELQ-RLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLR-- 1831
Cdd:TIGR02168 539 -IEAALGgRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRka 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1832 ------------SVAEEAKKQRQLAEDEA---------------ARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKE 1884
Cdd:TIGR02168 618 lsyllggvlvvdDLDNALELAKKLRPGYRivtldgdlvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1885 AENERLK---RQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNI---VEETLRQKKVVEEEIHIIRINF 1958
Cdd:TIGR02168 698 KALAELRkelEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLskeLTELEAEIEELEERLEEAEEEL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1959 ERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERL 2038
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2039 KQKAAEANKLKDKAEKELekqvilakEAAQKSTAAEQKAQDVLSKNKEDLlsQEKLRDEFENAKKlaqaaetakekaeke 2118
Cdd:TIGR02168 858 AAEIEELEELIEELESEL--------EALLNERASLEEALALLRSELEEL--SEELRELESKRSE--------------- 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2119 aalLRQKAEEA-EKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAeqalkqks 2197
Cdd:TIGR02168 913 ---LRRELEELrEKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI-------- 981
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 2198 qveKELGLVKLQ-LDETDKQKalmdEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLK 2257
Cdd:TIGR02168 982 ---KELGPVNLAaIEEYEELK----ERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
151-264 |
1.95e-21 |
|
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: 92.83 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 151 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 230
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220527 231 AERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 264
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFY 111
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
35-152 |
3.88e-21 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 92.07 E-value: 3.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 35 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDlvrnvrlprEKGRMRFHKLQNVQIALDF 114
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHN---------QRPTFRQMQLENVSVALEF 89
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655220527 115 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21308 90 LDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
35-152 |
4.09e-21 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 92.07 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 35 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERdlvrnvrlpREKGRMRFHKLQNVQIALDF 114
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKY---------HQRPTFRQMQLENVSVALEF 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655220527 115 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21309 87 LDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
164-264 |
4.95e-21 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 90.87 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 243
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1655220527 244 EDVDV--AHPDEKSIITYVSSLY 264
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1271-1977 |
1.29e-20 |
|
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: 101.29 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1271 KEQLTQEKKLLEEIEKNKDQIENCQKDAKAYID------------SLKDYEFQILAYRALQDPIASP------------- 1325
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSLERQAEKAERYKElkaelrelelalLVLRLEELREELEELQEELKEAeeeleeltaelqe 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1326 ---------LKKPKMESASDNIIQEYVTLrtrYSELSTLTSQyIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLE 1396
Cdd:TIGR02168 265 leekleelrLEVSELEEEIEELQKELYAL---ANEISRLEQQ-KQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1397 TQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQeIRSKNQQLEEAQVSRRKL 1476
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE-IERLEARLERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1477 EEEIHLIRIQLQTtiKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRkseaekeaARQ 1556
Cdd:TIGR02168 420 QQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ--------LQA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1557 KQKALDELQKHKMQAEEAERRLKQAEEEK-------VRQIKVVEE---------------VAQKTAATQLQAMSF----- 1609
Cdd:TIGR02168 490 RLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvlSELISVDEGyeaaieaalggrlqaVVVENLNAAKKAIAFlkqne 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1610 SEKTTKLEESLKKE---QGTVLQLQEEAEKLRKQEEEANKAREQAEKELETW--------RLKANEALRLRLRAEE---- 1674
Cdd:TIGR02168 570 LGRVTFLPLDSIKGteiQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvdDLDNALELAKKLRPGYrivt 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1675 ---------------EAQRKSLAQ------EEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKL 1733
Cdd:TIGR02168 650 ldgdlvrpggvitggSAKTNSSILerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1734 SAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAL----LQMKIQAEKVSQSNTEKS 1809
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqiEQLKEELKALREALDELR 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1810 KQLLETE------ALKMKQLAEEAARLRSVAEEAKKQ-RQLAED--EAARQRAEAEKILKEKLAAINEATRLKTEAEVAL 1880
Cdd:TIGR02168 810 AELTLLNeeaanlRERLESLERRIAATERRLEDLEEQiEELSEDieSLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1881 KAKEAENERLKRQAEDEAYQRKLLEDQ---AAQHKHDIQEKITQLQsssvSELDRQKniveETLRQKKVVEEEIHIIRIN 1957
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRREleeLREKLAQLELRLEGLE----VRIDNLQ----ERLSEEYSLTLEEAEALEN 961
|
810 820
....*....|....*....|
gi 1655220527 1958 FERASKEKsdLEVELKKLKG 1977
Cdd:TIGR02168 962 KIEDDEEE--ARRRLKRLEN 979
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
168-266 |
1.46e-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: 89.72 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 168 KLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD-PEDV 246
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1655220527 247 DVAHPDEKSIITYVSSLYDV 266
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYEL 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1126-1791 |
1.83e-20 |
|
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: 100.52 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1126 DAEDTVKSYESRLRDVSKvpaEEKEVEAHRSQLKAMRAEAEAD-----------QATFDRLQDELKAATSVSDKMTRLHS 1194
Cdd:TIGR02168 299 RLEQQKQILRERLANLER---QLEELEAQLEELESKLDELAEElaeleekleelKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1195 ERDAELEHYRQLAGSLLERWQAVFAQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQ--------EKIEAAPVWD 1266
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaeleelEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1267 SKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEfqiLAYRALQDPIASPLKKPKMESASDNIIQEYVTLR 1346
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ---ENLEGFSEGVKALLKNQSGLSGILGVLSELISVD 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1347 TRYS-ELSTLTSQYIKFILetQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKE 1425
Cdd:TIGR02168 533 EGYEaAIEAALGGRLQAVV--VENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1426 DASQRQGLA--------VDAEKQKQNIQLELTQLKNL--------------------SEQEIRSKNQQLEEAQVSRRKLE 1477
Cdd:TIGR02168 611 DPKLRKALSyllggvlvVDDLDNALELAKKLRPGYRIvtldgdlvrpggvitggsakTNSSILERRREIEELEEKIEELE 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1478 EEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQK 1557
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1558 QKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKL 1637
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1638 RKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKkakaeeaalkqkenAEKE 1717
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE--------------LRRE 916
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 1718 LEKQRTFAEQIAQQKLSAEQEYIRLKadfehaEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAL 1791
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1364-2442 |
3.24e-20 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 99.86 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1364 LETQRRLEDDEKASEKLKEdEKKRMAE-IQAQLETQKQLAEGHAKSVA-KAELEA--QELKLKMKEDASQRQGLAVDAEK 1439
Cdd:pfam01576 22 QKAESELKELEKKHQQLCE-EKNALQEqLQAETELCAEAEEMRARLAArKQELEEilHELESRLEEEEERSQQLQNEKKK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1440 QKQNIQLELTQLKnlsEQEIRSKNQQLEE--AQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEkvrka 1517
Cdd:pfam01576 101 MQQHIQDLEEQLD---EEEAARQKLQLEKvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEE----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1518 aqEEAERLRKQVNEETQKKKNAEDELKR--KSEAEKEAARQKQKA-LDELQKH----KMQAEEAERRLKQAEEE-KVRQI 1589
Cdd:pfam01576 173 --EKAKSLSKLKNKHEAMISDLEERLKKeeKGRQELEKAKRKLEGeSTDLQEQiaelQAQIAELRAQLAKKEEElQAALA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1590 KVVEEVAQKTAAtqlqamsfsekttklEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETwrLKANEALRLR 1669
Cdd:pfam01576 251 RLEEETAQKNNA---------------LKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEA--LKTELEDTLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1670 LRAEEEAQRKSLAQEEAEKQKT---EAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADF 1746
Cdd:pfam01576 314 TTAAQQELRSKREQEVTELKKAleeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1747 E-------HAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAE----KVSQSNTEKSKQLLET 1815
Cdd:pfam01576 394 RtlqqakqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgkniKLSKDVSSLESQLQDT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1816 EAL---KMKQLAEEAARLRSVAEEAKK-QRQLAEDEAARQRAEAEkilkeklaaineatrlkteaevaLKAKEAENERLK 1891
Cdd:pfam01576 474 QELlqeETRQKLNLSTRLRQLEDERNSlQEQLEEEEEAKRNVERQ-----------------------LSTLQAQLSDMK 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1892 RQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQ--SSSVSELDRQKNiveetlrqkkvveeeihiirinfeRASKEKSDLE 1969
Cdd:pfam01576 531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLEekAAAYDKLEKTKN------------------------RLQQELDDLL 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1970 VELKKLKGIADETQKskakaeeeaeklkklaaeeerkrreaeekvkkiaaaeeeaaRQRKAAQDEVERlKQKAAEANKLK 2049
Cdd:pfam01576 587 VDLDHQRQLVSNLEK-----------------------------------------KQKKFDQMLAEE-KAISARYAEER 624
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2050 DKAEKELE----KQVILAKEAAQKSTAAEQ--KAQDVLSKNKEDLLSQE----KLRDEFENAKKLAQAAETAkekaekea 2119
Cdd:pfam01576 625 DRAEAEAReketRALSLARALEEALEAKEEleRTNKQLRAEMEDLVSSKddvgKNVHELERSKRALEQQVEE-------- 696
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2120 alLRQKAEEAEKLKKAAED-----EAAKQA-KAQKDAErlrkeAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQAL 2193
Cdd:pfam01576 697 --MKTQLEELEDELQATEDaklrlEVNMQAlKAQFERD-----LQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAV 769
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2194 KQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKqkaqvenELSKVKMQMDELL--------KLKvRIEEE 2265
Cdd:pfam01576 770 AAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQR-------ELEEARASRDEILaqskesekKLK-NLEAE 841
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2266 NLRL-------------MQKNKDNTQKLLAEEAEKMKSLAEEAARLSV-------EAEETA--------RQRKTAE---- 2313
Cdd:pfam01576 842 LLQLqedlaaserarrqAQQERDELADEIASGASGKSALQDEKRRLEAriaqleeELEEEQsntellndRLRKSTLqveq 921
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2314 --AELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDK-QEIQQRLDKETQGFQKS-------- 2382
Cdd:pfam01576 922 ltTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKiAQLEEQLEQESRERQAAnklvrrte 1001
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 2383 ---------LEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRfkkqADEAKVRLQETEKQTTET 2442
Cdd:pfam01576 1002 kklkevllqVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASR----ANAARRKLQRELDDATES 1066
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
164-263 |
3.78e-20 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 88.31 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 243
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEP 79
|
90 100
....*....|....*....|..
gi 1655220527 244 EDVdVAH--PDEKSIITYVSSL 263
Cdd:cd21255 80 ADM-VLLpiPDKLIVMTYLCQL 100
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1149-1906 |
5.09e-20 |
|
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: 99.36 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1149 KEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQREL 1228
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1229 sllgRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDY 1308
Cdd:TIGR02168 312 ----ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1309 EFQILAYRALQDPIASPLKKPKMESAS--DNIIQEYVTLRTRYS-----ELSTLTSQYIKFILETQRRLEDDEKASEKLK 1381
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDrrERLQQEIEELLKKLEeaelkELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1382 E----------DEKKRMAEIQAQ---LETQKQLAEGHAKSVAKAELEAQEL---------KLKMKE-------------- 1425
Cdd:TIGR02168 468 EeleeaeqaldAAERELAQLQARldsLERLQENLEGFSEGVKALLKNQSGLsgilgvlseLISVDEgyeaaieaalggrl 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1426 -----DASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKN----QQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKST 1496
Cdd:TIGR02168 548 qavvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDreilKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1497 ADDELQKLRDQAAEAEKVRkAAQEEAERLRK---------QVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKH 1567
Cdd:TIGR02168 628 VDDLDNALELAKKLRPGYR-IVTLDGDLVRPggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1568 KMQAEEAERRLKQAEEEKVRQIkvveevaqktAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKA 1647
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQI----------SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1648 REQAEKELETwrlkaNEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAkaeeaalkqKENAEKELEKQRTFAEQ 1727
Cdd:TIGR02168 777 LAEAEAEIEE-----LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER---------LESLERRIAATERRLED 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1728 IAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTE 1807
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1808 KSKQL-LETEALKMkQLAEEAARLRS----VAEEAKKQRQLAEDEAARQRAEAEKiLKEKLAA---INEAtrlkteaevA 1879
Cdd:TIGR02168 923 KLAQLeLRLEGLEV-RIDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKR-LENKIKElgpVNLA---------A 991
|
810 820 830
....*....|....*....|....*....|
gi 1655220527 1880 LKAKEAENER---LKRQAEDEAYQRKLLED 1906
Cdd:TIGR02168 992 IEEYEELKERydfLTAQKEDLTEAKETLEE 1021
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
160-267 |
1.14e-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: 87.31 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 160 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTR 239
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*....
gi 1655220527 240 LLDPEDV-DVAHPDEKSIITYVSSLYDVM 267
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
164-263 |
6.36e-19 |
|
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: 84.90 E-value: 6.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 243
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFA-SLGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1655220527 244 ED-VDVAHPDEKSIITYVSSL 263
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1127-1815 |
1.13e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.62 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1127 AEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAAtsvsdkmtrlHSERDAELEHYRQL 1206
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----------LEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1207 AGSLLERWQAVFAQIDLRQRELSLLGRhmnsykqsyewliqwlREARLRQEKIEAApvWDSKALKEQLTQEKKLLEEIEK 1286
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEE----------------RLEELEEELAELE--EELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1287 NKDQIENCQKDAKAyidslkdyefqilayralqdpiasplKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILET 1366
Cdd:COG1196 352 ELEEAEAELAEAEE--------------------------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1367 QRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEgHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQL 1446
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1447 ELTQLKNLSE-QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQkLRDQAAEAEKVRKAAQEEAERL 1525
Cdd:COG1196 485 ELAEAAARLLlLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE-AALAAALQNIVVEDDEVAAAAI 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1526 rkqvneETQKKKNAEdelkRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQ 1605
Cdd:COG1196 564 ------EYLKAAKAG----RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1606 AMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEE 1685
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1686 AEKQKTEAERDakkkakaeeaalKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLkN 1765
Cdd:COG1196 714 EERLEEELEEE------------ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL-G 780
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 1766 EVN-------AAEKQRRQ-LEDELAKVRSEMDALLQMkiqaekVSQSNTEKSKQLLET 1815
Cdd:COG1196 781 PVNllaieeyEELEERYDfLSEQREDLEEARETLEEA------IEEIDRETRERFLET 832
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2345-2642 |
1.75e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.85 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2345 EELQKQKNQAqEKAKKLLEDKQEIQQRLD-KETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKK 2423
Cdd:COG1196 203 EPLERQAEKA-ERYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2424 QADEAKVRLQETEKQttetvVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKsKETASAQQEQMEQQKAM 2503
Cdd:COG1196 282 ELEEAQAEEYELLAE-----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2504 LQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAImdEAVKKQKEAEAEmKNKQ 2583
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL--ERLEEELEELEE-ALAE 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 2584 KEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVS 2642
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
164-262 |
1.83e-18 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 83.44 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGKLFNAIIHKHRPALLDMS-QVYRQSNQENLEQAFSVAERELGVTRLLD 242
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNeSLDKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1655220527 243 PEDVDVAHPDEKSIITYVSS 262
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
166-264 |
3.11e-18 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 83.12 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 166 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 245
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1655220527 246 -VDVAHPDEKSIITYVSSLY 264
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
167-263 |
3.17e-18 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 82.75 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 167 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ----ENLEQAFSVAERELGVTRLLD 242
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1655220527 243 PEDVDVAHPDEKSIITYVSSL 263
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1374-2374 |
4.50e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 92.82 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1374 EKASEKLKEDEKkRMAEIQAQLETQKQLAEGHAKSVAKAElEAQELKLKMKE-DASQRQGLAVDAEKQKQNIqleltqlk 1452
Cdd:TIGR02169 173 EKALEELEEVEE-NIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREyEGYELLKEKEALERQKEAI-------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1453 nlsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLqttikqkstaddelqklrdqAAEAEKVRKAAQEEAERLRKQVNEE 1532
Cdd:TIGR02169 243 ---ERQLASLEEELEKLTEEISELEKRLEEIEQLL--------------------EELNKKIKDLGEEEQLRVKEKIGEL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1533 TQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLkqaEEEKVRQIKVVEEVAqktaatqlqamsfsEK 1612
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI---EEERKRRDKLTEEYA--------------EL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1613 TTKLEESLKkeqgtvlQLQEEAEKLRKQEEEANKAREqaekELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTE 1692
Cdd:TIGR02169 363 KEELEDLRA-------ELEEVDKEFAETRDELKDYRE----KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1693 AERDAKKKAKAeeaalkqKENAEKELEKQrtfaeqiaqqklsaEQEYIRLKADFEHAEQqrglldnELQRLKNEVNAAEK 1772
Cdd:TIGR02169 432 IEAKINELEEE-------KEDKALEIKKQ--------------EWKLEQLAADLSKYEQ-------ELYDLKEEYDRVEK 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1773 QRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEAlKMKQLAEEAARLRSVAEEAKKQRQLAEDEAArqR 1852
Cdd:TIGR02169 484 ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVA-QLGSVGERYATAIEVAAGNRLNNVVVEDDAV--A 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1853 AEAEKILKEKlaAINEATRLKteaevalkakeaenerLKRQAEDEAYQRKLLEDQAAQHKHDiqekitqlqsssVSELDR 1932
Cdd:TIGR02169 561 KEAIELLKRR--KAGRATFLP----------------LNKMRDERRDLSILSEDGVIGFAVD------------LVEFDP 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1933 Q-KNIVEETLRQKKVVE--EEIHIIRINFERASkeksdLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRRE 2009
Cdd:TIGR02169 611 KyEPAFKYVFGDTLVVEdiEAARRLMGKYRMVT-----LEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEG 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2010 AEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAA-------QKSTAAEQKAQDVLS 2082
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEedlssleQEIENVKSELKELEA 765
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2083 KNKEDLLSQEKLRDEFENAKklaqaaetakekaekeAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERlrkeaeaeaa 2162
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLE----------------ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ---------- 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2163 kraaAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDEtdkqkalMDEELQRVKAQVNDAVKQKAQVE 2242
Cdd:TIGR02169 820 ----KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE-------LEEELEELEAALRDLESRLGDLK 888
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2243 NELSKVKMQMDEllkLKVRIEEENLRLMQKNK-DNTQKLLAEEA-EKMKSLAEEAARLSVEAEETARQRKTAEAELAEQR 2320
Cdd:TIGR02169 889 KERDELEAQLRE---LERKIEELEAQIEKKRKrLSELKAKLEALeEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2321 ALaEKMLKEKMQAIQeatklkaEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDK 2374
Cdd:TIGR02169 966 EI-RALEPVNMLAIQ-------EYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2212-2629 |
4.52e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.43 E-value: 4.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2212 ETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKD---------NTQKLLA 2282
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSkrkleekirELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2283 EEAEKMKSLAEEAARLS---------VEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQ 2353
Cdd:PRK03918 270 ELKKEIEELEEKVKELKelkekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2354 AQ-------------EKAKKLLEDKQEIQQRL-DKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEAT 2419
Cdd:PRK03918 350 LEkrleeleerhelyEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2420 RFKKQADEAKVRLQETEKQTTETVVQKLetqrlqsTREADDLKKAIAELEKEREKLKRDAQELQN--KSKETASAQQEQM 2497
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRKELLEEY-------TAELKRIEKELKEIEEKERKLRKELRELEKvlKKESELIKLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2498 EQQKAMLQQTFLTEKELLLKRERDVEDEKKKL------QKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKK 2571
Cdd:PRK03918 503 EQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 2572 QKEAEAEMKNKQKEMEALEKKRLE----------QEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2629
Cdd:PRK03918 583 GFESVEELEERLKELEPFYNEYLElkdaekelerEEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1807-2634 |
5.81e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 92.16 E-value: 5.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1807 EKSKQLLETEALKMKQLAEEAARlrSVAEEAKKQRQLAEDEAarqraeaekILKEKLAAINEATRLKTEAEVALKAKEAE 1886
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAES--ELKELEKKHQQLCEEKN---------ALQEQLQAETELCAEAEEMRARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1887 NERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELD-RQKNIVEETLRQKKV--VEEEIHIIRINFERASK 1963
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAaRQKLQLEKVTTEAKIkkLEEDILLLEDQNSKLSK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1964 EKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAA 2043
Cdd:pfam01576 153 ERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2044 EANKLKDKAEKELEK-QVILAKEAAQKSTAAEQ--KAQDVLSKNKEDLLSQEKLRDEFENAKK--------LAQAAETAK 2112
Cdd:pfam01576 233 ELRAQLAKKEEELQAaLARLEEETAQKNNALKKirELEAQISELQEDLESERAARNKAEKQRRdlgeeleaLKTELEDTL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2113 EKAEKEAALLRQKAEEAEKLKKAAEDEAakqakaqKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEqa 2192
Cdd:pfam01576 313 DTTAAQQELRSKREQEVTELKKALEEET-------RSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALE-- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2193 lKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRL--- 2269
Cdd:pfam01576 384 -SENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLskd 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2270 ---MQKNKDNTQKLLAEE-------AEKMKSLAEEAARLSVEAEETA-------RQRKTAEAELAEQRALAEKMLkEKMQ 2332
Cdd:pfam01576 463 vssLESQLQDTQELLQEEtrqklnlSTRLRQLEDERNSLQEQLEEEEeakrnveRQLSTLQAQLSDMKKKLEEDA-GTLE 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2333 AIQEATK-LKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKET--QGFQK----SLEAERKRQLEISAEAEKLKLR-V 2404
Cdd:pfam01576 542 ALEEGKKrLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdLDHQRqlvsNLEKKQKKFDQMLAEEKAISARyA 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2405 KELSSAQAKAEEEATRF---KKQADEAKVRLQETEKQTTEtvvQKLETQRLQSTReaDDLKKAIAELEKEREKLKRDAQE 2481
Cdd:pfam01576 622 EERDRAEAEAREKETRAlslARALEEALEAKEELERTNKQ---LRAEMEDLVSSK--DDVGKNVHELERSKRALEQQVEE 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2482 LQNKSKETASAQQE----------QMEQQKAMLQQTFLTEKE-------LLLKRERDVEDE--------------KKKLQ 2530
Cdd:pfam01576 697 MKTQLEELEDELQAtedaklrlevNMQALKAQFERDLQARDEqgeekrrQLVKQVRELEAElederkqraqavaaKKKLE 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2531 ---KHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLE-QEKLLADENKK 2606
Cdd:pfam01576 777 ldlKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQlQEDLAASERAR 856
|
890 900
....*....|....*....|....*...
gi 1655220527 2607 LREKLESLEVTSKQAASKTKEIEVQTDK 2634
Cdd:pfam01576 857 RQAQQERDELADEIASGASGKSALQDEK 884
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1545-2651 |
7.67e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 91.78 E-value: 7.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1545 RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLkkeq 1624
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEIL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1625 gtvlqlqEEAEKLRKQEEEANKAREQAEKELETWRLKANEALrlrlrAEEEAQRKSLaqeEAEKQKTEAERDAKKKAKAE 1704
Cdd:pfam01576 78 -------HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQL-----DEEEAARQKL---QLEKVTTEAKIKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1705 EAALKQKENAEKELEKQRtfaeqIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNA---AEKQRRQLEDEL 1781
Cdd:pfam01576 143 LEDQNSKLSKERKLLEER-----ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGrqeLEKAKRKLEGES 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1782 AKVRSEMdalLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEE----AKKQRQLAEDEAARQRAEAEK 1857
Cdd:pfam01576 218 TDLQEQI---AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELeaqiSELQEDLESERAARNKAEKQR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1858 I-LKEKLAAineatrLKTEAEVALKAKEAENE-RLKRQAEDEAYQrKLLEDQAAQHKHDIQEkITQLQSSSVSELDRQkn 1935
Cdd:pfam01576 295 RdLGEELEA------LKTELEDTLDTTAAQQElRSKREQEVTELK-KALEEETRSHEAQLQE-MRQKHTQALEELTEQ-- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1936 iVEETLRQKKVVEEEIHIIRinferasKEKSDLEVELKKLKGIADETQKskakaeeeaeklkklaaeeerKRREAEEKVK 2015
Cdd:pfam01576 365 -LEQAKRNKANLEKAKQALE-------SENAELQAELRTLQQAKQDSEH---------------------KRKKLEGQLQ 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2016 KIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKqviLAKEAAQkstaAEQKAQDVLSknkedlLSQEKLR 2095
Cdd:pfam01576 416 ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK---LSKDVSS----LESQLQDTQE------LLQEETR 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2096 DEFENAKKlaqaaetakekaekeaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLrkeaeaeaakraAAEAAALKQK 2175
Cdd:pfam01576 483 QKLNLSTR------------------LRQLEDERNSLQEQLEEEEEAKRNVERQLSTL------------QAQLSDMKKK 532
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2176 QEADAEMakhkkeAEQALKQKSQVEKELGLVKLQLDEtdkqKALMDEELQrvkaqvndavKQKAQVENELSKVKMQMDEL 2255
Cdd:pfam01576 533 LEEDAGT------LEALEEGKKRLQRELEALTQQLEE----KAAAYDKLE----------KTKNRLQQELDDLLVDLDHQ 592
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2256 LKLKvrieeENLRLMQKNKDntqKLLAEEAEKMKSLAEEAARlsveAEETARQRKTAEAELAeqRALAEkmLKEKMQAIQ 2335
Cdd:pfam01576 593 RQLV-----SNLEKKQKKFD---QMLAEEKAISARYAEERDR----AEAEAREKETRALSLA--RALEE--ALEAKEELE 656
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2336 EATK-LKAEAEELQKQKNQAQ------EKAKKLLEDK-QEIQQRLDKETQGFQKSLEAerKRQLEISAEAEKLKLRvKEL 2407
Cdd:pfam01576 657 RTNKqLRAEMEDLVSSKDDVGknvhelERSKRALEQQvEEMKTQLEELEDELQATEDA--KLRLEVNMQALKAQFE-RDL 733
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2408 SSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVV--QKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNK 2485
Cdd:pfam01576 734 QARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAakKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRE 813
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2486 SKETASAQQEQMEQQKAMLQQTFLTEKELLLKRE---------RDVEDEKKKLQKHLEDEVNKAKALKDEQQR---QQKL 2553
Cdd:pfam01576 814 LEEARASRDEILAQSKESEKKLKNLEAELLQLQEdlaaserarRQAQQERDELADEIASGASGKSALQDEKRRleaRIAQ 893
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2554 MDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEA---LEKKRLEQEKLLADENKKLREKLESLE--VTSKQAAS----- 2623
Cdd:pfam01576 894 LEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAersTSQKSESARQQLERQNKELKAKLQEMEgtVKSKFKSSiaale 973
|
1130 1140
....*....|....*....|....*....
gi 1655220527 2624 -KTKEIEVQTDKVPEEQLVSMTTVETTKK 2651
Cdd:pfam01576 974 aKIAQLEEQLEQESRERQAANKLVRRTEK 1002
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
37-149 |
1.09e-17 |
|
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: 81.47 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 37 QKKTFTKWVNKHLMKA--QRHITDLYEDLRDGHNLISLLEVLSGETLPRerdlvrnvrlPREKGRMRFHKLQNVQIALDF 114
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPG----------IHSRPKTRAQKLENIQACLQF 70
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220527 115 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21212 71 LAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
166-269 |
1.17e-17 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 81.63 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 166 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 245
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1655220527 246 VDV--AHPDEKSIITYVSSLYDVMPR 269
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1617-2495 |
1.39e-17 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 91.43 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1617 EESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEAlrlrlraeeeaqRKSLAQEEAEKQKTEAERD 1696
Cdd:NF041483 7 QESHRADDDHLSRFEAEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEA------------RRSLASRPAYDGADIGYQA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1697 AKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQqklsaeqeyirlkadfEHAEQQrglldnelQRLKNEVNAAEKQRRQ 1776
Cdd:NF041483 75 EQLLRNAQIQADQLRADAERELRDARAQTQRILQ----------------EHAEHQ--------ARLQAELHTEAVQRRQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1777 -LEDELAKVRSEMDALLQMKIQ-AEKVSQSNTEKSKQLL-ETEALKMKQLAEEAARLRSVAEEAkKQRQLAEDEAArqRA 1853
Cdd:NF041483 131 qLDQELAERRQTVESHVNENVAwAEQLRARTESQARRLLdESRAEAEQALAAARAEAERLAEEA-RQRLGSEAESA--RA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1854 EAEKILKeklaaineatRLKTEAEVALKAKEAENERLKRQAEdeayqrklledqaaqhkhdiqekitQLQSSSVSELDRQ 1933
Cdd:NF041483 208 EAEAILR----------RARKDAERLLNAASTQAQEATDHAE-------------------------QLRSSTAAESDQA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1934 KNIVEETLRQkkvveeeihiirinferASKEKSDLEVELKKLKGIADETqkskakaeeeaeklkklaaeeerKRREAEEK 2013
Cdd:NF041483 253 RRQAAELSRA-----------------AEQRMQEAEEALREARAEAEKV-----------------------VAEAKEAA 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2014 VKKIAAAEEEAARQRKAAQDEVERLKQKA--------AEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQ------- 2078
Cdd:NF041483 293 AKQLASAESANEQRTRTAKEEIARLVGEAtkeaealkAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQlakaart 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2079 --DVLSKNKEDllSQEKLRDEFENAKKLAQaaetakEKAEKEAALLRQKAEEAEKLKKAAEDEA----AKQAKAQKDAER 2152
Cdd:NF041483 373 aeEVLTKASED--AKATTRAAAEEAERIRR------EAEAEADRLRGEAADQAEQLKGAAKDDTkeyrAKTVELQEEARR 444
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2153 LrkeaeaeaakraAAEAAALKQKQEADAEM--AKHKKEAEQALKQKSQVEKELgLVKLQLDETD-KQKALMDEELQRVKA 2229
Cdd:NF041483 445 L------------RGEAEQLRAEAVAEGERirGEARREAVQQIEEAARTAEEL-LTKAKADADElRSTATAESERVRTEA 511
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2230 qVNDAVKQKAQVENELSKVKMQMDELlklkvRIE-EENLRLMQKNKDNTQKLLAEEAE-----KMKSLAEEAARLSVEAE 2303
Cdd:NF041483 512 -IERATTLRRQAEETLERTRAEAERL-----RAEaEEQAEEVRAAAERAARELREETEraiaaRQAEAAEELTRLHTEAE 585
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2304 EtarQRKTAEAELAEQRALAEKMLKEkmqAIQEATKLKAE-AEELQKQKNQAQEKAKKLledkqeiqqRLDKETQGFQKS 2382
Cdd:NF041483 586 E---RLTAAEEALADARAEAERIRRE---AAEETERLRTEaAERIRTLQAQAEQEAERL---------RTEAAADASAAR 650
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2383 LEAE----RKRQlEISAEAEKLKlrvkelssaqAKAEEEATRFKKQADEAKVRLqETEKQTTETVVQKLETQRlqsTREA 2458
Cdd:NF041483 651 AEGEnvavRLRS-EAAAEAERLK----------SEAQESADRVRAEAAAAAERV-GTEAAEALAAAQEEAARR---RREA 715
|
890 900 910
....*....|....*....|....*....|....*....
gi 1655220527 2459 DD-LKKAIAELEKEREKLKRDAQE-LQNKSKETASAQQE 2495
Cdd:NF041483 716 EEtLGSARAEADQERERAREQSEElLASARKRVEEAQAE 754
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1632-2486 |
1.39e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 91.28 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1632 EEAEKLRKQEEEANKAREQAEKELETWRLKANEALR---LRLRAEE-EAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAA 1707
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqaLLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1708 LKQKENAEKELEKQRTFAEQIAQQ-KLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRS 1786
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1787 EMDALlQMKIQAEKVSQ-SNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAED----------------EAA 1849
Cdd:TIGR02169 337 EIEEL-EREIEEERKRRdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkreinelkreldrlqEEL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1850 RQRAEAEKILKEKLAAINEA-TRLKTEAEVALKAKEAENERLKRQAED-EAYQRKLLEDQAAQHKhdIQEKITQLQSSsV 1927
Cdd:TIGR02169 416 QRLSEELADLNAAIAGIEAKiNELEEEKEDKALEIKKQEWKLEQLAADlSKYEQELYDLKEEYDR--VEKELSKLQRE-L 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1928 SELDRQKNIVEETLRQKKVVEEEI------------HIIRInferasKEKSDLEVEL---KKLKGIADETQ--------- 1983
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLkasiqgvhgtvaQLGSV------GERYATAIEVaagNRLNNVVVEDDavakeaiel 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1984 -KSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVER---LKQKAAEANKLKDKAekeleKQ 2059
Cdd:TIGR02169 567 lKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGdtlVVEDIEAARRLMGKY-----RM 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2060 VILAKEAAQKS---TAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAA 2136
Cdd:TIGR02169 642 VTLEGELFEKSgamTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2137 EDEAAK-QAKAQKDAERLRKEAEAEAAkraaaeaaaLKQKQEA-DAEMAKHKKEAEqalkqksqvEKELGLVKLQLDETD 2214
Cdd:TIGR02169 722 EKEIEQlEQEEEKLKERLEELEEDLSS---------LEQEIENvKSELKELEARIE---------ELEEDLHKLEEALND 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2215 KQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEEnlrlmqknKDNTQKLLAEEAEKMKSLAEE 2294
Cdd:TIGR02169 784 LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE--------IQELQEQRIDLKEQIKSIEKE 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2295 AARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLdk 2374
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-- 933
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2375 etqgfqKSLEAERKRQLEISAE---AEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQEtekqttetvvqkLETQR 2451
Cdd:TIGR02169 934 ------SEIEDPKGEDEEIPEEelsLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDE------------LKEKR 995
|
890 900 910
....*....|....*....|....*....|....*
gi 1655220527 2452 LQSTREADDLKKAIAELEKEREKLKRDAQELQNKS 2486
Cdd:TIGR02169 996 AKLEEERKAILERIEEYEKKKREVFMEAFEAINEN 1030
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
166-265 |
1.91e-17 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 80.78 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 166 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 245
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1655220527 246 VDVA--HPDEKSIITYVSSLYD 265
Cdd:cd21261 83 MMVMgrKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
166-264 |
4.33e-17 |
|
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: 80.13 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 166 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 245
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1655220527 246 -VDVAHPDEKSIITYVSSLY 264
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
168-266 |
1.05e-16 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 78.77 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 168 KLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPEDVD 247
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMA 87
|
90 100
....*....|....*....|
gi 1655220527 248 VAH-PDEKSIITYVSSLYDV 266
Cdd:cd21250 88 SAEePDKLSMVMYLSKFYEL 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2035-2644 |
1.92e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.42 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2035 VERLKQKAAEANKLKDK--AEKELEKQVILA--------KEAAQKSTAAEQKAQDVLSKNKEDLLSQ-EKLRDEFENAKK 2103
Cdd:TIGR02168 202 LKSLERQAEKAERYKELkaELRELELALLVLrleelreeLEELQEELKEAEEELEELTAELQELEEKlEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2104 LAQAAETAkekaekeaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAakraaaeaaalKQKQEADAEMA 2183
Cdd:TIGR02168 282 EIEELQKE----------LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE-----------SKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2184 KHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSkvkmqmdELLKLKVRIE 2263
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE-------RLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2264 EENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAE 2343
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2344 AEELQKQKNQAQEKAKKLLEDKQEIQQRLD------KETQGFQKSLEA---------------ERKRQLEISAEAEKLKL 2402
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGLSGILGvlseliSVDEGYEAAIEAalggrlqavvvenlnAAKKAIAFLKQNELGRV 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2403 RVKELSSAQAKAEEEATRFKKQADEAKVRLQeTEKQTTETVVQKLETQRLQSTREADDL--------------------- 2461
Cdd:TIGR02168 574 TFLPLDSIKGTEIQGNDREILKNIEGFLGVA-KDLVKFDPKLRKALSYLLGGVLVVDDLdnalelakklrpgyrivtldg 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2462 -----------------------KKAIAELEKEREKLKRDAQELQNKSKEtASAQQEQMEQQKAMLQQTFLTEKELLLKR 2518
Cdd:TIGR02168 653 dlvrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISAL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2519 ERDVEDEKKKLQKhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEK 2598
Cdd:TIGR02168 732 RKDLARLEAEVEQ-LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1655220527 2599 LLADENKKLREKLESLEVTSKQAASKTKEIEV--QTDKVPEEQLVSMT 2644
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDleEQIEELSEDIESLA 858
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1710-2595 |
2.93e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 86.66 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1710 QKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLL----DNELQRLKNEVNAAEKQRRQLEDELAKVR 1785
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1786 SEMDallQMKIQAEKVSQSNTEKsKQLLETEALKMKQLAEEaarlrsvaEEAKKQRQLAEDEAarQRAEAEKILKEKLAA 1865
Cdd:TIGR02169 251 EELE---KLTEEISELEKRLEEI-EQLLEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1866 INEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVS------ELDRQKNIVEE 1939
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaetrdELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1940 TLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQkskakaeeeaeklkklaaeeeRKRREAEEKVKKIAA 2019
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE---------------------EEKEDKALEIKKQEW 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2020 AEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEkQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQeklrdefe 2099
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVHGT-------- 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2100 nakkLAQaaetakekaekeaaLLRQKAEEAEKLKKAA----------EDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEA 2169
Cdd:TIGR02169 527 ----VAQ--------------LGSVGERYATAIEVAAgnrlnnvvveDDAVAKEAIELLKRRKAGRATFLPLNKMRDERR 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2170 AALKQKQEADAEMAKHKKEAEQALKQK-SQVEKELGLVklqlDETDKQKALMD---------EELQRVKAQVNDAVKQKA 2239
Cdd:TIGR02169 589 DLSILSEDGVIGFAVDLVEFDPKYEPAfKYVFGDTLVV----EDIEAARRLMGkyrmvtlegELFEKSGAMTGGSRAPRG 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2240 QVENELSkvkmQMDELLKLKVRIEEenlrlMQKNKDNtqklLAEEAEKMKSLAEEA-ARLSVEAEETARQRKTAEAELAE 2318
Cdd:TIGR02169 665 GILFSRS----EPAELQRLRERLEG-----LKRELSS----LQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQE 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2319 QRALAEKM--LKEKMQAIQEA-TKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLD----KETQGFQKSLEAERKRQL 2391
Cdd:TIGR02169 732 EEKLKERLeeLEEDLSSLEQEiENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIE 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2392 EISAEAEKlklRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRlqstrEADDLKKAIAELEKE 2471
Cdd:TIGR02169 812 ARLREIEQ---KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE-----ELEELEAALRDLESR 883
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2472 REKLKRDAQELQNKSKETASAQQEQMEQ--QKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQR 2549
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQieKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRV 963
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 2550 QQKLMD---------EEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLE 2595
Cdd:TIGR02169 964 EEEIRAlepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2267-2632 |
2.95e-16 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 86.33 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2267 LRLMQKNKDNTQKLLAEEAEKMkslaeEAARLSVEAEETARQ----RKTAEAELAEQRALaekmlkEKMQAIQeatklkA 2342
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKM-----EQERLRQEKEEKAREverrRKLEEAEKARQAEM------DRQAAIY------A 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2343 EAEELqkqknqAQEKAKKLLEDKQEIQQRldketqgfqkslEAERKRQLEISAEAEklklRVKELSSAQAKAEEEATRFK 2422
Cdd:pfam17380 338 EQERM------AMERERELERIRQEERKR------------ELERIRQEEIAMEIS----RMRELERLQMERQQKNERVR 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2423 KQADEA-KVRLQETEKQtTETVVQKLETQRLQSTREaDDLKKAIAELEKEREK-LKRDAQELQNKSKETASAQQEQMEQQ 2500
Cdd:pfam17380 396 QELEAArKVKILEEERQ-RKIQQQKVEMEQIRAEQE-EARQREVRRLEEERAReMERVRLEEQERQQQVERLRQQEEERK 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2501 KAMLQQtfltEKElllKRERDVEDEKKKlqKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQ-AIMDEavKKQKEAEAEm 2579
Cdd:pfam17380 474 RKKLEL----EKE---KRDRKRAEEQRR--KILEKELEERKQAMIEEERKRKLLEKEMEERQkAIYEE--ERRREAEEE- 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 2580 KNKQKEMEalEKKRLEQEKLLADENkklREKLESLEVTS------KQAASKTKEIEVQT 2632
Cdd:pfam17380 542 RRKQQEME--ERRRIQEQMRKATEE---RSRLEAMERERemmrqiVESEKARAEYEATT 595
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
38-147 |
3.80e-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: 76.99 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 38 KKTFTKWVNKHL-MKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRErdlvrnvrlpREKGRMRFHKLQNVQIALDFLK 116
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKI----------NKKPKSPFKKRENINLFLNACK 70
|
90 100 110
....*....|....*....|....*....|...
gi 1655220527 117 HRQV-KLVNIRNDDI-ADGNPKLTLGLIWTIIL 147
Cdd:cd00014 71 KLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
169-264 |
6.43e-16 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 76.63 E-value: 6.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 169 LLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDPED-VD 247
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1655220527 248 VAHPDEKSIITYVSSLY 264
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1249-1791 |
6.62e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.50 E-value: 6.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1249 LREARLRQEKIEAApVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEfqilayRALQDPIASPLKK 1328
Cdd:PRK03918 216 LPELREELEKLEKE-VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI------EELEEKVKELKEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1329 PKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRmAEIQAQLETQKQLAEGHAKS 1408
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-KELEKRLEELEERHELYEEA 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1409 VAKAElEAQELKLKMKEDASQR-QGLAVDAEKQKQNIQLE---LTQLKNLSEQEIRSKNQQLEEAQVSRRKLeeeihlir 1484
Cdd:PRK03918 368 KAKKE-ELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEiskITARIGELKKEIKELKKAIEELKKAKGKC-------- 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1485 iqlqTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEetqkKKNAEDELKRKSE--AEKEAARQKQKALD 1562
Cdd:PRK03918 439 ----PVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKE----LRELEKVLKKESEliKLKELAEQLKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1563 ELQKHkmQAEEAERRLKQAEEEKVRQIKVVEEVaqktaatqlqamsfsektTKLEESLKKEQGTVLQLQEEAEKLRKQEE 1642
Cdd:PRK03918 511 KLKKY--NLEELEKKAEEYEKLKEKLIKLKGEI------------------KSLKKELEKLEELKKKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1643 EankaREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEK-- 1720
Cdd:PRK03918 571 E----LAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEElr 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1721 ------QRTFAEQ----IAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDeLAKVRSEMDA 1790
Cdd:PRK03918 647 keleelEKKYSEEeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEE 725
|
.
gi 1655220527 1791 L 1791
Cdd:PRK03918 726 L 726
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
34-145 |
7.66e-16 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 76.42 E-value: 7.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 34 DRVQKKTFTKWVNKHLMKAQ-RHITDLYEDLRDGHNLISLLEVLSGETLPRERDLvrnvrlpreKGRMRFHKLQNVQIAL 112
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDL---------EPKNRIQMIQNLHLAM 72
|
90 100 110
....*....|....*....|....*....|....
gi 1655220527 113 DFL-KHRQVKLVNIRNDDIADGNPKLTLGLIWTI 145
Cdd:cd21225 73 LFIeEDLKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2190-2607 |
1.04e-15 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 84.77 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2190 EQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDEL---LKLKVRIEEEN 2266
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVvteFEATTCSLEEL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2267 LRLMQKNKDNTQkllaeeaEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRalaeKMLKEKMQAIQEATKLKAEAEE 2346
Cdd:pfam05483 365 LRTEQQRLEKNE-------DQLKIITMELQKKSSELEEMTKFKNNKEVELEELK----KILAEDEKLLDEKKQFEKIAEE 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2347 LQKQKN------QAQEKAKKLLEDKQEI----QQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSA------ 2410
Cdd:pfam05483 434 LKGKEQelifllQAREKEIHDLEIQLTAiktsEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEasdmtl 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2411 QAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEK-----EREKLKRDAQ----- 2480
Cdd:pfam05483 514 ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEnarsiEYEVLKKEKQmkile 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2481 --------ELQNKSKETASAQQEQME-QQKAMLQQTFLTEKELLL-KRERDVEDEKKKLQKHLEdevNKAKALKDEQQRQ 2550
Cdd:pfam05483 594 nkcnnlkkQIENKNKNIEELHQENKAlKKKGSAENKQLNAYEIKVnKLELELASAKQKFEEIID---NYQKEIEDKKISE 670
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 2551 QKLMdEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEAL-EKKRLEQEKLLADENKKL 2607
Cdd:pfam05483 671 EKLL-EEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALmEKHKHQYDKIIEERDSEL 727
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1449-1981 |
1.11e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.71 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1449 TQLKNLSEqEIRSKNQQLEEAQVSRRKLEE--EIHLIRIQLQTTIKQkstaddELQKLRDQAAEAEKVRKAAQEEAERLR 1526
Cdd:PRK02224 213 SELAELDE-EIERYEEQREQARETRDEADEvlEEHEERREELETLEA------EIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1527 KQVNEETQKKKNAEDELKRkSEAEKEAARQKQKALDElqkhkmQAEEAERRLkqaeeekvrqikvvEEVAQKTAATQLQA 1606
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGL-DDADAEAVEARREELED------RDEELRDRL--------------EECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1607 MSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEaqRKSLAQEEA 1686
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF--LEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1687 EKQKTEAERDAKKkakaeeaalkqkENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNE 1766
Cdd:PRK02224 423 ELREREAELEATL------------RTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1767 VNAAEKQRRQLEDeLAKVRSEMDALLQmkiQAEKVSQSNTEKsKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAED 1846
Cdd:PRK02224 491 VEEVEERLERAED-LVEAEDRIERLEE---RREDLEELIAER-RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1847 EAARQRAEAeKILKEKLAAINEA-TRLKTEAEVALKAKEAE------NERLKRQAEdeayqrklLEDQAAQHKHDIQEKI 1919
Cdd:PRK02224 566 EAEEAREEV-AELNSKLAELKERiESLERIRTLLAAIADAEdeierlREKREALAE--------LNDERRERLAEKRERK 636
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 1920 TQLQS----SSVSELDRQKNIVEETLRQkkvVEEEIHIIRINFERASKEKSDLEVELKKLKGIADE 1981
Cdd:PRK02224 637 RELEAefdeARIEEAREDKERAEEYLEQ---VEEKLDELREERDDLQAEIGAVENELEELEELRER 699
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1772-2609 |
1.23e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.73 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1772 KQRRQLEDELAKVrSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQ 1851
Cdd:TIGR02169 153 VERRKIIDEIAGV-AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1852 RAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQ-RKLLEDQAAQHKHDIQE---KITQLQSSsV 1927
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGEleaEIASLERS-I 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1928 SELDRQKNIVEETLRQkkvVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKR 2007
Cdd:TIGR02169 311 AEKERELEDAEERLAK---LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2008 REAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEA-NKLKDKAEKELEKQVILaKEAAQKSTAAEQKaqdvLSKNKE 2086
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLnAAIAGIEAKINELEEEK-EDKALEIKKQEWK----LEQLAA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2087 DLlsqEKLRDEFENAKKLAQAAETAKEKaekeaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAE-----------RLRK 2155
Cdd:TIGR02169 463 DL---SKYEQELYDLKEEYDRVEKELSK-------LQRELAEAEAQARASEERVRGGRAVEEVLKasiqgvhgtvaQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2156 EAEAEAAKRAAAEAAALKQKQEADAEMAkhkKEAEQALKQ-KSQVEKELGLVKLQLDETDKQKALMDE------ELQRVK 2228
Cdd:TIGR02169 533 VGERYATAIEVAAGNRLNNVVVEDDAVA---KEAIELLKRrKAGRATFLPLNKMRDERRDLSILSEDGvigfavDLVEFD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2229 AQVNDAVKQKAQ---VENELSKVKMQMDEL-------------------------LKLKVRIEEENLRLMQKNKDNTQKL 2280
Cdd:TIGR02169 610 PKYEPAFKYVFGdtlVVEDIEAARRLMGKYrmvtlegelfeksgamtggsraprgGILFSRSEPAELQRLRERLEGLKRE 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2281 LA---EEAEKMKSLAEEA-ARLSVEAEETARQRKTAEAELAEQRALAEKM--LKEKMQAIQEA-TKLKAEAEELQKQKNQ 2353
Cdd:TIGR02169 690 LSslqSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQEEEKLKERLeeLEEDLSSLEQEiENVKSELKELEARIEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2354 AQEKAKKLLEDKQEIQQRLD----KETQGFQKSLEAERKRQLEISAEAEKlklRVKELSSAQAKAEEEATRFKKQADEAK 2429
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARLREIEQ---KLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2430 VRLQETEKQTTETVVQKLETQrlqstREADDLKKAIAELEKEREKLKRDAQELQNKSKEtasaQQEQMEQQKAMLQQTFL 2509
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELE-----EELEELEAALRDLESRLGDLKKERDELEAQLRE----LERKIEELEAQIEKKRK 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2510 TEKELLLKRErDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKL--MDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEME 2587
Cdd:TIGR02169 918 RLSELKAKLE-ALEEELSEIEDPKGEDEEIPEEELSLEDVQAELqrVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRA 996
|
890 900
....*....|....*....|..
gi 1655220527 2588 ALEKKRLEQEKLLADENKKLRE 2609
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKKKRE 1018
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2186-2628 |
3.11e-15 |
|
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: 83.15 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2186 KKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKV----R 2261
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2262 IEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLK 2341
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2342 AEAEELQKQknqaqekakklLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELssaqakaEEEATRF 2421
Cdd:TIGR04523 391 SQINDLESK-----------IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL-------TNQDSVK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2422 KKQADEAKVRLQETEKQTTETvvqKLETQRLQSTREadDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQK 2501
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVL---SRSINKIKQNLE--QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2502 AMlqQTFLTEKELLLKrerDVEDEKKKLQKHLEDEvnKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKN 2581
Cdd:TIGR04523 528 KL--ESEKKEKESKIS---DLEDELNKDDFELKKE--NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1655220527 2582 KQKEMEALEKKRLEQEKLLADENKKlREKLESLEVTSKQAASKTKEI 2628
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQE 646
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1352-2252 |
3.35e-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: 83.30 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1352 LSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKK----------RMAEIQAQLETQK-QLA---------------EGH 1405
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegestdlqeQIAELQAQIAELRaQLAkkeeelqaalarleeETA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1406 AKSVA-KAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSE---------QEIRSKNQQleEAQVSRRK 1475
Cdd:pfam01576 258 QKNNAlKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdtldttaaqQELRSKREQ--EVTELKKA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1476 LEEEIHLIRIQLQTTIKQKSTADDELQKLRDQA----AEAEKVRKAAQEEAERLRKQVN-------EETQKKKNAEDELK 1544
Cdd:pfam01576 336 LEEETRSHEAQLQEMRQKHTQALEELTEQLEQAkrnkANLEKAKQALESENAELQAELRtlqqakqDSEHKRKKLEGQLQ 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1545 RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSfsEKTTKLEESLKkeq 1624
Cdd:pfam01576 416 ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE--ETRQKLNLSTR--- 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1625 gtVLQLQEEAEKLRKQEEEANKAREQAEKELETWR----------------LKANEALRLRLRAEEEAQRKSLAQEEAEK 1688
Cdd:pfam01576 491 --LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQaqlsdmkkkleedagtLEALEEGKKRLQRELEALTQQLEEKAAAY 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1689 QKTEA--ERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQ---EYIRLKADFEHAEQQRGLLDNELQRL 1763
Cdd:pfam01576 569 DKLEKtkNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARyaeERDRAEAEAREKETRALSLARALEEA 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1764 KNEVNAAEKQRRQLedelakvRSEMDALLQMKIQAEKvSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKkqrql 1843
Cdd:pfam01576 649 LEAKEELERTNKQL-------RAEMEDLVSSKDDVGK-NVHELERSKRALEQQVEEMKTQLEELEDELQATEDAK----- 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1844 aedeaarqraeaekilkeklaaineaTRLkteaEVALKAKEAENERlKRQAEDEayqrklledQAAQHKHDIQEKITQLQ 1923
Cdd:pfam01576 716 --------------------------LRL----EVNMQALKAQFER-DLQARDE---------QGEEKRRQLVKQVRELE 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1924 SssvsELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEE 2003
Cdd:pfam01576 756 A----ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKES 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2004 ERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKlkDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSK 2083
Cdd:pfam01576 832 EKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGAS--GKSALQDEKRRLEARIAQLEEELEEEQSNTELLN 909
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2084 NKEDLLSQ--EKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDE--AAKQAKAQKDAERLRKEAEA 2159
Cdd:pfam01576 910 DRLRKSTLqvEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSsiAALEAKIAQLEEQLEQESRE 989
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2160 EAAKRAAAEAAALKQKqEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKA 2239
Cdd:pfam01576 990 RQAANKLVRRTEKKLK-EVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNE 1068
|
970
....*....|...
gi 1655220527 2240 QVENELSKVKMQM 2252
Cdd:pfam01576 1069 SMNREVSTLKSKL 1081
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1149-1984 |
3.35e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 83.48 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1149 KEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEhyrqlagSLLERWQAVFAQIDLRQREL 1228
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK-------LQEEELKLLAKEEEELKSEL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1229 SLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLTQEKKLLEEIEKNKDQiencqkdakayidslkdy 1308
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL------------------ 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1309 efQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRyselstlTSQYIKFILETQRRLEDDEKaseklkeDEKKRM 1388
Cdd:pfam02463 365 --QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE-------EEKEAQLLLELARQLEDLLK-------EEKKEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1389 AEIQAQLETQKQLAEGHAKSVaKAELEAQELKLKMKEdasqrqglavDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEE 1468
Cdd:pfam02463 429 LEILEEEEESIELKQGKLTEE-KEELEKQELKLLKDE----------LELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1469 AQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSE 1548
Cdd:pfam02463 498 RSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGA 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1549 AEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGtvl 1628
Cdd:pfam02463 578 RKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL--- 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1629 qLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAAL 1708
Cdd:pfam02463 655 -EEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1709 KQKENAEKELEKQRTFAEQ--IAQQKLSAEQEYIRLKADFEHAEQQRglldNELQRLKNEVNAAEKQRRQLEDELAKVRS 1786
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEEekSRLKKEEKEEEKSELSLKEKELAEER----EKTEKLKVEEEKEEKLKAQEEELRALEEE 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1787 EMDALLQMKIQAEKVSQSN---TEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKL 1863
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEkikEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1864 AAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSsvseldrQKNIVEETLRQ 1943
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKE-------ENNKEEEEERN 962
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 1655220527 1944 KKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQK 1984
Cdd:pfam02463 963 KRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4062-4100 |
3.81e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.59 E-value: 3.81e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1655220527 4062 LLEAQIATGGIIDPQESHRLPVETAYERGLFDEEMNQIL 4100
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2174-2629 |
4.27e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.78 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2174 QKQEADAEMAKHkkeaEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQV-------NDAVKQKAQVENELS 2246
Cdd:PRK02224 235 TRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLeeleeerDDLLAEAGLDDADAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2247 KVKMQMDELLKLKVRIEE--ENLRLMQKNKDNTQKLLAEEAEKMKSLA----EEAARLSVEAEETARQRKTAEAELAEQR 2320
Cdd:PRK02224 311 AVEARREELEDRDEELRDrlEECRVAAQAHNEEAESLREDADDLEERAeelrEEAAELESELEEAREAVEDRREEIEELE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2321 ALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKL 2400
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETI 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2401 ---KLRVKELSSAQAKAEEEATRFKKQADEAKvRLQETEKQttetvVQKLETQRLQSTREADDLKKAIAELEKEREKLKR 2477
Cdd:PRK02224 471 eedRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDR-----IERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2478 DAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELL-LKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDE 2556
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAeLKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDE 624
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 2557 EKKKLQAimdeavKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2629
Cdd:PRK02224 625 RRERLAE------KRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE 691
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1345-2273 |
4.27e-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: 83.17 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1345 LRTRYSELSTLTsQYIKfILETQRRLEDDEK-------ASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQ 1417
Cdd:TIGR00606 171 LKQKFDEIFSAT-RYIK-ALETLRQVRQTQGqkvqehqMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1418 ELKLKMKEDASQRQGLavdaekqkQNIQLELTQLKNlSEQEIRSKNQQLEEAQVS-RRKLEEEIHLIRIQLQTTIKQKSt 1496
Cdd:TIGR00606 249 PLKNRLKEIEHNLSKI--------MKLDNEIKALKS-RKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKE- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1497 addelQKLRDQAAEAEKVRKAA----QEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAE 1572
Cdd:TIGR00606 319 -----RELVDCQRELEKLNKERrllnQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1573 EAERRLKQAEEEKVRQI-KVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQA 1651
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAaQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1652 EKELETWRlkanEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAeeaalkqKENAEKELEKQ-RTFAEQIAQ 1730
Cdd:TIGR00606 474 LELDQELR----KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLD-------QEMEQLNHHTTtRTQMEMLTK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1731 QKLSAEQEYIRLKAdfEHAEQQRGLLDN--ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEK 1808
Cdd:TIGR00606 543 DKMDKDEQIRKIKS--RHSDELTSLLGYfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQ 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1809 SKQLLET--EALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATR-LKTEAEVALKAKEA 1885
Cdd:TIGR00606 621 LSSYEDKlfDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvFQTEAELQEFISDL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1886 ENERLKRQAEDEAYQRKLLEDQAAQH----KHDIQEKITQLQSSSVSEL-DRQKNIVEETLRQKKVVEE-EIHIIRINFE 1959
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDemlgLAPGRQSIIDLKEKEIPELrNKLQKVNRDIQRLKNDIEEqETLLGTIMPE 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1960 RASKEksDLEVELKKLKGIADETQKSKAKAEEEAEKL-----KKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDE 2034
Cdd:TIGR00606 781 EESAK--VCLTDVTIMERFQMELKDVERKIAQQAAKLqgsdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2035 VERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEK 2114
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2115 AEKEAALLRQKAEEAEKLKKAAEDeaakqaKAQKDAERlrkeaeaeaakraaaeaaalkQKQEADAEMAKHKKEAEQALK 2194
Cdd:TIGR00606 939 AQDKVNDIKEKVKNIHGYMKDIEN------KIQDGKDD---------------------YLKQKETELNTVNAQLEECEK 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2195 QKSQVEKELGLVKLQLDETDKQKALMDEELQRVKaqVNDAVKqkaQVENELSKVKMQMDELLKLKVRIE----EENLRLM 2270
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK--RENELK---EVEEELKQHLKEMGQMQVLQMKQEhqklEENIDLI 1066
|
...
gi 1655220527 2271 QKN 2273
Cdd:TIGR00606 1067 KRN 1069
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
164-264 |
5.17e-15 |
|
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: 74.34 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 243
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1655220527 244 ED-VDVAHPDEKSIITYVSSLY 264
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1797-2533 |
6.70e-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: 82.32 E-value: 6.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1797 QAEKVSQSNTEKSKQLLEtEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEA 1876
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLM-NLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1877 EVALKAKEAENERLKRQAEdEAYQRKLLEDQAAQHKHDIQEKITQLQ--SSSVSELDRQKNIVEETLRQKKVVEEEIHII 1954
Cdd:TIGR00618 232 REALQQTQQSHAYLTQKRE-AQEEQLKKQQLLKQLRARIEELRAQEAvlEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1955 RINFERASKEKSdLEVELKKLKGIAdeTQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDE 2034
Cdd:TIGR00618 311 RIHTELQSKMRS-RAKLLMKRAAHV--KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2035 VERLKQKAAEANKLKDKAEKELEKQvilakEAAQKSTAAEQkaQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEK 2114
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQREQATI-----DTRTSAFRDLQ--GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2115 AEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAaeaaaLKQKQEADAEMAKHKKEAEQALK 2194
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH-----PNPARQDIDNPGPLTRRMQRGEQ 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2195 QKSQVEKELGLVKLQLDETDKQKALMDEELQRVK------AQVNDAVKQKAQ-VENELSKVKMQMDELLKLKVRIEEENL 2267
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQqsfsilTQCDNRSKEDIPnLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2268 RLMQK--NKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQR--------KTAEAELAEQRALAEKMLKEKMQAI--- 2334
Cdd:TIGR00618 616 ALLRKlqPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehalsiRVLPKELLASRQLALQKMQSEKEQLtyw 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2335 -----QEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQgFQKSLEAERKRQLEISAEAEK---LKLRVKE 2406
Cdd:TIGR00618 696 kemlaQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ-SLKELMHQARTVLKARTEAHFnnnEEVTAAL 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2407 LSSAQ-AKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQnK 2485
Cdd:TIGR00618 775 QTGAElSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL-K 853
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1655220527 2486 SKETASAQQEQMEQQKAMLQQtfltEKELLLKRERDVEDEKKKLQKHL 2533
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQL----SDKLNGINQIKIQFDGDALIKFL 897
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1436-1847 |
7.37e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 81.74 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1436 DAEKQKQNIQLELTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEIHLIR--IQLQTTIKQKSTADDELQKLRDQAAEAEK 1513
Cdd:COG4717 75 ELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1514 VRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQ------AEEEKVR 1587
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEeleeleEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1588 QIKVVEEVAQKTAATQLQAMSFS---------------------------EKTTKLEESLKKEQGTVLQLQEEAEKLRKQ 1640
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAAallallglggsllsliltiagvlflvlGLLALLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1641 EEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEK 1720
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1721 QRTFAEqiAQQKLSAEQEYIRLKADFEHAEQQRGLLDN---ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLqmkiq 1797
Cdd:COG4717 394 AEEYQE--LKEELEELEEQLEELLGELEELLEALDEEEleeELEELEEELEELEEELEELREELAELEAELEQLE----- 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1798 aekvSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDE 1847
Cdd:COG4717 467 ----EDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1437-1767 |
8.12e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 81.71 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1437 AEKQKQNiqleltQLKNLSEQEIRSKNQQLEEAQVSRRKLEEeihliriqlqttikQKSTADDELQKLRDQAAEAEKVRK 1516
Cdd:pfam17380 285 SERQQQE------KFEKMEQERLRQEKEEKAREVERRRKLEE--------------AEKARQAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1517 AAQEEAERLRkqvneetQKKKNAEDELKRKSEAEKEAARQKQkaLDELQKHKMQAE-------EAERRLKQAEEEKVRQI 1589
Cdd:pfam17380 345 ERERELERIR-------QEERKRELERIRQEEIAMEISRMRE--LERLQMERQQKNervrqelEAARKVKILEEERQRKI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1590 KVVEEVAQKTAATQLQAMsfSEKTTKLEESLKKEQGTV----LQLQEEAEKLRKQEEEANKAREQAEKELETwRLKANEA 1665
Cdd:pfam17380 416 QQQKVEMEQIRAEQEEAR--QREVRRLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLELEKEKRD-RKRAEEQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1666 LRLRLRAEEEAQRKSLAQEEAEKQKTEAERDakkKAKAEEAALKQKENAEKELEKQRTFAE--QIAQQKLSAEQEYIRLK 1743
Cdd:pfam17380 493 RRKILEKELEERKQAMIEEERKRKLLEKEME---ERQKAIYEEERRREAEEERRKQQEMEErrRIQEQMRKATEERSRLE 569
|
330 340
....*....|....*....|....
gi 1655220527 1744 ADFEHAEQQRGLLDNELQRLKNEV 1767
Cdd:pfam17380 570 AMEREREMMRQIVESEKARAEYEA 593
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1829-2615 |
8.12e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.04 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1829 RLRSVAE-EAKKQRQLAEDEAARQR-AEAEKILKEKlaaINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLED 1906
Cdd:TIGR02169 161 EIAGVAEfDRKKEKALEELEEVEENiERLDLIIDEK---RQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1907 QAAQHKHDIQEKITQLQSSSVSELDRQKNIV-------EETLRQKKVVEEEIHIIRinferasKEKSDLEVELKKLKGIA 1979
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEeieqlleELNKKIKDLGEEEQLRVK-------EKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1980 DETQkskakaeeeaeklkklaaeeerkrreaeEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELekq 2059
Cdd:TIGR02169 311 AEKE----------------------------RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY--- 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2060 vilaKEAAQKSTAAEQKAQDVLSKNKEdllSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDE 2139
Cdd:TIGR02169 360 ----AELKEELEDLRAELEEVDKEFAE---TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2140 AAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQE---ADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQ 2216
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElydLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2217 KALMDEELQRVKAQVNDAVKQKAQ-----------------VENELskVKMQMDELLKL------------KVRIEEENL 2267
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQLGSVGERyataievaagnrlnnvvVEDDA--VAKEAIELLKRrkagratflplnKMRDERRDL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2268 RLMQKNK---------DNTQK------------LLAEEAEKMKSLAEEAARLSVEAE------------ETARQR----K 2310
Cdd:TIGR02169 591 SILSEDGvigfavdlvEFDPKyepafkyvfgdtLVVEDIEAARRLMGKYRMVTLEGElfeksgamtggsRAPRGGilfsR 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2311 TAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQkqknQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQ 2390
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS----QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2391 LEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEK 2470
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2471 EREKLKRDAQELQNKSKETASaqQEQMEQQKAMLQQTFLTEKELLLKR----ERDVEDEKKKLQKHLEDEVNKAKALKDE 2546
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKE--QIKSIEKEIENLNGKKEELEEELEEleaaLRDLESRLGDLKKERDELEAQLRELERK 904
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 2547 QQrQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLAdENKKLREKLESLE 2615
Cdd:TIGR02169 905 IE-ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQA-ELQRVEEEIRALE 971
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1647-2448 |
9.19e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 81.70 E-value: 9.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1647 AREQAEKELETWRLKANEaLRLRLRAEEEAQ-------RKSLAQEEAEKQKTEAERDA-----KKKAKAEEAALKQKENA 1714
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKD-LQRRLNESNELHekqkfylRQSVIDLQTKLQEMQMERDAmadirRRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1715 EKELEKQRTFAE-----------QIAQQKLSAE---QEYIRLKADFEHAEQQRGLLDNELQRL--KNEVNAAEKQRRQLE 1778
Cdd:pfam15921 151 VHELEAAKCLKEdmledsntqieQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1779 DELAKVRSEM----DALLQMKIQA----EKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAAR 1850
Cdd:pfam15921 231 TEISYLKGRIfpveDQLEALKSESqnkiELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1851 QRAEAEKILKEKLAAINEatrLKTEAEVALKAKEAENERLKRQ---AEDEAYQRKLLEDQAAQHKHDIQEkitQLQSSSV 1927
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQ---LRSELREAKRMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDD---QLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1928 SELDRQKNIVEETLRQKKVVEEEIHiIRINFERASKEKSDLEVELKKLKGIAdETQKSkakaeeeaeklkklaaeeerkr 2007
Cdd:pfam15921 385 DLHKREKELSLEKEQNKRLWDRDTG-NSITIDHLRRELDDRNMEVQRLEALL-KAMKS---------------------- 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2008 reaeekvkkiaAAEEEAARQRKAAQDEVERLKQKAAEANKLkdKAEKELEKQVIlAKEAAQKST--AAEQKAQDVLSKNK 2085
Cdd:pfam15921 441 -----------ECQGQMERQMAAIQGKNESLEKVSSLTAQL--ESTKEMLRKVV-EELTAKKMTleSSERTVSDLTASLQ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2086 EDLLSQEKLRDEFENAKKLAQAaetakekaekeaallrqKAEEAEKLKKaaEDEAAKQAKAQKDAERLrkeaeaeAAKRA 2165
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVDL-----------------KLQELQHLKN--EGDHLRNVQTECEALKL-------QMAEK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2166 AAEAAALKQKQEADAEM-AKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAvkqkaqvenE 2244
Cdd:pfam15921 561 DKVIEILRQQIENMTQLvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL---------E 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2245 LSKVKM--QMDELLKLKVRIEEENLRLMQKNKDNTQKL--LAEEAEKMK-SLAEEAARLSVEAEETARQRKTAEAELAEQ 2319
Cdd:pfam15921 632 LEKVKLvnAGSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKrNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2320 RALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLledkQEIQQRLDKETQgFQKSLEAERKRQLE-ISAEAE 2398
Cdd:pfam15921 712 RNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL----EEAMTNANKEKH-FLKEEKNKLSQELStVATEKN 786
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2399 KLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQE----TEKQTTETVVQKLE 2448
Cdd:pfam15921 787 KMAGELEVLRSQERRLKEKVANMEVALDKASLQFAEcqdiIQRQEQESVRLKLQ 840
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1364-1644 |
1.46e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 80.94 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1364 LETQR-RLEDDEKASE-----KLKEDEKKRmaeiQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQR---QGLA 1434
Cdd:pfam17380 296 MEQERlRQEKEEKAREverrrKLEEAEKAR----QAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERirqEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1435 VDAEKQKQ--NIQLELTQLKNLSEQEIRS-KNQQLEEAQVSRRKLEEEIHLIRIQLQttikQKSTADDELQKLRDQAA-E 1510
Cdd:pfam17380 372 MEISRMREleRLQMERQQKNERVRQELEAaRKVKILEEERQRKIQQQKVEMEQIRAE----QEEARQREVRRLEEERArE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1511 AEKVRKAAQE-----------EAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLK 1579
Cdd:pfam17380 448 MERVRLEEQErqqqverlrqqEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQK 527
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 1580 QAEEEKVRQIKVVEEVAQKTAA----TQLQAMSFSEKTTKLeESLKKEQGTVLQLQeEAEKLRKQEEEA 1644
Cdd:pfam17380 528 AIYEEERRREAEEERRKQQEMEerrrIQEQMRKATEERSRL-EAMEREREMMRQIV-ESEKARAEYEAT 594
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
39-152 |
1.53e-14 |
|
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: 72.65 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 39 KTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEVLSgetlPRERDLVRNVRLPREKGRMrFHKLQNVQIALDFLKHR 118
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIK----PGVVDWSRVNKPFKKLGAN-MKKIENCNYAVELGKKL 81
|
90 100 110
....*....|....*....|....*....|....
gi 1655220527 119 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21298 82 KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3079-3117 |
1.87e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 69.66 E-value: 1.87e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1655220527 3079 LLEAQAATGFVIDPVKNEKVSVDDAVKSGLVGPELHEQL 3117
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2015-2622 |
2.34e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.49 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2015 KKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKL 2094
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2095 RDEFENAKKLAQAAETAKEKAEKEAALlRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEaeaeaakraaaeaaaLKQ 2174
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE---------------ING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2175 KQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDE-----------ELQRVKAQVNDAVKQKAQVEN 2243
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlkkrltglTPEKLEKELEELEKAKEEIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2244 ELSKVKmqmDELLKLKVRIEEENLRLMQKNK--------------DNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQR 2309
Cdd:PRK03918 406 EISKIT---ARIGELKKEIKELKKAIEELKKakgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2310 KTAEAELAEQRAL-AEKMLKEKMQAIQEATKlKAEAEELQKQKNQAQEKAKKLLEDKQEIqqrldketqgfqKSLEAERK 2388
Cdd:PRK03918 483 RELEKVLKKESELiKLKELAEQLKELEEKLK-KYNLEELEKKAEEYEKLKEKLIKLKGEI------------KSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2389 RQLEISAEAEKLKLRVKELSSAQAKAEEEATRFK-KQADEAKVRLQETEKqttetvvqkletqrlqSTREADDLKKAIAE 2467
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEP----------------FYNEYLELKDAEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2468 LEKEREKLKRDAQELQNKSKETASAQQEqMEQQKAMLQQtfltekellLKRERDVEDEKKKLQKHLEDEvNKAKALKDEQ 2547
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKR-LEELRKELEE---------LEKKYSEEEYEELREEYLELS-RELAGLRAEL 682
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 2548 QRQQKLMDEEKKKLqaimdeavKKQKEAEAEMKNKQKEMEALEKKRleqekllaDENKKLREKLESLEVTSKQAA 2622
Cdd:PRK03918 683 EELEKRREEIKKTL--------EKLKEELEEREKAKKELEKLEKAL--------ERVEELREKVKKYKALLKERA 741
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
37-149 |
2.48e-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: 71.95 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 37 QKKTFTKWVNKHLMK--AQRHITDLYEDLRDGHNLISLLEVLSGETLPrerDLVRNvrlPREKGRMRfhklQNVQIALDF 114
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLP---GIDWN---PTTDAERK----ENVEKVLQF 70
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220527 115 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21213 71 MASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
164-264 |
2.49e-14 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 71.98 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 243
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1655220527 244 ED-VDVAHPDEKSIITYVSSLY 264
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2212-2629 |
4.93e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.31 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2212 ETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELlklkvrieEENLRLMQKNKDNTQKLLAEEAEK---M 2288
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERY--------EEQREQARETRDEADEVLEEHEERreeL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2289 KSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQaqekakkLLEDKQEI 2368
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREE-------LEDRDEEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2369 QQRLDKE---TQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQ 2445
Cdd:PRK02224 327 RDRLEECrvaAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2446 --KLETQRLQSTREADDLKKAIAELEKEREKLK---RDAQELQNKSK--------------ETASAQQEQMEQQKAMLQQ 2506
Cdd:PRK02224 407 lgNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELED 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2507 TFLTEKELLLKRER-----DVEDEKKKLQ---KHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAE 2578
Cdd:PRK02224 487 LEEEVEEVEERLERaedlvEAEDRIERLEerrEDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 2579 MKNKQKEMEALEKKRleqekllaDENKKLREKLESLEVTSKQAASKTKEIE 2629
Cdd:PRK02224 567 AEEAREEVAELNSKL--------AELKERIESLERIRTLLAAIADAEDEIE 609
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
164-261 |
5.32e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 70.87 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALL-DMSQVYRQSNQENLEQAFSVAERELGVTRLLD 242
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1655220527 243 PEDVDVAHPDEKSIITYVS 261
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2311-2647 |
5.50e-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: 79.34 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2311 TAEAELAEQRALAE-KMLKEKMQAIQEATK-LKAEAEELQKQKNQAqEKAKKLLEDKQEIQQR-LDKETQGFQKSLEAER 2387
Cdd:TIGR02169 165 VAEFDRKKEKALEElEEVEENIERLDLIIDeKRQQLERLRREREKA-ERYQALLKEKREYEGYeLLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2388 KRQLEISAEAEKLKL----RVKELSSAQAKAEEEATRFKKQADEAKVRLQEtEKQTTETVVQKLETQRLQSTREADDLKK 2463
Cdd:TIGR02169 244 RQLASLEEELEKLTEeiseLEKRLEEIEQLLEELNKKIKDLGEEEQLRVKE-KIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2464 AIAELEKEREKLKRDAQELqnksketaSAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQ------KHLEDEV 2537
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEEL--------EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdelKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2538 NKAKALKDEQQRQQKLMDEEKKKL---QAIMDEAVK----KQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKK---L 2607
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLseeLADLNAAIAgieaKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElydL 474
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1655220527 2608 REKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVSMTTVE 2647
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1365-1922 |
7.03e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.80 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1365 ETQRRLEDDEKASEKLK--EDEKKRMAEIQAQLETQKQLAEGHAksVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQ 1442
Cdd:COG4913 239 RAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1443 NIQLELTQLKNLSEQEIRSKNQQLEEaqvsrrkLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEA 1522
Cdd:COG4913 317 RLDALREELDELEAQIRGNGGDRLEQ-------LEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1523 ERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKM----QAEEAERRLKQA---EEEKVR------QI 1589
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEAlglDEAELPfvgeliEV 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1590 KVVEEVAQK-------TAATQL--------QAMSFSEKTT--------KLEESLKKEQGTVLQLQEEAEKLrkqEEEANK 1646
Cdd:COG4913 470 RPEEERWRGaiervlgGFALTLlvppehyaAALRWVNRLHlrgrlvyeRVRTGLPDPERPRLDPDSLAGKL---DFKPHP 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1647 AREQAEKEL--------------------------------------------ETWRL-KANEALRLRLRAEEEAQRKSL 1681
Cdd:COG4913 547 FRAWLEAELgrrfdyvcvdspeelrrhpraitragqvkgngtrhekddrrrirSRYVLgFDNRAKLAALEAELAELEEEL 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1682 AQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRtfaEQIAQqklsAEQEYIRLKA---DFEHAEQQrglldn 1758
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE---REIAE----LEAELERLDAssdDLAALEEQ------ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1759 eLQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAK 1838
Cdd:COG4913 694 -LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1839 KQRQLAEDEAARQRAEAEKILKE--------------KLAAINE-ATRLKTEAEVALKAKEAENERLKRQAEDEayQRKL 1903
Cdd:COG4913 773 ERIDALRARLNRAEEELERAMRAfnrewpaetadldaDLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIE--FVAD 850
|
650
....*....|....*....
gi 1655220527 1904 LEDQAAQHKHDIQEKITQL 1922
Cdd:COG4913 851 LLSKLRRAIREIKERIDPL 869
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1510-2204 |
9.09e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 78.47 E-value: 9.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1510 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEA-ARQKQKALDELQKHKMQAEEAERrlKQAEEEKVRQ 1588
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAeLLTLRSQLLTLCTPCMPDTYHER--KQVLEKELKH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1589 IKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRL 1668
Cdd:TIGR00618 231 LREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1669 RLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENA-EKELEKQRTFAEQIAQQKlSAEQEYIRLKADFE 1747
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHiRDAHEVATSIREISCQQH-TLTQHIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1748 HAEQQRGLLDNELQRLKNEVNAAEKQ---RRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQ---LLETEALKMK 1821
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRtsaFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLekiHLQESAQSLK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1822 QLAEEAARLRSVAEEAKKQRQLAEDEAARQrAEAEKILKEKLAAINEA----------TRLKTEAEVALKAKEAENERLK 1891
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLEL-QEEPCPLCGSCIHPNPArqdidnpgplTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1892 RQAEDEAYQRKLLEDQAAQHKHDIQeKITQLQSSSVSELDRQKNIVEETLrqkKVVEEEIHIIRINFERASKEKSDLEVE 1971
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQ---DLTEKLSEAEDMLACEQHALLRKLQPE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1972 LKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAE-EEAARQRKAAQDEVERLKQKAAEANKLKD 2050
Cdd:TIGR00618 625 QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELlASRQLALQKMQSEKEQLTYWKEMLAQCQT 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2051 KAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKK-------------------------LA 2105
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKarteahfnnneevtaalqtgaelshLA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2106 QAAETAKEKAEKEAALLRQKaeEAEKLKKAAEDEAAKQAKAQKDAERLrkEAEAEAAKRAAAEAAALKQKQEADAEMAKH 2185
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTL--EAEIGQEIPSDEDILNLQCETLVQEE--EQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
730
....*....|....*....
gi 1655220527 2186 KKEAEQALKQKSQVEKELG 2204
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDKLN 879
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1256-1837 |
1.27e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.77 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1256 QEKIEAAPVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAkayidslkdyefqilayralqdpiasplkkpkmesas 1335
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA------------------------------------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1336 DNIIQEYvtlRTRYSELSTLTsqyikfilETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELE 1415
Cdd:PRK02224 240 DEVLEEH---EERREELETLE--------AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1416 AQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEqEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKS 1495
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1496 TADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELK--RKSEAEKEAARQKQKA------------L 1561
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRtaRERVEEAEALLEAGKCpecgqpvegsphV 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1562 DELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEvAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQE 1641
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1642 EEankareqAEKELETWRLKANEAlrlRLRAEEEAQRksLAQEEAEKQKTEAERDAKKKAKAEEAALkqkENAEKELEKQ 1721
Cdd:PRK02224 547 AE-------LEAEAEEKREAAAEA---EEEAEEAREE--VAELNSKLAELKERIESLERIRTLLAAI---ADAEDEIERL 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1722 RTFAEQIAQQKlsaEQEYIRLKADFEHAEQQRGLLDNE-LQRLKNEVNAAEKQRRQLEDELAKVRSEMDAlLQMKIQAek 1800
Cdd:PRK02224 612 REKREALAELN---DERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDD-LQAEIGA-- 685
|
570 580 590
....*....|....*....|....*....|....*..
gi 1655220527 1801 vsqsnTEKSKQLLETEALKMKQLAEEAARLRSVAEEA 1837
Cdd:PRK02224 686 -----VENELEELEELRERREALENRVEALEALYDEA 717
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1365-1874 |
1.40e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.77 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1365 ETQRRLEDDEKASEKLKED----EKKRMA---EIQAQLETQKQLAEGHAKSVAKAELEAQElklkmKEDASQRQGlavDA 1437
Cdd:PRK02224 248 ERREELETLEAEIEDLRETiaetEREREElaeEVRDLRERLEELEEERDDLLAEAGLDDAD-----AEAVEARRE---EL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1438 EKQKQNIQLELTQlknlSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRiqlqttiKQKSTADDELQKLRDQAAEAEKVRKA 1517
Cdd:PRK02224 320 EDRDEELRDRLEE----CRVAAQAHNEEAESLREDADDLEERAEELR-------EEAAELESELEEAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1518 AQEEAERLRKQVNEETQKKKNAEDELKRKSEaEKEAARQKQKALD-ELQKHKMQAEEAERRLKQAE----EEKVRQIKVV 1592
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELRE-ERDELREREAELEaTLRTARERVEEAEALLEAGKcpecGQPVEGSPHV 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1593 EEVAQKtaatqlqamsfSEKTTKLE---ESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLR 1669
Cdd:PRK02224 468 ETIEED-----------RERVEELEaelEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1670 LRAEEEAQRKSLAQEEAEKQKTEAErdakkkakaeeaalKQKENAEKELEKQRTFAEQIAQQKLSAEQ-EYIR-LKADFE 1747
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAA--------------EAEEEAEEAREEVAELNSKLAELKERIESlERIRtLLAAIA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1748 HAEQQRGLLDNELQRLkNEVNaaeKQRRQLEDELAKVRSEMDAllqmKIQAEKVS--QSNTEKSKQLLETEALKMKQLAE 1825
Cdd:PRK02224 603 DAEDEIERLREKREAL-AELN---DERRERLAEKRERKRELEA----EFDEARIEeaREDKERAEEYLEQVEEKLDELRE 674
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1826 EAARLRSVAEEAKkqRQLAEDEAARQRAEAEKILKEKLAAI-NEATRLKT 1874
Cdd:PRK02224 675 ERDDLQAEIGAVE--NELEELEELRERREALENRVEALEALyDEAEELES 722
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
166-264 |
2.58e-13 |
|
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: 68.92 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 166 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 245
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90
....*....|....*....
gi 1655220527 246 VdVAHPDEKSIITYVSSLY 264
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFH 102
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3743-3781 |
2.85e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.58 E-value: 2.85e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1655220527 3743 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPELHDKL 3781
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
31-148 |
3.51e-13 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 68.85 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 31 DERDrvqKKTFTKWVNKHLMKAQrhITDLYEDLRDGhnlISLLEVLsgETLprERDLVRNVRLPREKGRMRFHKLQNVQI 110
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKI--QPGCVNWKKVNKPKPLNKFKKVENCNY 69
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655220527 111 ALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 148
Cdd:cd21219 70 AVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2828-2866 |
7.33e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.43 E-value: 7.33e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1655220527 2828 FLDVQLATGGIIDPVNSHRLPLQTAYKQGQFDPDMNKKL 2866
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2173-2403 |
1.01e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 73.26 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2173 KQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKvkmQM 2252
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE---LL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2253 DELLKLKvRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALaekmLKEKMQ 2332
Cdd:COG4942 111 RALYRLG-RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL----LAELEE 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 2333 AIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLR 2403
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2034-2681 |
1.07e-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: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2034 EVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEdllSQEKLRDEFENAkklaqaAETAKE 2113
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQ---SQEDLRNQLQNT------VHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2114 KAEKEAALLRQKAEEAEKLKKA--AEDEAAKQAKA------QKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKH 2185
Cdd:pfam15921 157 AKCLKEDMLEDSNTQIEQLRKMmlSHEGVLQEIRSilvdfeEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2186 K------KEAEQALKQKSQVEKELGLVKLQldetDKQKALMDEElqrvKAQVNDAVKQKAQVENELSKVKMQMdELLKLK 2259
Cdd:pfam15921 237 KgrifpvEDQLEALKSESQNKIELLLQQHQ----DRIEQLISEH----EVEITGLTEKASSARSQANSIQSQL-EIIQEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2260 VRieEENLRLMQKNKDntqklLAEEAEKMKSLAEEAARLSVEA-EETARQRKTAEAELAEQRALAEKMLKEKMQAIQEAT 2338
Cdd:pfam15921 308 AR--NQNSMYMRQLSD-----LESTVSQLRSELREAKRMYEDKiEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2339 KLKAEAEELQKQKNQAQEKAKKL-----------------LEDKQEIQQRLDKETQGFQKSLEAERKRQLE-ISAEAEKL 2400
Cdd:pfam15921 381 KLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlrreLDDRNMEVQRLEALLKAMKSECQGQMERQMAaIQGKNESL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2401 KlrvkELSSAQAKAEEEATRFKKQADE---AKVRLQETEKQTTETVVQKLETQR-LQSTR-EADDLKKAIAELEKEREKL 2475
Cdd:pfam15921 461 E----KVSSLTAQLESTKEMLRKVVEEltaKKMTLESSERTVSDLTASLQEKERaIEATNaEITKLRSRVDLKLQELQHL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2476 KRDAQELQNKSKETASAQQEQMEQQKAM--LQQTFLTEKELLLKRERD---VEDEKKKLQKHLED---EVNKAKALKDEQ 2547
Cdd:pfam15921 537 KNEGDHLRNVQTECEALKLQMAEKDKVIeiLRQQIENMTQLVGQHGRTagaMQVEKAQLEKEINDrrlELQEFKILKDKK 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2548 qrqqklmDEEKKKLQA-IMDEAVKKQKEAEAemknKQKEMEALEKKRLEQEKLLaDENKKLREKLESL----EVTSKQAA 2622
Cdd:pfam15921 617 -------DAKIRELEArVSDLELEKVKLVNA----GSERLRAVKDIKQERDQLL-NEVKTSRNELNSLsedyEVLKRNFR 684
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 2623 SKTKEIEVQTDKVPEEQLVSMTTVETTKKVFNgSVEAvkKDGASPLAFEGIRESVPAER 2681
Cdd:pfam15921 685 NKSEEMETTTNKLKMQLKSAQSELEQTRNTLK-SMEG--SDGHAMKVAMGMQKQITAKR 740
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3155-3193 |
1.13e-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: 1.13e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1655220527 3155 LLEAQLSTGGIIDPVKSYRVPQEVACKRGYFNEEMAKTL 3193
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
628-818 |
1.22e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 70.17 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 628 QLHTFVTAATKELMWLNEKEEEEVNYDWSDRNTNMTAKKDNYSGLMRELELREKKVNGVQTTGDKLLRDGHPGRKTIEAF 707
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 708 TAALQTQWSWILQLCCCIETHLKENTAHFQFFSDVKEAEERIKKMQDTMKRKYTCDrsiTVTRLEDLVQDAADEREQLNE 787
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|.
gi 1655220527 788 IKTHLEGLKRRAKTIVQLKPRNPATPIKSKL 818
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4332-4370 |
1.23e-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: 1.23e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1655220527 4332 LLEAQACTGGIIDPNTGEKFSVADAMNKGLVDKIMVDRI 4370
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1515-1924 |
1.32e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.42 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1515 RKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE--KVRQIKVV 1592
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEleKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1593 EEVAQKTAATQLQAMSFSEKTTKLEESLKkeqgtvlQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRlRLRA 1672
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLE-------ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1673 EEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIA----------------------- 1729
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllsliltiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1730 ---QQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAK--VRSEMDALLQMKIQAEKVSQS 1804
Cdd:COG4717 280 flvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeeLLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1805 NTEKSKQLLETE--ALKMKQLAEEAARLRSVAEEAKKQRQLAE--DEAARQRAEAEKILKEKLAAINEATRLKTEAEVAL 1880
Cdd:COG4717 360 EEELQLEELEQEiaALLAEAGVEDEEELRAALEQAEEYQELKEelEELEEQLEELLGELEELLEALDEEELEEELEELEE 439
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1655220527 1881 KAKEAENER---LKRQAEDEAYQRKLLEDQAAQH-KHDIQEKITQLQS 1924
Cdd:COG4717 440 ELEELEEELeelREELAELEAELEQLEEDGELAElLQELEELKAELRE 487
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1653-2639 |
1.41e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 74.70 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1653 KELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEK------ELEKQRTFAE 1726
Cdd:TIGR00606 158 QEDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEirdqitSKEAQLESSR 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1727 QIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEvnaaEKQRRQLEDELAKVRsemdallqmkiqaEKVSQSNT 1806
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR----KKQMEKDNSELELKM-------------EKVFQGTD 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1807 EKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLA-------EDEAARQRAEAEKILKEKLAAINEATRLKTEAEVA 1879
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLnqektelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELD 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1880 LKAKEAENERLKRQAEDEAYQRKLLEDQ-AAQHKHDIQEKITqLQSSSVSELDRQKNIVEETLRQKKVVeeeihiirinf 1958
Cdd:TIGR00606 381 GFERGPFSERQIKNFHTLVIERQEDEAKtAAQLCADLQSKER-LKQEQADEIRDEKKGLGRTIELKKEI----------- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1959 eraskeksdLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAaqdEVERL 2038
Cdd:TIGR00606 449 ---------LEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKA---DLDRK 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2039 KQKAAEANKLKDKAEKELEKQVILAKeaaqKSTAAEQKAQDVLSKNKEDLLSQEKlrdEFENAKKLAQAAETAKEKaeke 2118
Cdd:TIGR00606 517 LRKLDQEMEQLNHHTTTRTQMEMLTK----DKMDKDEQIRKIKSRHSDELTSLLG---YFPNKKQLEDWLHSKSKE---- 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2119 aalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAalkqkQEADAEMAKHKKEAEQALKQKSQ 2198
Cdd:TIGR00606 586 ---INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-----QDEESDLERLKEEIEKSSKQRAM 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2199 VEKELGLVKLQLDETD--------------KQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLkvriee 2264
Cdd:TIGR00606 658 LAGATAVYSQFITQLTdenqsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGL------ 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2265 enLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAEL-AEQRALAEKMLKEKMQAIQEATKLKAE 2343
Cdd:TIGR00606 732 --APGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEeSAKVCLTDVTIMERFQMELKDVERKIA 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2344 AEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQgfqkSLEAERKRQLEISAEAEKLKLRVKELSSAqakaeeeatrfKK 2423
Cdd:TIGR00606 810 QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVS----KIELNRKLIQDQQEQIQHLKSKTNELKSE-----------KL 874
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2424 QADEAKVRLQETEKQTTEtvvqkLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAM 2503
Cdd:TIGR00606 875 QIGTNLQRRQQFEEQLVE-----LSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEK 949
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2504 LQQTFLTEKELllkrERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQ----------- 2572
Cdd:TIGR00606 950 VKNIHGYMKDI----ENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQErwlqdnltlrk 1025
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 2573 -----KEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQ 2639
Cdd:TIGR00606 1026 renelKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFR 1097
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1281-1983 |
1.45e-12 |
|
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: 74.72 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1281 LEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDPI------ASPLKKPKMESASDNIIQEYVTLRTRYSELST 1354
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKreyegyELLKEKEALERQKEAIERQLASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1355 LTSQYIKFILETQRRLEDDEKASEKLKEDE----KKRMAEIQAQLETQKqlaeghaKSVAKAELEAQELKLKMKEDASQR 1430
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvKEKIGELEAEIASLE-------RSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1431 QGLAVDAEKQKQNI---QLELTQLKNL---SEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKL 1504
Cdd:TIGR02169 332 DKLLAEIEELEREIeeeRKRRDKLTEEyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1505 RDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE 1584
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1585 kvrqikvVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQA---EKELETWR-- 1659
Cdd:TIGR02169 492 -------LAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvvEDDAVAKEai 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1660 --LKANEALRL------RLRAEEEAQRKSLAQ-------------EEAEK------------QKTEAERDAKKKAKA--- 1703
Cdd:TIGR02169 565 elLKRRKAGRAtflplnKMRDERRDLSILSEDgvigfavdlvefdPKYEPafkyvfgdtlvvEDIEAARRLMGKYRMvtl 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1704 --------------EEAALKQKENAEKELEKQRTFAEQIaqQKLSAEQEyiRLKADFEHAEQQRGLLDNELQRLKNEVNA 1769
Cdd:TIGR02169 645 egelfeksgamtggSRAPRGGILFSRSEPAELQRLRERL--EGLKRELS--SLQSELRRIENRLDELSQELSDASRKIGE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1770 AEKQRRQLEDELAKVRSEMDAlLQMKIQAEKVSQSNTEKSKQLLETEalkMKQLAEEAARLRsvAEEAKKQRQLAEDEAA 1849
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQEIENVKSELKELEAR---IEELEEDLHKLE--EALNDLEARLSHSRIP 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1850 RQRAEAEKIlKEKLAAINEATRlktEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSvSE 1929
Cdd:TIGR02169 795 EIQAELSKL-EEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE-EE 869
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 1930 LDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQ 1983
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
166-261 |
1.92e-12 |
|
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: 66.26 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 166 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALL-DMSQVYRQSNQENLEQAFSVAERELGVTRLLDPE 244
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1655220527 245 DVDVAHPDEKSIITYVS 261
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2407-2626 |
2.11e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.49 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2407 LSSAQAKAEEEATRFKKQADEAKVRLQETEK--QTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQN 2484
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKelAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2485 KSKETAS---AQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQ------KHLEDEVNKAKALKDEQQRQQKLMD 2555
Cdd:COG4942 91 EIAELRAeleAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2556 EEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLAD---ENKKLREKLESLEVTSKQAASKTK 2626
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAEAAAAAERTP 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2410-2629 |
2.21e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.10 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2410 AQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKEt 2489
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2490 asaQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHledevnkaKALKDEQQRQQKLMDEEKKKLQAIMDEAV 2569
Cdd:COG4942 102 ---QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL--------KYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2570 KKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2629
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1365-1923 |
2.47e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 74.09 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1365 ETQRRLEDDEkaSEKLKEDEKKRMAEIQAQLETQKQ-------------LAEGHAKSV---AKAELEAQELKLKMKEDAS 1428
Cdd:NF041483 603 ERIRREAAEE--TERLRTEAAERIRTLQAQAEQEAErlrteaaadasaaRAEGENVAVrlrSEAAAEAERLKSEAQESAD 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1429 QRQGLAV-------------------DAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQT 1489
Cdd:NF041483 681 RVRAEAAaaaervgteaaealaaaqeEAARRRREAEETLGSARAEADQERERAREQSEELLASARKRVEEAQAEAQRLVE 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1490 TIKQKST-----ADDELQKLRD-----------------QAAE--AEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKR 1545
Cdd:NF041483 761 EADRRATelvsaAEQTAQQVRDsvaglqeqaeeeiaglrSAAEhaAERTRTEAQEEADRVRSDAYAERERASEDANRLRR 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1546 KSEAEKEAA-----RQKQKALDELQKHKMQAEEAERRLK--------QAEEEKVRQIKVVEEVAQK------TAATQLQA 1606
Cdd:NF041483 841 EAQEETEAAkalaeRTVSEAIAEAERLRSDASEYAQRVRteasdtlaSAEQDAARTRADAREDANRirsdaaAQADRLIG 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1607 MSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQeeeankAREQAEKELETwrlKANEALRLRlraEEEAQRKSLAQEEA 1686
Cdd:NF041483 921 EATSEAERLTAEARAEAERLRDEARAEAERVRAD------AAAQAEQLIAE---ATGEAERLR---AEAAETVGSAQQHA 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1687 EKQKTEAERDAKKKAKAEEAALKQK--------ENAEKELEKQRT-FAEQIAQQKLSAEQEYIRLKADfEHAEQQRGLLD 1757
Cdd:NF041483 989 ERIRTEAERVKAEAAAEAERLRTEAreeadrtlDEARKDANKRRSeAAEQADTLITEAAAEADQLTAK-AQEEALRTTTE 1067
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1758 NELQRlKNEVNAAEKQRRQLEDE--------LAKVRSEMDALLqmkIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAAR 1829
Cdd:NF041483 1068 AEAQA-DTMVGAARKEAERIVAEatvegnslVEKARTDADELL---VGARRDATAIRERAEELRDRITGEIEELHERARR 1143
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1830 -----LRSVAEEAKKQRQLAEDEAARQRAEAEKILKE--------KLAAINEATRLKTEAEVALKAKEAENERLKRQAED 1896
Cdd:NF041483 1144 esaeqMKSAGERCDALVKAAEEQLAEAEAKAKELVSDanseaskvRIAAVKKAEGLLKEAEQKKAELVREAEKIKAEAEA 1223
|
650 660 670
....*....|....*....|....*....|...
gi 1655220527 1897 EAY------QRKLleDQAAQHKHDIQEKITQLQ 1923
Cdd:NF041483 1224 EAKrtveegKREL--DVLVRRREDINAEISRVQ 1254
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1491-1903 |
2.71e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 73.23 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1491 IKQKSTADDELQKLRDQAAEAEKV--RKAAQEEAERLRKQVNEETQKKkNAEDELKRKSEAEKEAARQKQKALDELQKHK 1568
Cdd:pfam17380 213 IQMSTVAPKEVQGMPHTLAPYEKMerRKESFNLAEDVTTMTPEYTVRY-NGQTMTENEFLNQLLHIVQHQKAVSERQQQE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1569 MQAEEAERRLKQAEEEKVRQIkvveevaqktaatqlqamsfsEKTTKLEESLKKEQGtvlQLQEEAEKLRKQEEEAnkar 1648
Cdd:pfam17380 292 KFEKMEQERLRQEKEEKAREV---------------------ERRRKLEEAEKARQA---EMDRQAAIYAEQERMA---- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1649 EQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQeeaEKQKTEAERDAKKKAKAEEAALKQKENAEKElEKQRTFAEQI 1728
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQEEIAMEISRMR---ELERLQMERQQKNERVRQELEAARKVKILEE-ERQRKIQQQK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1729 AQ-QKLSAEQEYIRlKADFEHAEQQRgllDNELQRLKNEVNAAEKQ---RRQLEDELAKVRSEMDALLQMKIQAEkvsqs 1804
Cdd:pfam17380 420 VEmEQIRAEQEEAR-QREVRRLEEER---AREMERVRLEEQERQQQverLRQQEEERKRKKLELEKEKRDRKRAE----- 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1805 ntEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLA-EDEAARQRAEAEK---ILKEKLAAINEATRLKTEAEVAL 1880
Cdd:pfam17380 491 --EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAiYEEERRREAEEERrkqQEMEERRRIQEQMRKATEERSRL 568
|
410 420
....*....|....*....|...
gi 1655220527 1881 KAKEAENERLKRQAEDEAYQRKL 1903
Cdd:pfam17380 569 EAMEREREMMRQIVESEKARAEY 591
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
32-143 |
2.82e-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: 66.29 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 32 ERDRvQKKTFTKWVNKhlMKAQRHITDLYEDLRDGhnLIsLLEVLSGeTLPRERDLVRNVRLPREKGRMRFHKLQNVQIA 111
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDG--LI-LLQAYDK-VIPGSVNWKKVNKAPASAEISRFKAVENTNYA 76
|
90 100 110
....*....|....*....|....*....|..
gi 1655220527 112 LDFLKHRQVKLVNIRNDDIADGNPKLTLGLIW 143
Cdd:cd21300 77 VELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
55-146 |
4.04e-12 |
|
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: 65.69 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 55 HITDLYEDLRDGHNLISLLEVLSGEtlpreRDLVRNVRLPrEKGRMRfhKLQNVQIALDFLKHRQV----KLVNIRNDDI 130
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGD-----WSLLSKLRVP-AISRLQ--KLHNVEVALKALKEAGVlrggDGGGITAKDI 96
|
90
....*....|....*.
gi 1655220527 131 ADGNPKLTLGLIWTII 146
Cdd:cd21223 97 VDGHREKTLALLWRII 112
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1925-2629 |
5.35e-12 |
|
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: 72.79 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1925 SSVSELDRQKnivEETLRQKKVVEEEIHIIRI-------NFERASKEKSDLEvELKKLKGIADETQKSKAKAEEEAEKLK 1997
Cdd:TIGR02169 163 AGVAEFDRKK---EKALEELEEVEENIERLDLiidekrqQLERLRREREKAE-RYQALLKEKREYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1998 KLAAEEErkrreaeekVKKIAAAEEEAARQRKAAQDEVERLKQKAAEAN-KLKDKAEKE-----------------LEKQ 2059
Cdd:TIGR02169 239 KEAIERQ---------LASLEEELEKLTEEISELEKRLEEIEQLLEELNkKIKDLGEEEqlrvkekigeleaeiasLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2060 VILAKEAAQKSTAAEQKAQDVLSKNKEDLlsqEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDE 2139
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEI---EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2140 aakqakaQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKAL 2219
Cdd:TIGR02169 387 -------LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2220 MDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEE------NLRLMQKNKDNTQKLLAE--EAEKMKSL 2291
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrggraVEEVLKASIQGVHGTVAQlgSVGERYAT 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2292 AEEAA---RLS---VEAEETA-------RQRKTAEA------ELAEQRALAEKMLKEK---------------------- 2330
Cdd:TIGR02169 540 AIEVAagnRLNnvvVEDDAVAkeaiellKRRKAGRAtflplnKMRDERRDLSILSEDGvigfavdlvefdpkyepafkyv 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2331 ------MQAIQEATKLKA-------EAEELQK--------------QKNQAQEKAKklLEDKQEIQQRLDKETQGFQKSL 2383
Cdd:TIGR02169 620 fgdtlvVEDIEAARRLMGkyrmvtlEGELFEKsgamtggsraprggILFSRSEPAE--LQRLRERLEGLKRELSSLQSEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2384 EAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTEtvvQKLETQRLQStrEADDLKK 2463
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN---VKSELKELEA--RIEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2464 AIAELEKEREKLKRD-AQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERdVEDEKkklqKHLEDEVNKAKA 2542
Cdd:TIGR02169 773 DLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY-LEKEI----QELQEQRIDLKE 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2543 LKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADEN---KKLREKLESLEVTSK 2619
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiEKKRKRLSELKAKLE 927
|
810
....*....|
gi 1655220527 2620 QAASKTKEIE 2629
Cdd:TIGR02169 928 ALEEELSEIE 937
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1934-2497 |
6.41e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1934 KNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKlkklaaeeerkrreaeek 2013
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS------------------ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2014 VKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEkqvilAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEK 2093
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-----LSEFYEEYLDELREIEKRLSRLEEEINGIEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2094 LRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLK-KAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAAL 2172
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKaKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2173 KQKQEAdAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKAL---------MDEELQRVKAQVNDAVKQKAQVEN 2243
Cdd:PRK03918 409 KITARI-GELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLeeytaelkrIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2244 ------ELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKL-------------LAEEAEKMKSLAEEAARLSVEAEE 2304
Cdd:PRK03918 488 vlkkesELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLkekliklkgeiksLKKELEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2305 TARQRKTAEAELAEQRALAEKMLKEKMQAIQEATK----LKAEAEELQKQKNQaQEKAKKLLEDKQEIQQRLDKETQGFQ 2380
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEPFYNeyleLKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELR 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2381 KSLEAERKRQLEisAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTEtvvqkletqRLQSTREADD 2460
Cdd:PRK03918 647 KELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE---------REKAKKELEK 715
|
570 580 590
....*....|....*....|....*....|....*..
gi 1655220527 2461 LKKAIAELEKEREKLKRdaqeLQNKSKETASAQQEQM 2497
Cdd:PRK03918 716 LEKALERVEELREKVKK----YKALLKERALSKVGEI 748
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1448-1871 |
6.48e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1448 LTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHliriQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRK 1527
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELK----EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1528 QVN--EETQKKKNAEDELKRKSEaEKEAARQKQKALDELQKhkmQAEEAERRLKQAEEEkvrqikVVEEVAQKTAATQLQ 1605
Cdd:COG4717 124 LLQllPLYQELEALEAELAELPE-RLEELEERLEELRELEE---ELEELEAELAELQEE------LEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1606 AMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEE--EANKAREQAEKELETWRL----------------------- 1660
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEARLllliaaallallglggsllslil 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1661 ----------------------KANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKEL 1718
Cdd:COG4717 274 tiagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1719 EKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQ--QRGLLDNELQRLKNEVNAAEkqrRQLEDELAKVRSEMDALLQMKI 1796
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELE---EQLEELLGELEELLEALDEEEL 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 1797 QAEKvsqsntEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATR 1871
Cdd:COG4717 431 EEEL------EELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLAL 499
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2172-2475 |
8.65e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 72.30 E-value: 8.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2172 LKQKQEADAEMAKHKKEAEQalkQKSQVEKELGLVKLQLdeTDKQKALmdEELQRVKAQVNDAVK--QKAQVENELSKVk 2249
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEA---RAEAAEEEVDELKSQL--ADYQQAL--DVQQTRAIQYQQAVQalERAKQLCGLPDL- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2250 mqmdELLKLKVRIEEenlrLMQKNKDNTQKLLAEE-----AEKMKSLAEEAARL------SVEAEETARQRKTAEAELAE 2318
Cdd:PRK04863 436 ----TADNAEDWLEE----FQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLRE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2319 QRALAEKM--LKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAE 2396
Cdd:PRK04863 508 QRHLAEQLqqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2397 AEKLKLRVKELSS-AQA--KAEEEATRFKKQADEAkvrlQETEKQTTETVVQKLETQRlQSTREADDLKKAIAELEKERE 2473
Cdd:PRK04863 588 LEQLQARIQRLAArAPAwlAAQDALARLREQSGEE----FEDSQDVTEYMQQLLERER-ELTVERDELAARKQALDEEIE 662
|
..
gi 1655220527 2474 KL 2475
Cdd:PRK04863 663 RL 664
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
166-265 |
1.05e-11 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 64.28 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 166 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSN---QENLEQAFSVAERE-LGVTRLL 241
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLgLPELDLF 80
|
90 100
....*....|....*....|....
gi 1655220527 242 DPEDVdVAHPDEKSIITYVSSLYD 265
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2313-2638 |
1.54e-11 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 70.81 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2313 EAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEK---AKKLLEDKQEiQQRLDKETQGFqKSLEaerkr 2389
Cdd:NF033838 103 ELNVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKveeAEKKAKDQKE-EDRRNYPTNTY-KTLE----- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2390 qLEIsAEAEkLKLRVKELSSAQAKAEEEATRFKKQADEAKVRlqetEKQTTETVVQKLETQRLQSTREADdlKKAIAELE 2469
Cdd:NF033838 176 -LEI-AESD-VEVKKAELELVKEEAKEPRDEEKIKQAKAKVE----SKKAEATRLEKIKTDREKAEEEAK--RRADAKLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2470 KEREKLKRDAQELQNKSKETASAQQEQM----EQQKAMLQQTFLTEKEL---LLKRERDVEDEKKKLqkhlEDEVNKAKA 2542
Cdd:NF033838 247 EAVEKNVATSEQDKPKRRAKRGVLGEPAtpdkKENDAKSSDSSVGEETLpspSLKPEKKVAEAEKKV----EEAKKKAKD 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2543 LKDEQQRQQKlmDEEKKKLQAIMDEAVKKQKEAEAEM-KNKQKEMEALEKKRLEQEKLladENKKLR-EKLESLEVTSKQ 2620
Cdd:NF033838 323 QKEEDRRNYP--TNTYKTLELEIAESDVKVKEAELELvKEEAKEPRNEEKIKQAKAKV---ESKKAEaTRLEKIKTDRKK 397
|
330
....*....|....*...
gi 1655220527 2621 AASKTKEIEVQTDKVPEE 2638
Cdd:NF033838 398 AEEEAKRKAAEEDKVKEK 415
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2752-2789 |
1.67e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.67e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1655220527 2752 LLEAQAASGYIVDPVKNKLLTVDEAVKEELIGPELHTR 2789
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1506-1746 |
1.69e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.41 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1506 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEK 1585
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1586 VRQIKVVEEV---AQKTA-ATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRlk 1661
Cdd:COG4942 100 EAQKEELAELlraLYRLGrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1662 anealrlRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIR 1741
Cdd:COG4942 178 -------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 1655220527 1742 LKADF 1746
Cdd:COG4942 251 LKGKL 255
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
533-722 |
2.03e-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: 66.70 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 533 LRYIQDLLGWVEENQRRVDDGEWGSDLPAVESQLGSHRGLHQSVEEFRSKIERAKADESQI---SPASKAAYRDYLAKLE 609
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 610 LQYDKLLHDSKAR---LRYLVQLHTFVTAATKELMWLNEKEEEEVNYDWSDRNTNMTAKKDNYSGLMRELELREKKVNGV 686
Cdd:cd00176 86 QRWEELRELAEERrqrLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1655220527 687 QTTGDKLLRDGHP-GRKTIEAFTAALQTQWSWILQLC 722
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1307-1976 |
2.11e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 70.52 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1307 DYEFQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKaseKLKEDEKK 1386
Cdd:pfam05483 38 DPAFQKLNFLPMLEQVANSGDCHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKEN---KLQENRKI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1387 rmaeIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQR-------QGLAVDAEK------QKQNIQLELTQLKN 1453
Cdd:pfam05483 115 ----IEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnllkETCARSAEKtkkyeyEREETRQVYMDLNN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1454 LSEQEIRSKNQQLEEAQVSRR----KLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQV 1529
Cdd:pfam05483 191 NIEKMILAFEELRVQAENARLemhfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1530 NEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLK-------QAEEEKVRQIkvvEEVAQKTAAT 1602
Cdd:pfam05483 271 NQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQM---EELNKAKAAH 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1603 QLQAMSFSEKTTKLEESLKKEQGTVLQ-------LQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLrlrAEEE 1675
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEKnedqlkiITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKL---LDEK 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1676 AQRKSLAQE-------------EAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQ--KLSAEQEYI 1740
Cdd:pfam05483 425 KQFEKIAEElkgkeqelifllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdKLLLENKEL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1741 RLKAD---FEHAEQQRGLLDNELQ--RLKNEVNAAEKQRRQLEDELAKVRSEM-DALLQMKIQAEKvSQSNTEKSKQLLE 1814
Cdd:pfam05483 505 TQEASdmtLELKKHQEDIINCKKQeeRMLKQIENLEEKEMNLRDELESVREEFiQKGDEVKCKLDK-SEENARSIEYEVL 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1815 TEALKMKQLAEEAARLRSVAEEAKK--QRQLAEDEAARQRAEAE-------KILKEKLAAINEATRLKTEAEVALKAKEA 1885
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIENKNKniEELHQENKALKKKGSAEnkqlnayEIKVNKLELELASAKQKFEEIIDNYQKEI 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1886 ENERLKRQA-EDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKkvvEEEIHIIRINFERASKE 1964
Cdd:pfam05483 664 EDKKISEEKlLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSELGLYKNKEQEQSSA 740
|
730
....*....|..
gi 1655220527 1965 KSDLEVELKKLK 1976
Cdd:pfam05483 741 KAALEIELSNIK 752
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3486-3520 |
2.11e-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: 2.11e-11
10 20 30
....*....|....*....|....*....|....*
gi 1655220527 3486 LLEAQFATGGIIDPVSSHRVPNDVAIQRGYLSKQM 3520
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPET 35
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2213-2625 |
2.33e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2213 TDKQKALMDEELQRVKAQVNDAVKQK---AQVENELSKVKMQMDELLKLKVRIEEE--NLRLMQKNKDNTQKLLAEEAEk 2287
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAE- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2288 MKSLAEEAARLSVEAE---ETARQRKTAEAELAE-QRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLE 2363
Cdd:COG4717 141 LAELPERLEELEERLEelrELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2364 DKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEE------------ATRFKKQADEAKVR 2431
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2432 LQETEKQTTETVVQKLETQRLQSTREADDLKKAI--AELEKEREKLKRDAQELQNKSKETASAQQEQ-MEQQKAMLQQTF 2508
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLspEELLELLDRIEELQELLREAEELEEELQLEElEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2509 LTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKL----MDEEKKKLQAIMDEAVKKQKEAEAEMKNKQK 2584
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeeLEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1655220527 2585 EMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKT 2625
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALEL 501
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1013-1694 |
2.44e-11 |
|
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: 70.53 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1013 TKIKDLRLKLDGCESrtvTRLRQPVDKEPLKACAQKTAEQMKVQSEL-EGLKKDLNSITEKTEEILASPQ---QSSSAPM 1088
Cdd:pfam15921 117 TKLQEMQMERDAMAD---IRRRESQSQEDLRNQLQNTVHELEAAKCLkEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSIL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1089 LRSElDVTLKKMDHVYGLSSVYLDKLKT-IDIVIRNTkdaeDTVKSY-ESRLrdvskVPAEEkeveahrsQLKAMRAEAE 1166
Cdd:pfam15921 194 VDFE-EASGKKIYEHDSMSTMHFRSLGSaISKILREL----DTEISYlKGRI-----FPVED--------QLEALKSESQ 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1167 ADQATFdrLQDElkaatsvSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQREL----SLLGRHMNSYKQSY 1242
Cdd:pfam15921 256 NKIELL--LQQH-------QDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQArnqnSMYMRQLSDLESTV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1243 EWLIQWLREA-RLRQEKIEA---------APVWDSKALKEQLTQE--------KKLLEEIEKNKDQIENCQKDAKAYID- 1303
Cdd:pfam15921 327 SQLRSELREAkRMYEDKIEElekqlvlanSELTEARTERDQFSQEsgnlddqlQKLLADLHKREKELSLEKEQNKRLWDr 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1304 -------------SLKDYEFQILAYRALQDPIASPLKKpKMESASDNIIQEYVTLRtrysELSTLTSQyIKFILETQRRL 1370
Cdd:pfam15921 407 dtgnsitidhlrrELDDRNMEVQRLEALLKAMKSECQG-QMERQMAAIQGKNESLE----KVSSLTAQ-LESTKEMLRKV 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1371 EDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAK----AELEAQELK-LKMKEDASQR-----QGLAVDAEKQ 1440
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrVDLKLQELQhLKNEGDHLRNvqtecEALKLQMAEK 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1441 KQNIQLELTQLKNLSeQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQ--TTIKQKSTA----------DDELQKLRDQA 1508
Cdd:pfam15921 561 DKVIEILRQQIENMT-QLVGQHGRTAGAMQVEKAQLEKEINDRRLELQefKILKDKKDAkirelearvsDLELEKVKLVN 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1509 AEAEKVRkaAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALD-ELQKHKMQAEEAERRLKQA------ 1581
Cdd:pfam15921 640 AGSERLR--AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtTTNKLKMQLKSAQSELEQTrntlks 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1582 -EEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRL 1660
Cdd:pfam15921 718 mEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS 797
|
730 740 750
....*....|....*....|....*....|....
gi 1655220527 1661 KANealrlrlRAEEEAQRKSLAQEEAEKQKTEAE 1694
Cdd:pfam15921 798 QER-------RLKEKVANMEVALDKASLQFAECQ 824
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2347-2644 |
2.58e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.15 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2347 LQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLEisaEAEKLKlrvkelssaQAKAEEEATRFKKQAD 2426
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKE----EKAREVERRRKLE---EAEKAR---------QAEMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2427 EAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKERE-KLKRDAQELqnkskETASAQQEQMEQQKAMLQ 2505
Cdd:pfam17380 342 MAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQqKNERVRQEL-----EAARKVKILEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2506 QTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKalKDEQQRQQKL-----MDEEKKKLQAIMDEAVKKQKEAEAE-M 2579
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQREVRRLEEERAREMERVR--LEEQERQQQVerlrqQEEERKRKKLELEKEKRDRKRAEEQrR 494
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 2580 KNKQKEMEALEKKRLEQE---KLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVSMT 2644
Cdd:pfam17380 495 KILEKELEERKQAMIEEErkrKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKAT 562
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2278-2599 |
2.64e-11 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 68.41 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2278 QKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEK 2357
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2358 AKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEklkLRVKELSSAQAKAEEEATRFKKQADEAKvrlqetEK 2437
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREED---ERILEYLKEKAEREEEREAEREEIEEEK------ER 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2438 QTTETVVQKLETQRLQSTREADDLKKAIAELE-KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQtfltekelll 2516
Cdd:pfam13868 185 EIARLRAQQEKAQDEKAERDELRAKLYQEEQErKERQKEREEAEKKARQRQELQQAREEQIELKERRLAE---------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2517 KRERDVEDEKKKLQKHLEDEvnkaKALKDEQQRQQKLMDEEKKKLQAIMDE---AVKKQKEAEAEMKNKQKEMEALEKKR 2593
Cdd:pfam13868 255 EAEREEEEFERMLRKQAEDE----EIEQEEAEKRRMKRLEHRRELEKQIEEreeQRAAEREEELEEGERLREEEAERRER 330
|
....*.
gi 1655220527 2594 LEQEKL 2599
Cdd:pfam13868 331 IEEERQ 336
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2380-2606 |
3.20e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 68.64 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2380 QKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQttetvVQKLETQRLQSTREAD 2459
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE-----LAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2460 DLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQ--QTFLTEKELLLKRERDVEDEKKKLQKHLEDEV 2537
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 2538 NKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKK 2606
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1436-1976 |
4.41e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1436 DAEKQKQNIQLELTQLKNlSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVR 1515
Cdd:PRK03918 190 NIEELIKEKEKELEEVLR-EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1516 KAAQEEAERLRKQVNEETQKKKNAEdELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRqikvVEEV 1595
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER----LEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1596 AQKTAATQlqamsfsEKTTKLEESLKKEQgTVLQLQEEAEKLRKQE-----EEANKAREQAEKELETWRLKANEALRLRL 1670
Cdd:PRK03918 344 KKKLKELE-------KRLEELEERHELYE-EAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1671 RAEEEAQRKSLAQEEAEKQK----------TEAERDAKKKAKAEEAALKQKE--NAEKELEKQRTFAEQIaQQKLSAEQE 1738
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKgkcpvcgrelTEEHRKELLEEYTAELKRIEKElkEIEEKERKLRKELREL-EKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1739 YIRLKadfEHAEQQRGlLDNELQRL-KNEVNAAEKQRRQLEDELAKVRSEMdallqmkiqaekvsqsntekskQLLETEA 1817
Cdd:PRK03918 495 LIKLK---ELAEQLKE-LEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEI----------------------KSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1818 LKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDE 1897
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 1898 AYQRKLLEDQAAQHKhDIQEKITQLQSSSVSEldRQKNIVEETLRqkkvVEEEIHIIRINFERASKEKSDLEVELKKLK 1976
Cdd:PRK03918 629 DKAFEELAETEKRLE-ELRKELEELEKKYSEE--EYEELREEYLE----LSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2124-2475 |
4.44e-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: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2124 QKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKqeadaemakhKKEAEQALKQK--SQVEK 2201
Cdd:pfam17380 307 EKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER----------KRELERIRQEEiaMEISR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2202 ELGLVKLQLDETDKQkalmdeelQRVKAQVNDAVKQKAQVENELSKVKMQMDELlkLKVRIEEENLRlmqknkdntqkll 2281
Cdd:pfam17380 377 MRELERLQMERQQKN--------ERVRQELEAARKVKILEEERQRKIQQQKVEM--EQIRAEQEEAR------------- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2282 aeeAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlaekmlkekmqaiqEATKLKAEAEELQKQKNQAQEKAKKL 2361
Cdd:pfam17380 434 ---QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE--------------ERKRKKLELEKEKRDRKRAEEQRRKI 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2362 LEdkQEIQQRLdketqgfQKSLEAERKRQLeISAEAEKlklRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTE 2441
Cdd:pfam17380 497 LE--KELEERK-------QAMIEEERKRKL-LEKEMEE---RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
330 340 350
....*....|....*....|....*....|....
gi 1655220527 2442 tvvqklETQRLQSTREADDLKKAIAELEKEREKL 2475
Cdd:pfam17380 564 ------ERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1466-1985 |
5.10e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1466 LEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVnEETQKKKNAEDELKR 1545
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1546 K---SEAEKEAARQKQKALDE-LQKHKMQAEEAERRLKQAeEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLK 1621
Cdd:PRK03918 239 EieeLEKELESLEGSKRKLEEkIRELEERIEELKKEIEEL-EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1622 KEQGTVLQLQEEAEKLRKQEEEANKAREQAEK------ELETWRLKANEALRLRLRAEE-EAQRKSLAQEEAEKQKTEAE 1694
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKElekrleELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1695 RdakkkakaeeaalkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKA------------DFEHAEQQRGLLDNELQR 1762
Cdd:PRK03918 398 K--------------AKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEEHRKELLEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1763 LKNEVNAAEKQRRQLEDELAKVRSEMDA---LLQMKIQAEKVSQSNTEKSKQLLEtealKMKQLAEEAARLRSVAEEAKK 1839
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKeseLIKLKELAEQLKELEEKLKKYNLE----ELEKKAEEYEKLKEKLIKLKG 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1840 QRQLAEDEAARqraeaEKILKEKLAAINEATRlKTEAEVALKAKEAENERLKRQAEDE--------AYQRKLLEDQAAQH 1911
Cdd:PRK03918 540 EIKSLKKELEK-----LEELKKKLAELEKKLD-ELEEELAELLKELEELGFESVEELEerlkelepFYNEYLELKDAEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1912 KHDIQEKITQLQSS---SVSELDRQKNIVEETLRQ-----KKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQ 1983
Cdd:PRK03918 614 LEREEKELKKLEEEldkAFEELAETEKRLEELRKEleeleKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693
|
..
gi 1655220527 1984 KS 1985
Cdd:PRK03918 694 KT 695
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1518-2058 |
6.14e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1518 AQEEAERLRKQVNEetqKKKNAEDELKRKSEAE---KEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKvrqiKVVEE 1594
Cdd:PRK03918 163 AYKNLGEVIKEIKR---RIERLEKFIKRTENIEeliKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1595 VAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRlRAEE 1674
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-EIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1675 EAQRKSLAQEEAEKQKTEAERDakkkAKAEEAALKQKENAEKELEKQRTFAEqiaqqklsaeqEYIRLKADFEHAEQQRG 1754
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHE-----------LYEEAKAKKEELERLKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1755 LL-DNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQS---------------NTEKSKQLLETEAL 1818
Cdd:PRK03918 380 RLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1819 KMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQR--------AEAEKILKEKLAAINeATRLKTEAEVALKAKEAEN--- 1887
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelAEQLKELEEKLKKYN-LEELEKKAEEYEKLKEKLIklk 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1888 -------ERLKRQAEDEAYQRKLLE--DQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQkkvveeeihiirinF 1958
Cdd:PRK03918 539 geikslkKELEKLEELKKKLAELEKklDELEEELAELLKELEELGFESVEELEERLKELEPFYNE--------------Y 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1959 ERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRRE-AEEKVKKIAAAEEEAARQRKAAQDEVER 2037
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEE 684
|
570 580
....*....|....*....|.
gi 1655220527 2038 LKQKAAEANKLKDKAEKELEK 2058
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEE 705
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1124-1836 |
7.03e-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: 69.23 E-value: 7.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1124 TKDAEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRL---HSERDAEL 1200
Cdd:TIGR00618 207 TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQeavLEETQERI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1201 EHYRQLAGSLLE---------RWQAVFAQIDLRQREL-SLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKAL 1270
Cdd:TIGR00618 287 NRARKAAPLAAHikavtqieqQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1271 -KEQLTQEKKLLEEIEKNKDQIENCQKDAKAyIDSLKDYEFQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRY 1349
Cdd:TIGR00618 367 iREISCQQHTLTQHIHTLQQQKTTLTQKLQS-LCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1350 SELSTLTSQYIKFIL--ETQRRLeDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELE-AQELKLKMKED 1426
Cdd:TIGR00618 446 AITCTAQCEKLEKIHlqESAQSL-KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHpNPARQDIDNPG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1427 ASQRQGLAVDAEKQKQniqleltqlknlsEQEIRSKNQQLEEAQVSRRKLEEEIHLIriqlqttikqkstaDDELQKLRD 1506
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQL-------------ETSEEDVYHQLTSERKQRASLKEQMQEI--------------QQSFSILTQ 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1507 QAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEE-------AERRLK 1579
Cdd:TIGR00618 578 CDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKltalhalQLTLTQ 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1580 QAEEEKVRQIKVVEEVAQKTAATQLQAM-SFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETW 1658
Cdd:TIGR00618 658 ERVREHALSIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1659 RLKANEALRlrlRAEEEAQRKSLAQEEAEKQKTEAErdakkkaKAEEAALKQKENAEKELE-KQRTFAEQIAQQKLSAEQ 1737
Cdd:TIGR00618 738 EDALNQSLK---ELMHQARTVLKARTEAHFNNNEEV-------TAALQTGAELSHLAAEIQfFNRLREEDTHLLKTLEAE 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1738 EYIRLKADFEHAEQQRGLLDNELQRLKNevnaaekQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEA 1817
Cdd:TIGR00618 808 IGQEIPSDEDILNLQCETLVQEEEQFLS-------RLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
|
730
....*....|....*....
gi 1655220527 1818 LKMKQLAEEAARLRSVAEE 1836
Cdd:TIGR00618 881 INQIKIQFDGDALIKFLHE 899
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1532-2591 |
8.23e-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: 68.92 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1532 ETQKKKNAEDELKRKSEAEKEAARQKQKALDelQKHKMQAEEAERRLKQAEEEKVRQI--KVVEEVAQKTAATQLqAMSF 1609
Cdd:TIGR00606 167 EGKALKQKFDEIFSATRYIKALETLRQVRQT--QGQKVQEHQMELKYLKQYKEKACEIrdQITSKEAQLESSREI-VKSY 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1610 SEKTTKLEESLKK---EQGTVLQLQEEAEKLRKQEEEankaREQAEKELETWRLKANEALRLRLRAEEEAQRKSLaqEEA 1686
Cdd:TIGR00606 244 ENELDPLKNRLKEiehNLSKIMKLDNEIKALKSRKKQ----MEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTV--REK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1687 EKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRG-LLDNELQrlkn 1765
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpFSERQIK---- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1766 evNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKK----QR 1841
Cdd:TIGR00606 394 --NFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegsSD 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1842 QLAEDEAARQRAEAEKILKEKlaaiNEATRLKTEAEVALKAKEAENERLKRqAEDEAYQRKLLEDQA-------AQHKHD 1914
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEK----NSLTETLKKEVKSLQNEKADLDRKLR-KLDQEMEQLNHHTTTrtqmemlTKDKMD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1915 IQEKITQLQSSSVSELDRQKNiveeTLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLkgiadETQKSkakaeeeae 1994
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLG----YFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASL-----EQNKN--------- 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1995 klkklaaeeerkrreaeekvkKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLkDKAEKELEKQvilAKEAAQKSTAAE 2074
Cdd:TIGR00606 609 ---------------------HINNELESKEEQLSSYEDKLFDVCGSQDEESDL-ERLKEEIEKS---SKQRAMLAGATA 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2075 QKAQDVlsknkedllsqEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLR 2154
Cdd:TIGR00606 664 VYSQFI-----------TQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLA 732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2155 KEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKqkalmdeeLQRVKAQVNDA 2234
Cdd:TIGR00606 733 PGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI--------MERFQMELKDV 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2235 VKQKAQVENELSKVKMqmdellklkvrieeeNLRLMQKNKDNTQKllAEEAEKMKSLAEEAARLSVEAEETARQRKTAEA 2314
Cdd:TIGR00606 805 ERKIAQQAAKLQGSDL---------------DRTVQQVNQEKQEK--QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTN 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2315 ELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRldkETQGFQKSLEAERKRQLEIS 2394
Cdd:TIGR00606 868 ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE---KEELISSKETSNKKAQDKVN 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2395 AEAEKLKLRVKELSSAQAKAEEEATRFKKQAD----EAKVRLQETEKQTTE------TVVQKLETQRLQSTREADDLKka 2464
Cdd:TIGR00606 945 DIKEKVKNIHGYMKDIENKIQDGKDDYLKQKEtelnTVNAQLEECEKHQEKinedmrLMRQDIDTQKIQERWLQDNLT-- 1022
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2465 iaeLEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLT---EKELLLKRERDVEDEKKKLQKHLedevnKAK 2541
Cdd:TIGR00606 1023 ---LRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLikrNHVLALGRQKGYEKEIKHFKKEL-----REP 1094
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2542 ALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEK 2591
Cdd:TIGR00606 1095 QFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINK 1144
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3986-4024 |
9.88e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.26 E-value: 9.88e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1655220527 3986 LLEAQAATGYVIDPIKNLKLNVTEAVKMGVVGPEFKDKL 4024
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1427-1835 |
1.07e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 68.44 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1427 ASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKnQQLEEAQVSRRKLEEEI-----HLIRiqLQTTIKQKSTAD--- 1498
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMA-RELEELSARESDLEQDYqaasdHLNL--VQTALRQQEKIEryq 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1499 DELQKLRDQAAEAEKVRKAAQEEAERLRKQvneetqkKKNAEDELKrkseaekEAARQ---KQKALDELQKHKMQAEEAE 1575
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEAR-------LEAAEEEVD-------SLKSQladYQQALDVQQTRAIQYQQAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1576 RRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRK--QEEEANKAREQAEK 1653
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiaGEVERSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1654 ELETWRLKANEALRLR-LRAE-EEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELE----KQRTFAEQ 1727
Cdd:COG3096 500 LLRRYRSQQALAQRLQqLRAQlAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEeleeQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1728 IAQ-----QKLSAEQEYIRLKADFEHAEQQRglldneLQRLKNEVNAAekqrrqLEDelakvRSEMDALLQMKIQAE--- 1799
Cdd:COG3096 580 RSElrqqlEQLRARIKELAARAPAWLAAQDA------LERLREQSGEA------LAD-----SQEVTAAMQQLLERErea 642
|
410 420 430
....*....|....*....|....*....|....*..
gi 1655220527 1800 KVSQSNTEKSKQLLETEALKMKQLA-EEAARLRSVAE 1835
Cdd:COG3096 643 TVERDELAARKQALESQIERLSQPGgAEDPRLLALAE 679
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4408-4446 |
1.16e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.88 E-value: 1.16e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1655220527 4408 FLEVQYLTGGLIEPDTTGRVSIDEAVKKGSLDARTAQKL 4446
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1268-1918 |
1.52e-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: 67.82 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1268 KALKE-QLTQEK---KLLEEIEKNKDQIEncQKDAKAYIDSLkdyefqilayraLQDPIA-SPLKKPKMESASDNIIQEY 1342
Cdd:pfam05483 120 KAIQElQFENEKvslKLEEEIQENKDLIK--ENNATRHLCNL------------LKETCArSAEKTKKYEYEREETRQVY 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1343 VTLRTRYSELST----LTSQYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQ---LETQKQLAEGHAKSVAKAELE 1415
Cdd:pfam05483 186 MDLNNNIEKMILafeeLRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1416 AQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKS 1495
Cdd:pfam05483 266 SRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1496 TADDELQKLRDQAAEAEKVRKAAQEEAERLRKQ---VNEETQKKKNAEDE---LKRKSEAEKEAAR----QKQKALDELQ 1565
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQlkiITMELQKKSSELEEmtkFKNNKEVELEELKkilaEDEKLLDEKK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1566 KHKMQAEEAERR------LKQAEEEKVRQIKVveEVAQKTAATQLQAMSFSEKTTKLE-ESLKKEQGTV---------LQ 1629
Cdd:pfam05483 426 QFEKIAEELKGKeqelifLLQAREKEIHDLEI--QLTAIKTSEEHYLKEVEDLKTELEkEKLKNIELTAhcdklllenKE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1630 LQEEAE----KLRKQEEEANKAREQAEKELEtwRLKANEALRLRLRAEEEAQRKSLAQ---------EEAEKQKTEAERD 1696
Cdd:pfam05483 504 LTQEASdmtlELKKHQEDIINCKKQEERMLK--QIENLEEKEMNLRDELESVREEFIQkgdevkcklDKSEENARSIEYE 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1697 AKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKlsaeqeyirlkadfeHAEQQRGLLDNElqrlknEVNAAEKQRRQ 1776
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN---------------KALKKKGSAENK------QLNAYEIKVNK 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1777 LEDELAKVRS---EMDALLQMKIQAEKVSQSNtekskqlLETEALKMKQLAEEAARLRSVAEEaKKQRQLAEDEA--ARQ 1851
Cdd:pfam05483 641 LELELASAKQkfeEIIDNYQKEIEDKKISEEK-------LLEEVEKAKAIADEAVKLQKEIDK-RCQHKIAEMVAlmEKH 712
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 1852 RAEAEKILKEKLAAI-------NEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEK 1918
Cdd:pfam05483 713 KHQYDKIIEERDSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1676-1930 |
1.64e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.33 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1676 AQRKSLAQEEAEKQKTEAerdakkkakaeeaalkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGL 1755
Cdd:COG4942 17 AQADAAAEAEAELEQLQQ----------------EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1756 LDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAE 1835
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1836 EAKKQRQlaedEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDI 1915
Cdd:COG4942 161 ELAALRA----ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|....*
gi 1655220527 1916 QEKITQLQSSSVSEL 1930
Cdd:COG4942 237 AAAAERTPAAGFAAL 251
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1407-2254 |
1.74e-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: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1407 KSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRS--KNQQLEEAQVSRR------KLEE 1478
Cdd:pfam05483 9 KSFNKCTEDDFEFPFAKSNLSKNGENIDSDPAFQKLNFLPMLEQVANSGDCHYQEglKDSDFENSEGLSRlysklyKEAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1479 EIHLIRIQLQTTIKQKSTaddelqKLRDQAAEAEKVRKAAQE---EAERLRKQVNEETQKKKNAEDELKRKSEAEKEAAR 1555
Cdd:pfam05483 89 KIKKWKVSIEAELKQKEN------KLQENRKIIEAQRKAIQElqfENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1556 QKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQaMSFS-----EKTTKLEESLKKEQGT---- 1626
Cdd:pfam05483 163 TCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLE-MHFKlkedhEKIQHLEEEYKKEINDkekq 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1627 ----VLQLQEEAEKLRKQ----EEEANKAREQAEK-ELETWRLKANEALRLRLRAEEEAQRKSLaQEEAEKQKTeAERDA 1697
Cdd:pfam05483 242 vsllLIQITEKENKMKDLtfllEESRDKANQLEEKtKLQDENLKELIEKKDHLTKELEDIKMSL-QRSMSTQKA-LEEDL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1698 KKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQklsaeqeyirLKADFEHAEQqrgLLDNELQRLKNEvnaaEKQRRQL 1777
Cdd:pfam05483 320 QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE----------FEATTCSLEE---LLRTEQQRLEKN----EDQLKII 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1778 EDELAKVRSEMDALLQMKiqaekvsqSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAK-KQRQLAEDEAARQRAEAE 1856
Cdd:pfam05483 383 TMELQKKSSELEEMTKFK--------NNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgKEQELIFLLQAREKEIHD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1857 KILKEKLAAINEATRLKteaEVALKAKEAENERLKRQAEDEAYQRKLLEDQaaqhkhdiqeKITQLQSSSVSELDRQKni 1936
Cdd:pfam05483 455 LEIQLTAIKTSEEHYLK---EVEDLKTELEKEKLKNIELTAHCDKLLLENK----------ELTQEASDMTLELKKHQ-- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1937 vEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKK 2016
Cdd:pfam05483 520 -EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2017 IAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKedlLSQEKLRD 2096
Cdd:pfam05483 599 LKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK---ISEEKLLE 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2097 EFENAKKLaqaaetakekaekeaallrqkAEEAEKLKKAAEDEAAKQAKaqkdaerlrkeaeaeaakraaaeaaalkqkq 2176
Cdd:pfam05483 676 EVEKAKAI---------------------ADEAVKLQKEIDKRCQHKIA------------------------------- 703
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 2177 EADAEMAKHKKEAEQALKQKsqvEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDE 2254
Cdd:pfam05483 704 EMVALMEKHKHQYDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2187-2428 |
2.30e-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: 65.94 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2187 KEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELlklkvrieEEN 2266
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL--------EKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2267 LRLMQKNKDNTQKLLAE---EAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlaekmlkekmQAIQEATKLKAE 2343
Cdd:COG4942 92 IAELRAELEAQKEELAEllrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR----------EQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2344 AEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKK 2423
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....*
gi 1655220527 2424 QADEA 2428
Cdd:COG4942 242 RTPAA 246
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4330-4367 |
3.04e-10 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 57.88 E-value: 3.04e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1655220527 4330 QRLLEAQACTGGIIDPNTGEKFSVADAMNKGLVDKIMV 4367
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1830-2551 |
3.24e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 67.16 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1830 LRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKlaaINEATRLKTE--AEVALKAKEAENERLKRQAEDEAYQRKLLEdQ 1907
Cdd:NF041483 78 LRNAQIQADQLRADAERELRDARAQTQRILQEH---AEHQARLQAElhTEAVQRRQQLDQELAERRQTVESHVNENVA-W 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1908 AAQHKHDIQEKITQLQSSSVSELDrqKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKlkgiadETQKSKA 1987
Cdd:NF041483 154 AEQLRARTESQARRLLDESRAEAE--QALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARK------DAERLLN 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1988 KAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRkaAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAA 2067
Cdd:NF041483 226 AASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQR--MQEAEEALREARAEAEKVVAEAKEAAAKQLASAESAN 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2068 QK--STAAEQKAQDVLSKNKEdllsQEKLRDEFENAKKLAQAAETakekaekeaallRQKAEEAEKLK-KAAEDEAAKQA 2144
Cdd:NF041483 304 EQrtRTAKEEIARLVGEATKE----AEALKAEAEQALADARAEAE------------KLVAEAAEKARtVAAEDTAAQLA 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2145 KAQKDAER-LRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKE------LGLVKLQLD------ 2211
Cdd:NF041483 368 KAARTAEEvLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDdtkeyrAKTVELQEEarrlrg 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2212 ETDKQKALMDEELQRVKAQV-NDAVKQ----KAQVENELSKVKMQMDElLKLKVRIEEENLRLMQKNKDNTQKLLAEEAe 2286
Cdd:NF041483 448 EAEQLRAEAVAEGERIRGEArREAVQQieeaARTAEELLTKAKADADE-LRSTATAESERVRTEAIERATTLRRQAEET- 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2287 kMKSLAEEAARLSVEAEETAR-QRKTAEAELAEQRALAEK-MLKEKMQAIQEATKLKAEAEE----LQKQKNQAQEKAKK 2360
Cdd:NF041483 526 -LERTRAEAERLRAEAEEQAEeVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAEErltaAEEALADARAEAER 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2361 LLEDKQEIQQRLDKETqgfqksleAERKRQLEISAEAEKLKLR---VKELSSAQAKAEEEATRFKKQADEAKVRLQETEK 2437
Cdd:NF041483 605 IRREAAEETERLRTEA--------AERIRTLQAQAEQEAERLRteaAADASAARAEGENVAVRLRSEAAAEAERLKSEAQ 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2438 QTTETVVQKLETqrlQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQkamlqqtfltEKELLLK 2517
Cdd:NF041483 677 ESADRVRAEAAA---AAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQ----------SEELLAS 743
|
730 740 750
....*....|....*....|....*....|....*.
gi 1655220527 2518 RERDVEDEKKKLQKHLEDEVNKAKAL--KDEQQRQQ 2551
Cdd:NF041483 744 ARKRVEEAQAEAQRLVEEADRRATELvsAAEQTAQQ 779
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1457-1787 |
3.41e-10 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 66.04 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1457 QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVR-KAAQEEAERLRKQVNEETQK 1535
Cdd:pfam02029 17 EERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRqKRLQEALERQKEFDPTIADE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1536 KKNAEDELKRKSEAEKEAARQKQKALDELQKHKMqaEEAERRLKQAEEEKVRQ-IKVVEEVAQKTAATQLQAMSFSEKTT 1614
Cdd:pfam02029 97 KESVAERKENNEEEENSSWEKEEKRDSRLGRYKE--EETEIREKEYQENKWSTeVRQAEEEGEEEEDKSEEAEEVPTENF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1615 KLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAE 1694
Cdd:pfam02029 175 AKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1695 RdakkkakaeeaalkqkENAEKELEKqrtfAEQIAQQKLSAEQEYIRLKadfEHAEQQRGLLDNELQRLKNEVN----AA 1770
Cdd:pfam02029 255 R----------------RRQEKESEE----FEKLRQKQQEAELELEELK---KKREERRKLLEEEEQRRKQEEAerklRE 311
|
330
....*....|....*..
gi 1655220527 1771 EKQRRQLEDELAKVRSE 1787
Cdd:pfam02029 312 EEEKRRMKEEIERRRAE 328
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1253-1602 |
3.50e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 66.69 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1253 RLRQEKIEaapvwdsKALKEQLTQEKK-LLEEIEKNKdQIENCQKDAKAYIDSlkdyefqilayralQDPIASPLKKPKM 1331
Cdd:pfam17380 287 RQQQEKFE-------KMEQERLRQEKEeKAREVERRR-KLEEAEKARQAEMDR--------------QAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1332 ESASDniiQEYVTLRTRYSELSTLTSQYIKFILETQRRLE--------DDEKASEKLKEDEKKRMAEIQAQLETQKQLAE 1403
Cdd:pfam17380 345 ERERE---LERIRQEERKRELERIRQEEIAMEISRMRELErlqmerqqKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1404 ghAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKnlsEQEIRSKNQQLEEAQVSRRKLEEEihli 1483
Cdd:pfam17380 422 --MEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ---EEERKRKKLELEKEKRDRKRAEEQ---- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1484 riqlqttikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEEtQKKKNAEDElkRKSEAEKEAARQKQKALDE 1563
Cdd:pfam17380 493 ---------RRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-ERRREAEEE--RRKQQEMEERRRIQEQMRK 560
|
330 340 350
....*....|....*....|....*....|....*....
gi 1655220527 1564 LQKHKMQAEEAERrlkqaEEEKVRQIKVVEEVAQKTAAT 1602
Cdd:pfam17380 561 ATEERSRLEAMER-----EREMMRQIVESEKARAEYEAT 594
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1126-1678 |
3.60e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1126 DAEDTVKSYESRLRDV-SKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYR 1204
Cdd:COG1196 278 ELELELEEAQAEEYELlAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1205 QLAGSLLERWQAVFAQIDLRQRElsllgrhmnsykqsyewliqwlrEARLRQEKIEAApvwdsKALKEQLTQEKKLLEEI 1284
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEE-----------------------LEELAEELLEAL-----RAAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1285 EKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDpiasplkkpKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFIL 1364
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALE---------EAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1365 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAE-------------GHAKSVAKAELEAQELKLKMKEDASQRQ 1431
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavavligvEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1432 GLAVDAEKQKQNIQ--LELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAA 1509
Cdd:COG1196 561 AAIEYLKAAKAGRAtfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1510 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQI 1589
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1590 KVVEEVAQKTAATQLQamsfsekttkLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwRLKA-Nealrl 1668
Cdd:COG1196 721 LEEEALEEQLEAEREE----------LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE--ALGPvN----- 783
|
570
....*....|
gi 1655220527 1669 rLRAEEEAQR 1678
Cdd:COG1196 784 -LLAIEEYEE 792
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2029-2615 |
3.64e-10 |
|
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: 66.53 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2029 KAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAqdVLSKNKEDLLSQEKLRDEFENAKKLAQAA 2108
Cdd:TIGR00618 229 KHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEA--VLEETQERINRARKAAPLAAHIKAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2109 ETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKE 2188
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQ 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2189 AEQALKQKSQV-----EKELGLVKLQLDETDKQKALMDEELQ---RVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKV 2260
Cdd:TIGR00618 387 QKTTLTQKLQSlckelDILQREQATIDTRTSAFRDLQGQLAHakkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2261 RIEEENLRLMQKnkdntQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELaEQRALAEKMLKEKMQAIQEATKL 2340
Cdd:TIGR00618 467 SLKEREQQLQTK-----EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR-QDIDNPGPLTRRMQRGEQTYAQL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2341 KAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLE-AERKRQLEISAEAEKLKLRVKELSSAQAKAEEEAt 2419
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEdIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR- 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2420 rfKKQADEAKVRLQETEKQTTETVVQKLETQrlqsTREADDLKKaiaelEKEREKLKR-DAQELQNKSKETASAQQEQME 2498
Cdd:TIGR00618 620 --KLQPEQDLQDVRLHLQQCSQELALKLTAL----HALQLTLTQ-----ERVREHALSiRVLPKELLASRQLALQKMQSE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2499 QQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKA-----LKDEQQRQQKLMDEEKKKLQAIMDEAVKKQK 2573
Cdd:TIGR00618 689 KEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSdlaarEDALNQSLKELMHQARTVLKARTEAHFNNNE 768
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1655220527 2574 EAEAEMKNKQKEMEaLEKKRLEQEKLLADENKKLREKLESLE 2615
Cdd:TIGR00618 769 EVTAALQTGAELSH-LAAEIQFFNRLREEDTHLLKTLEAEIG 809
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1434-1835 |
3.68e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.90 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1434 AVDAEKQKQNIQLELtqlkNLSEQEIRSKNQQLEEAQVSRRKLEEEI-----HLIRIQ----LQTTIKQkstADDELQKL 1504
Cdd:PRK04863 288 ALELRRELYTSRRQL----AAEQYRLVEMARELAELNEAESDLEQDYqaasdHLNLVQtalrQQEKIER---YQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1505 RDQAAEAEKVRKAAQEEAERLRkqvneetqkkknaedelKRKSEAEKEAARQK------QKALDELQKHKMQAEEAERRL 1578
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENE-----------------ARAEAAEEEVDELKsqladyQQALDVQQTRAIQYQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1579 KQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRK------QEEEANKAREqAE 1652
Cdd:PRK04863 424 ERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevsRSEAWDVARE-LL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1653 KELETWRLKAN--EALRLRLRaeeEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQ 1730
Cdd:PRK04863 503 RRLREQRHLAEqlQQLRMRLS---ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1731 QKLSAEQEYIRLKADFEHAEQQRglldnelQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSN--TEK 1808
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAARA-------PAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERdeLAA 652
|
410 420
....*....|....*....|....*...
gi 1655220527 1809 SKQLLETEALKMKQL-AEEAARLRSVAE 1835
Cdd:PRK04863 653 RKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3819-3857 |
3.84e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 57.72 E-value: 3.84e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1655220527 3819 LLEAQNATGGLMDPEYCFHLPTDVAMQRGYINKETLDRI 3857
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2408-2672 |
4.27e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 65.24 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2408 SSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSK 2487
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2488 ETASAQQEQMEQQKAMLQ-------QTFLTEKELLlkrerdvedekKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKK 2560
Cdd:COG3883 90 ERARALYRSGGSVSYLDVllgsesfSDFLDRLSAL-----------SKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2561 LQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2640
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250 260 270
....*....|....*....|....*....|..
gi 1655220527 2641 VSMTTVETTKKVFNGSVEAVKKDGASPLAFEG 2672
Cdd:COG3883 239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1427-1663 |
4.35e-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: 65.17 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1427 ASQRQGLAVDAEKQKQNIQLELTQLknlsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRD 1506
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1507 QAAEAEKVRKAAQEE-AERLRK-QVNEETQKKK---NAED--ELKRKSEAEKEAARQKQKALDELQKhkmQAEEAERRLK 1579
Cdd:COG4942 91 EIAELRAELEAQKEElAELLRAlYRLGRQPPLAlllSPEDflDAVRRLQYLKYLAPARREQAEELRA---DLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1580 QAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWR 1659
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....
gi 1655220527 1660 LKAN 1663
Cdd:COG4942 248 FAAL 251
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1358-1981 |
5.48e-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: 66.30 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1358 QYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLEtQKQLAEGHAKSVAKAELEAQElklkmkedasqrqglavDA 1437
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQ-EMQMERDAMADIRRRESQSQE-----------------DL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1438 EKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQ---VSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKL--RDQAAEAE 1512
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRkmmLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1513 KVRKAAQEEAERLRKQVNEetqkkknAEDELkrksEAEKEAARQKQKALdeLQKHKmqaEEAERRLKQAEEEkvrqikvV 1592
Cdd:pfam15921 224 KILRELDTEISYLKGRIFP-------VEDQL----EALKSESQNKIELL--LQQHQ---DRIEQLISEHEVE-------I 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1593 EEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVL----QLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALrl 1668
Cdd:pfam15921 281 TGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMrqlsDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL-- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1669 rlrAEEEAQRKSLAQEEA----EKQKTEAErdakkkakaeeaalKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKA 1744
Cdd:pfam15921 359 ---TEARTERDQFSQESGnlddQLQKLLAD--------------LHKREKELSLEKEQNKRLWDRDTGNSITIDHLRREL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1745 DFEHAEQQRglLDNELQRLKNEVNAaekqrrQLEDELAKVRSEMDALlqmkiqaEKVSQ--SNTEKSKQLLE--TEALKM 1820
Cdd:pfam15921 422 DDRNMEVQR--LEALLKAMKSECQG------QMERQMAAIQGKNESL-------EKVSSltAQLESTKEMLRkvVEELTA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1821 KQLAEEAARlRSVAEEAKkqrQLAEDEAARQRAEAE--KILKEKLAAINEATRLKTEAEvALKAKEAENERLKRQAEDEA 1898
Cdd:pfam15921 487 KKMTLESSE-RTVSDLTA---SLQEKERAIEATNAEitKLRSRVDLKLQELQHLKNEGD-HLRNVQTECEALKLQMAEKD 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1899 YQRKLLEDQAaqhkhdiqEKITQL---QSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKE----KSDLEVE 1971
Cdd:pfam15921 562 KVIEILRQQI--------ENMTQLvgqHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRElearVSDLELE 633
|
650
....*....|
gi 1655220527 1972 LKKLKGIADE 1981
Cdd:pfam15921 634 KVKLVNAGSE 643
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2264-2493 |
8.15e-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: 64.40 E-value: 8.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2264 EENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRalaekmlkekmqaiQEATKLKAE 2343
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE--------------AELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2344 AEELQKQKNQAQEKAKKLLED--KQEIQQRLD-----KETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEE 2416
Cdd:COG4942 92 IAELRAELEAQKEELAELLRAlyRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 2417 EATRFKKQADEAKVRLQ--ETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQ 2493
Cdd:COG4942 172 ERAELEALLAELEEERAalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1484-1696 |
8.74e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.06 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1484 RIQLQttikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE---ETQKKKNAEDELKRKSEAEKEAARQKQKA 1560
Cdd:PRK09510 66 RQQQQ----QKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKErlaAQEQKKQAEEAAKQAALKQKQAEEAAAKA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1561 ldeLQKHKMQAEEAERRL----KQAEEEKVRQikvVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEK 1636
Cdd:PRK09510 142 ---AAAAKAKAEAEAKRAaaaaKKAAAEAKKK---AEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEA 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1637 LRKQEEEANKAREQAEKELEtwrlkanealrlrlrAEEEAQRKSLAQEEAEKQKTEAERD 1696
Cdd:PRK09510 216 KKKAAAEAKAAAAKAAAEAK---------------AAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2066-2623 |
8.97e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 65.63 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2066 AAQKSTAAEQKAQDVLSKNKEDLLSQekLRDEfenakklaqaaetakekaekeaalLRQKAEEAEKLKKAAeDEAAKQAK 2145
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNQLLRT--LDDQ------------------------WKEKRDELNGELSAA-DAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2146 AQKDAerlrkeaeaeaakraaaEAAALKQKQEADAEmaKHKKEAEQALKQKSQVEKELGLVKLQLD-------ETDKQKA 2218
Cdd:pfam12128 322 SELEA-----------------LEDQHGAFLDADIE--TAAADQEQLPSWQSELENLEERLKALTGkhqdvtaKYNRRRS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2219 LMDEELQRVKAQVND--------AVKQKAQVENELSKVKMQM------------DELLKLKVRIEEENLRLMQknkdntq 2278
Cdd:pfam12128 383 KIKEQNNRDIAGIKDklakireaRDRQLAVAEDDLQALESELreqleagklefnEEEYRLKSRLGELKLRLNQ------- 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2279 kLLAEEAEKMKslaeeaarLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKA 2358
Cdd:pfam12128 456 -ATATPELLLQ--------LENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2359 KKLLEDKQEIQQRLDKETQGFQKSLEAERKRQL--------EISAEAEK-------LKLRVKELSSAQAKAEEEATRfkk 2423
Cdd:pfam12128 527 LQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELlhrtdldpEVWDGSVGgelnlygVKLDLKRIDVPEWAASEEELR--- 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2424 qadeAKVRLQETEKQTTETVVQKLETQrlqstreaddLKKAIAELEKEREKLKRDAQELQNkSKETASAQQEQMEQQKAM 2503
Cdd:pfam12128 604 ----ERLDKAEEALQSAREKQAAAEEQ----------LVQANGELEKASREETFARTALKN-ARLDLRRLFDEKQSEKDK 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2504 LQQTFLTEKELLLKRERDVEDEKKKLQKHLED--EVNKAKALKDEQQRQQK---LMDEEKKKLQAIMDEAVKKQKEAEAE 2578
Cdd:pfam12128 669 KNKALAERKDSANERLNSLEAQLKQLDKKHQAwlEEQKEQKREARTEKQAYwqvVEGALDAQLALLKAAIAARRSGAKAE 748
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1655220527 2579 MKNKQKEME-ALEKKRLEQEKL--LADENKKLREKLESLEVTSKQAAS 2623
Cdd:pfam12128 749 LKALETWYKrDLASLGVDPDVIakLKREIRTLERKIERIAVRRQEVLR 796
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1499-1981 |
1.11e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1499 DELQKLRDQAAEAEKVRKAAQEEAERLRkQVNEETQKKKNAEDELkRKSEAEKEAAR--QKQKALDELQKhkmQAEEAER 1576
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLE-PIRELAERYAAARERL-AELEYLRAALRlwFAQRRLELLEA---ELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1577 RLKQAEEEKVRQikvveEVAQKTAATQLQAmsfsekttkLEESLKKEQGTVL-QLQEEAEKLRKQEEEANKAREQAEKEL 1655
Cdd:COG4913 303 ELARLEAELERL-----EARLDALREELDE---------LEAQIRGNGGDRLeQLEREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1656 ET--WRLKANEA--LRLRLRAEEEAQRKSLAQEEAEKQKTEAERDakkkakaeeaaLKQKENAEKELEKQRtfaEQIAQQ 1731
Cdd:COG4913 369 AAlgLPLPASAEefAALRAEAAALLEALEEELEALEEALAEAEAA-----------LRDLRRELRELEAEI---ASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1732 KLSAEQEYIRLKADFEHAeqqRGLLDNELQ--------RLKNEV--NAAEK----QRRQL---EDELAKVRSEMDAL-LQ 1793
Cdd:COG4913 435 KSNIPARLLALRDALAEA---LGLDEAELPfvgelievRPEEERwrGAIERvlggFALTLlvpPEHYAAALRWVNRLhLR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1794 MKIQAEKVSQSNTEKSKQLLETEALKMK--------------QLAEEAARLR--SVAE---------------------E 1836
Cdd:COG4913 512 GRLVYERVRTGLPDPERPRLDPDSLAGKldfkphpfrawleaELGRRFDYVCvdSPEElrrhpraitragqvkgngtrhE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1837 AKKQRQLAED-----EAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLleDQAAQH 1911
Cdd:COG4913 592 KDDRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAERE 669
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 1912 KHDIQEKITQLQSSS--VSELDRQkniVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADE 1981
Cdd:COG4913 670 IAELEAELERLDASSddLAALEEQ---LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
27-149 |
1.22e-09 |
|
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: 58.75 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 27 EKYKDERDRVQ--KKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerdLVRNVRLPREKGrmrfHK 104
Cdd:cd21222 5 DLFDEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVP----LHEYHLTPSTDD----EK 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1655220527 105 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21222 77 LHNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1132-1941 |
1.24e-09 |
|
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: 64.81 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1132 KSYESRLRDVSKVPAEEKEVEAHRSQLKamraeaEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLL 1211
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSLSKLK------NKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1212 ERWQAVFAQIDLRQREL-SLLGRHMNSYKQSYEWLIQwLREARLR----QEKIEAAPVWDSKALKeqltQEKKLLEEIEK 1286
Cdd:pfam01576 229 AQIAELRAQLAKKEEELqAALARLEEETAQKNNALKK-IRELEAQiselQEDLESERAARNKAEK----QRRDLGEELEA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1287 NKDQIENCQkDAKAYIDSLkdyefqilayRALQDPIASPLKKpKMESASDNIIQEYVTLRTRYSE-LSTLTSQyikfiLE 1365
Cdd:pfam01576 304 LKTELEDTL-DTTAAQQEL----------RSKREQEVTELKK-ALEEETRSHEAQLQEMRQKHTQaLEELTEQ-----LE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1366 TQRRledDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEdasqrqglavdAEKQKQNIQ 1445
Cdd:pfam01576 367 QAKR---NKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE-----------SERQRAELA 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1446 LELTQLKNlseqEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTikQKSTADDELQKLrdqaAEAEKVRkAAQEEAERL 1525
Cdd:pfam01576 433 EKLSKLQS----ELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT--QELLQEETRQKL----NLSTRLR-QLEDERNSL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1526 RKQVNEETQKKKNAEdelkrkseaekeaaRQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQ 1605
Cdd:pfam01576 502 QEQLEEEEEAKRNVE--------------RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1606 AmsfsEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEAlrlRLRAEEEAQRK------ 1679
Cdd:pfam01576 568 Y----DKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEE---RDRAEAEAREKetrals 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1680 -SLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEK---ELEKQRTFAEQIAQQ------------------KLSAEQ 1737
Cdd:pfam01576 641 lARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKnvhELERSKRALEQQVEEmktqleeledelqatedaKLRLEV 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1738 EYIRLKADF--------EHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDelAKVRSEMDaLLQMKIQAEKVSQSNTEKS 1809
Cdd:pfam01576 721 NMQALKAQFerdlqardEQGEEKRRQLVKQVRELEAELEDERKQRAQAVA--AKKKLELD-LKELEAQIDAANKGREEAV 797
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1810 KQLLETEAlKMKQLAEEAARLRSVAEEAKKQRQlaEDEAARQRAEAEKI-LKEKLAAINEATRlKTEAEVALKAKEAENE 1888
Cdd:pfam01576 798 KQLKKLQA-QMKDLQRELEEARASRDEILAQSK--ESEKKLKNLEAELLqLQEDLAASERARR-QAQQERDELADEIASG 873
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 1889 RLKRQAEDEAYQRklLEDQAAQHKHDIQEKitQLQSSSVSELDRQKNIVEETL 1941
Cdd:pfam01576 874 ASGKSALQDEKRR--LEARIAQLEEELEEE--QSNTELLNDRLRKSTLQVEQL 922
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
38-146 |
1.32e-09 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 58.74 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 38 KKTFTKWVNKHLMKaQRHIT----------DLYEDLRDGHNLISLLEVLSGETLPrERDLVRnvrlprEKGRMRFHKLQN 107
Cdd:cd21217 3 KEAFVEHINSLLAD-DPDLKhllpidpdgdDLFEALRDGVLLCKLINKIVPGTID-ERKLNK------KKPKNIFEATEN 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655220527 108 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 146
Cdd:cd21217 75 LNLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
32-151 |
1.47e-09 |
|
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: 59.24 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 32 ERDRVQKKTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEVLSgetLPRERDLVRNVRLPREKGRMRfhKLQNVQIA 111
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIK---VPVDWNKVNKPPYPKLGANMK--KLENCNYA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1655220527 112 LDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 151
Cdd:cd21331 91 VELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1516-1776 |
1.47e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 63.33 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1516 KAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELqKHKMQAEEAERRLKQAEEEKVRQIKVVEEV 1595
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKEL-EQRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1596 AQKTAAtqlqamsfsekttklEESLKKEQGTVLQLQEEAEKlrKQEEEAN-KAREQAEKELETWRLKANEAlrlrLRAEE 1674
Cdd:TIGR02794 125 KAKQAA---------------EAKAKAEAEAERKAKEEAAK--QAEEEAKaKAAAEAKKKAEEAKKKAEAE----AKAKA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1675 EAQRKslAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEyirlkadfehAEQQRG 1754
Cdd:TIGR02794 184 EAEAK--AKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSN----------AEKQGG 251
|
250 260
....*....|....*....|..
gi 1655220527 1755 LLDNELQRLKNEVNAAEKQRRQ 1776
Cdd:TIGR02794 252 ARGAAAGSEVDKYAAIIQQAIQ 273
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1046-1584 |
1.58e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1046 AQKTAEQMKVQSELEGLKKDLNSITEKTEEILASPQQsssapmLRSELDVTLKKMDHvyglssvylDKLKTIDIVIRNTK 1125
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYE------LLAELARLEQDIAR---------LEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1126 DAEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQ 1205
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1206 LAGSLLERWQAVFAQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAApvwdSKALKEQLTQEKKLLEEIE 1285
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE----EEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1286 KNKDQIENCQKDAKAYIDSLKDyefQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILE 1365
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLE---AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1366 tqRRLEDDEKASEKLKEDEKKR--------MAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDA 1437
Cdd:COG1196 554 --EDDEVAAAAIEYLKAAKAGRatflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1438 EKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKA 1517
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220527 1518 AQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELqkhKMQAEEAERRLKQAEEE 1584
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE---PPDLEELERELERLERE 775
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2124-2629 |
1.58e-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: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2124 QKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEA-DAEMAKHKKEAEQALKQKSQVEKE 2202
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEElRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2203 LGLVKLQLDETDkqkalmDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELlKLKVRIEEENLrlmQKNKDNTQKLLA 2282
Cdd:COG4913 325 LDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALLAAL-GLPLPASAEEF---AALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2283 EEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRA----LAEKMLkEKMQAIQEATKLKAE-----AEELQ-KQKN 2352
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksnIPARLL-ALRDALAEALGLDEAelpfvGELIEvRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2353 QAQEKA-------------------KKLLE--DKQEIQQRLDkeTQGFQKSLEAERKRQLEISAEAEKLKLRVkelSSAQ 2411
Cdd:COG4913 474 ERWRGAiervlggfaltllvppehyAAALRwvNRLHLRGRLV--YERVRTGLPDPERPRLDPDSLAGKLDFKP---HPFR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2412 AKAEEEATRfkkQADEAKVR----LQETEKQTTET---------------------------VVQKLETQRlqstREADD 2460
Cdd:COG4913 549 AWLEAELGR---RFDYVCVDspeeLRRHPRAITRAgqvkgngtrhekddrrrirsryvlgfdNRAKLAALE----AELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2461 LKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKA 2540
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2541 KALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQ 2620
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
|
....*....
gi 1655220527 2621 AASKTKEIE 2629
Cdd:COG4913 782 LNRAEEELE 790
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1371-1738 |
1.59e-09 |
|
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: 64.61 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1371 EDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDaeKQKQNIQLELTQ 1450
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD--KINEELKLLKQK 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1451 LKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKstADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVN 1530
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKV--EEEKEEKLKAQEEELRALEEELKEEAELLEEEQL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1531 EETQKKKNAEDELKRKSEAEKEAARQKQKALDELQ-KHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSF 1609
Cdd:pfam02463 823 LIEQEEKIKEEELEELALELKEEQKLEKLAEEELErLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKEL 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1610 SEKTTKLEESLKKEQGTVLQLQEEAEKLRK----------------QEEEANKAREQAEKELETWRLKANEALRLRLRAE 1673
Cdd:pfam02463 903 EEESQKLNLLEEKENEIEERIKEEAEILLKyeeepeellleeadekEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEE 982
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 1674 EEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQE 1738
Cdd:pfam02463 983 FEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAE 1047
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2333-2563 |
2.19e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2333 AIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQA 2412
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2413 KAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQrLQSTREADDLKKAIAELEKEREKLKRDAQELQNKsKETASA 2492
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAAL-RAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 2493 QQEQMEQQKAMLQQtfltEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQA 2563
Cdd:COG4942 172 ERAELEALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1461-1690 |
2.41e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1461 SKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAE 1540
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1541 DELKRKSE--AEKEAARQKQKALDELQ--KHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKL 1616
Cdd:COG4942 97 AELEAQKEelAELLRALYRLGRQPPLAllLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 1617 EESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRL--RLRAEEEAQRKSLAQEEAEKQK 1690
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAAGFAALK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1273-1981 |
2.62e-09 |
|
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: 63.50 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1273 QLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQIlayralqdpIASPLKKPKMESASDNIIQEyvtLRTRYSEL 1352
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKI---------NNSNNKIKILEQQIKDLNDK---LKKNKDKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1353 STLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRmaeiqaqLETQKQLAEgHAKSVAKAELEAQELKLKMKedasqrqg 1432
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQK-------KENKKNIDK-FLTEIKKKEKELEKLNNKYN-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1433 lavDAEKQKQNIQLELTQLKNlseqEIRSKNQQLEEAQVSRRKLEeeihliriQLQTTIKQKSTADDELQKlrdQAAEAE 1512
Cdd:TIGR04523 163 ---DLKKQKEELENELNLLEK----EKLNIQKNIDKIKNKLLKLE--------LLLSNLKKKIQKNKSLES---QISELK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1513 KVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVV 1592
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1593 EEVAQKTAATQLQamSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETwrlKANEALRLrlra 1672
Cdd:TIGR04523 305 EQDWNKELKSELK--NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE---KQNEIEKL---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1673 EEEAQRKSLAQEEAEKQKTEAERdakkkakaeeaALKQKENAEKELEKQrtfAEQIAQQKLSAEQEYIRLKADFEHAEQQ 1752
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLES-----------KIQNQEKLNQQKDEQ---IKKLQQEKELLEKEIERLKETIIKNNSE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1753 RGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALlqmKIQAEKVSQSNTEKSKQLLETEALKmKQLAEEAARLRS 1832
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKI---KQNLEQKQKELKSKEKELKKLNEEK-KELEEKVKDLTK 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1833 VAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQA-EDEAYQRKLLEDQAAQH 1911
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSlKKKQEEKQELIDQKEKE 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1912 KHDIQEKITqLQSSSVSELDRQKNIVEETLRQ-----------KKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIAD 1980
Cdd:TIGR04523 598 KKDLIKEIE-EKEKKISSLEKELEKAKKENEKlssiiknikskKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
|
.
gi 1655220527 1981 E 1981
Cdd:TIGR04523 677 D 677
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2074-2654 |
2.97e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 63.83 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2074 EQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERL 2153
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2154 RKEAEAEaakraaaeaaaLKQKQEADAEMAKHKkEAEQALKQKSQVEKELGLVKlQLDETDKQKALMDEELQ-------R 2226
Cdd:TIGR00618 259 QQLLKQL-----------RARIEELRAQEAVLE-ETQERINRARKAAPLAAHIK-AVTQIEQQAQRIHTELQskmrsraK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2227 VKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNT-QKLLAEEAEKMKSLAEEAARLSVEAEET 2305
Cdd:TIGR00618 326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTlTQHIHTLQQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2306 ARQRKTAEAELAEQRALAEKMLKEKMQaiQEATKLKAEAEELQKQKNQAQEKAKKLLEdkQEIQQRLDKETQGFQkSLEA 2385
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLQGQLAHAKKQ--QELQQRYAELCAAAITCTAQCEKLEKIHL--QESAQSLKEREQQLQ-TKEQ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2386 ERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVrlqetekqtTETVVQKLETQRLQSTREADDLKKAI 2465
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGP---------LTRRMQRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2466 AELEKEREKLKRDAQELQnksketasaqqeQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHledevnkAKALKD 2545
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQ------------QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA-------EDMLAC 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2546 EQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMkNKQKEMEALEKKRLEQEKLLADENKKL----REKLESLEVTSKQA 2621
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLT-ALHALQLTLTQERVREHALSIRVLPKEllasRQLALQKMQSEKEQ 691
|
570 580 590
....*....|....*....|....*....|...
gi 1655220527 2622 ASKTKEIEVQTDKVPEEQLvsmTTVETTKKVFN 2654
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELE---THIEEYDREFN 721
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1466-1923 |
3.13e-09 |
|
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: 63.49 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1466 LEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEdelKR 1545
Cdd:NF033838 71 LSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEAT---KK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1546 KSEAEKEAARQKQK-----ALDELQKHKMQAEEAERRLKQAEEEKVRQikvveevaqktaatqlqamsfSEKTTKLEESL 1620
Cdd:NF033838 148 VEEAEKKAKDQKEEdrrnyPTNTYKTLELEIAESDVEVKKAELELVKE---------------------EAKEPRDEEKI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1621 KKEQGTVLQLQEEAEKLRKQEEEANKAREqaekeletwrlkanEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDakkk 1700
Cdd:NF033838 207 KQAKAKVESKKAEATRLEKIKTDREKAEE--------------EAKRRADAKLKEAVEKNVATSEQDKPKRRAKRG---- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1701 AKAEEAALKQKENAEKELEKQrTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRlknevNAAEKQRRQLEDE 1780
Cdd:NF033838 269 VLGEPATPDKKENDAKSSDSS-VGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRR-----NYPTNTYKTLELE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1781 LAKVRSEM-DALLQMkIQAEKVSQSNTEKSKQLLEtealKMKQLAEEAARLrsvaEEAKKQRQLAEDEAARQRAEAEKIl 1859
Cdd:NF033838 343 IAESDVKVkEAELEL-VKEEAKEPRNEEKIKQAKA----KVESKKAEATRL----EKIKTDRKKAEEEAKRKAAEEDKV- 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 1860 KEKLAainEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKllEDQAAQHKHDIQEKITQLQ 1923
Cdd:NF033838 413 KEKPA---EQPQPAPAPQPEKPAPKPEKPAEQPKAEKPADQQA--EEDYARRSEEEYNRLTQQQ 471
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1726-2481 |
5.37e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 62.82 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1726 EQIAQQKLSAEQEYIRlKADFEHAEQQRGL---LDNELQRLKNEVNAAEKQRRQLEDELAKVRSemdaLLQMKIQAEKVS 1802
Cdd:pfam05483 51 EQVANSGDCHYQEGLK-DSDFENSEGLSRLyskLYKEAEKIKKWKVSIEAELKQKENKLQENRK----IIEAQRKAIQEL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1803 QSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEvALKA 1882
Cdd:pfam05483 126 QFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFE-ELRV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1883 kEAENERLKRQAedeayqrKLLEDQaaqhkhdiqEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERAS 1962
Cdd:pfam05483 205 -QAENARLEMHF-------KLKEDH---------EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1963 KEKSDLEVELKklkgIADETQKskakaeeeaeklkklaaeeeRKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKA 2042
Cdd:pfam05483 268 DKANQLEEKTK----LQDENLK--------------------ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2043 AEANKLKDKAEKELEKqviLAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALL 2122
Cdd:pfam05483 324 KTICQLTEEKEAQMEE---LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2123 RQKAEEAEKLKKA-AEDEaaKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEK 2201
Cdd:pfam05483 401 NNKEVELEELKKIlAEDE--KLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2202 ELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLL 2281
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFI 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2282 AEEAE---KMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKA 2358
Cdd:pfam05483 559 QKGDEvkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKV 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2359 KKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQ---------------AKAEEEATRFKK 2423
Cdd:pfam05483 639 NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQkeidkrcqhkiaemvALMEKHKHQYDK 718
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2424 QADE--AKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQE 2481
Cdd:pfam05483 719 IIEErdSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1464-1972 |
5.49e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1464 QQLEEAQVSRRKLEEEI-HLIRIQlqttikqksTADDELQKLRDQAAEAEKVRKA-----AQEEAERLRKQVNEETQKKK 1537
Cdd:COG4913 235 DDLERAHEALEDAREQIeLLEPIR---------ELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1538 NAEDELKRKSEAEKEAARQKQKALDELQKHKMQA-EEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMS----FSEK 1612
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeeFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1613 TTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwRLKANealRLRLRAEEEAQRKSLAQE----EAEK 1688
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA--SLERR---KSNIPARLLALRDALAEAlgldEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1689 Q--------KTEAERdakkkakaeeaalkqKENA-EKELEKQRT-----------FAEQIAQQKLSAEQEYIRLKADFEH 1748
Cdd:COG4913 461 PfvgelievRPEEER---------------WRGAiERVLGGFALtllvppehyaaALRWVNRLHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1749 AEQQRGLLDNELQRLKNEVNAAekqRRQLEDELA------KVRSEMD------------------ALLQMKIQAEKVSQ- 1803
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKPHPF---RAWLEAELGrrfdyvCVDSPEElrrhpraitragqvkgngTRHEKDDRRRIRSRy 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1804 ----SNTEKsKQLLETEAlkmKQLAEEAARLRSVAEEAKKQRQLAED--EAARQRAE-----------AEKI--LKEKLA 1864
Cdd:COG4913 603 vlgfDNRAK-LAALEAEL---AELEEELAEAEERLEALEAELDALQErrEALQRLAEyswdeidvasaEREIaeLEAELE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1865 AINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQ- 1943
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAa 758
|
570 580 590
....*....|....*....|....*....|.
gi 1655220527 1944 --KKVVEEEIHIIRINFERASKEKSDLEVEL 1972
Cdd:COG4913 759 lgDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2325-2598 |
5.95e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2325 KMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGfqksLEAERKRQLEISAEAEKLKLRV 2404
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK----LEKEVKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2405 KELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTE-TVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQ 2483
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2484 NKSKEtasaqqeqmeqqkamlqqtfLTEKElllKRERDVEDEKKKLQKHLED------EVNKAKALKDEQQR-QQKLMDE 2556
Cdd:PRK03918 328 ERIKE--------------------LEEKE---ERLEELKKKLKELEKRLEEleerheLYEEAKAKKEELERlKKRLTGL 384
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1655220527 2557 EKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEK 2598
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1191-1942 |
6.63e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.67 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1191 RLHSERDAELEhyRQLAGSLLERWQAVFAQIDLRqRELSLLGRHMNSYKQSYEWLIQWL---REARLRQEKIEAAPVwDS 1267
Cdd:PRK04863 282 RVHLEEALELR--RELYTSRRQLAAEQYRLVEMA-RELAELNEAESDLEQDYQAASDHLnlvQTALRQQEKIERYQA-DL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1268 KALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLK----DYE--FQILAYRALQDPIA-SPLKKPK-----MESAS 1335
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqlaDYQqaLDVQQTRAIQYQQAvQALERAKqlcglPDLTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1336 DNI---IQEYVT-----------LRTRYSELSTLTSQYIKfILETQRRLEDD-------EKASEKLKEDEKKRMAEIQAQ 1394
Cdd:PRK04863 438 DNAedwLEEFQAkeqeateellsLEQKLSVAQAAHSQFEQ-AYQLVRKIAGEvsrseawDVARELLRRLREQRHLAEQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1395 lETQKQLAEghaksvAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELtqlknlsEQEIRSKNQQLEEAQVSRR 1474
Cdd:PRK04863 517 -QLRMRLSE------LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEEL-------EARLESLSESVSEARERRM 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1475 KLEEEIHLIRIQLQTTIKQKS---TADDELQKLRDQAAEA----EKVRKAAQEEAERLRK--QVNEETQKKKNA-EDELK 1544
Cdd:PRK04863 583 ALRQQLEQLQARIQRLAARAPawlAAQDALARLREQSGEEfedsQDVTEYMQQLLEREREltVERDELAARKQAlDEEIE 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1545 RKSEAE-KEAARQKQKA----------------LDElqkhkmqAEEAERRLKQAeeekvRQIKVVEEVaqKTAATQLQAM 1607
Cdd:PRK04863 663 RLSQPGgSEDPRLNALAerfggvllseiyddvsLED-------APYFSALYGPA-----RHAIVVPDL--SDAAEQLAGL 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1608 ---------------SFSEKTTKLEEslkKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETwrlkanealrLRLRA 1672
Cdd:PRK04863 729 edcpedlyliegdpdSFDDSVFSVEE---LEKAVVVKIADRQWRYSRFPEVPLFGRAAREKRIEQ----------LRAER 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1673 EEEAQRksLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKqrtfaeqiAQQKLSaEQEyiRLKADFEHAEQQ 1752
Cdd:PRK04863 796 EELAER--YATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEAELRQ--------LNRRRV-ELE--RALADHESQEQQ 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1753 rglLDNELQRLKNEVNAAEK--------QRRQLEDELAKVRSEMDALLqmkiQAEKVSQSNtEKSKQLLETEALKMKQLA 1824
Cdd:PRK04863 863 ---QRSQLEQAKEGLSALNRllprlnllADETLADRVEEIREQLDEAE----EAKRFVQQH-GNALAQLEPIVSVLQSDP 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1825 EEAARLRSVAEEAKKQRQlaedeAARQRAEAEKILKEKLAAineatrLKTEAEVALKAKEAE-NERLKRQAEDEAYQRKL 1903
Cdd:PRK04863 935 EQFEQLKQDYQQAQQTQR-----DAKQQAFALTEVVQRRAH------FSYEDAAEMLAKNSDlNEKLRQRLEQAEQERTR 1003
|
810 820 830
....*....|....*....|....*....|....*....
gi 1655220527 1904 LEDQAAQHKHDIQEKiTQLQSSSVSELDRQKNIVEETLR 1942
Cdd:PRK04863 1004 AREQLRQAQAQLAQY-NQVLASLKSSYDAKRQMLQELKQ 1041
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1495-1945 |
7.71e-09 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 62.38 E-value: 7.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1495 STADDELQkLRDQAAEAEKVRKAAQEEaerlrkqVNEETQKKKNAEDElkRKSEAEKeaARQKQKALDELQKhkMQAEEa 1574
Cdd:PRK10929 20 ATAPDEKQ-ITQELEQAKAAKTPAQAE-------IVEALQSALNWLEE--RKGSLER--AKQYQQVIDNFPK--LSAEL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1575 eRRLKQAEEEKVRQIkvveEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKE 1654
Cdd:PRK10929 85 -RQQLNNERDEPRSV----PPNMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1655 LEtwrlkaneALRLRLRAEEEAQRKSLaQEEAEKQKTEAErdakkkakaeeaalkqkenaekELEkqrtfaeqIAQqkLS 1734
Cdd:PRK10929 160 LQ--------TLGTPNTPLAQAQLTAL-QAESAALKALVD----------------------ELE--------LAQ--LS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1735 A--EQEYIRLKADFEHAEQQRglLDNELQRLKNEVNAaekqRRQLEDELAKVRSEMdallqmkiQAEKVSQSNTEKSKQL 1812
Cdd:PRK10929 199 AnnRQELARLRSELAKKRSQQ--LDAYLQALRNQLNS----QRQREAERALESTEL--------LAEQSGDLPKSIVAQF 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1813 LETEALKMkQLAEEAARLRSVAEeakKQRQLAEDeaARQRAEAEKILKEKL------AAINEATRlkteAEVALKAKEAE 1886
Cdd:PRK10929 265 KINRELSQ-ALNQQAQRMDLIAS---QQRQAASQ--TLQVRQALNTLREQSqwlgvsNALGEALR----AQVARLPEMPK 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1887 NERLKRQAEDEAYQRKLLEDQAAQhkhdiQEKITQLQSSSVSEL-DRQKNIVEETLRQKK 1945
Cdd:PRK10929 335 PQQLDTEMAQLRVQRLRYEDLLNK-----QPQLRQIRQADGQPLtAEQNRILDAQLRTQR 389
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
164-263 |
8.40e-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: 56.23 E-value: 8.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYrQSNQ--ENLEQAFSVAERELGVTRLL 241
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCPDWESW-DPNQpvQNAREAMQQADDWLGVPQVI 86
|
90 100
....*....|....*....|..
gi 1655220527 242 DPEDVDVAHPDEKSIITYVSSL 263
Cdd:cd21314 87 APEEIVDPNVDEHSVMTYLSQF 108
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2308-2504 |
8.45e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.98 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2308 QRKTAEAELAEQRalaekmlKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRldKETQGFQKSLEAER 2387
Cdd:PRK09510 68 QQQQKSAKRAEEQ-------RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAA--KQAALKQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2388 KRQLEisAEAEKLKLRVKELSSAQAKAEEEATRF------KKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDL 2461
Cdd:PRK09510 139 AKAAA--AAKAKAEAEAKRAAAAAKKAAAEAKKKaeaeaaKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1655220527 2462 KKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAML 2504
Cdd:PRK09510 217 KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2178-2419 |
9.26e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 9.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2178 ADAEMAKHKKEAEQALKQKSQVEKelglvklQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELL- 2256
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2257 KLKVRIeeenlRLMQKNKDNTQKLLA-EEAEKMKSLAEEAARLSVEAE---ETARQRKTAEAELAEQRALAEKMLKEKMQ 2332
Cdd:COG3883 87 ELGERA-----RALYRSGGSVSYLDVlLGSESFSDFLDRLSALSKIADadaDLLEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2333 AIQEatkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQA 2412
Cdd:COG3883 162 LKAE---LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
....*..
gi 1655220527 2413 KAEEEAT 2419
Cdd:COG3883 239 AAAAAAS 245
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2122-2482 |
1.04e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 61.45 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2122 LRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKE--------AEQAL 2193
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELsasseelsEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2194 KQKSQVEKELGLVKLQLD-ETDKQKALMDE-ELQRVKAQVNDAVKQKAQVENElskvkmqmDELLKLKVRIEEENLRLMQ 2271
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDiKTLTQRVLEREtELERMKERAKKAGAQRKEEEAE--------RKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2272 KNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKmqaiQEATKLKAEAEELQKQK 2351
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE----RKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2352 NQAQ-EKAKKLLEDKQ-------------EIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEE 2417
Cdd:pfam07888 268 DRTQaELHQARLQAAQltlqladaslalrEGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 2418 ATRFKkqaDEAKVRLQETEkqttetvvqkletqrlqstREADDLKKAIAELEKEREKLKRDAQEL 2482
Cdd:pfam07888 348 LGREK---DCNRVQLSESR-------------------RELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1373-1696 |
1.04e-08 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 61.27 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1373 DEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKsvakaeleAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQ-- 1450
Cdd:pfam03528 3 DEDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAK--------FKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1451 --LKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKqkstaDDELQ---KLRDQAAEAEKVRKAAQEEAERL 1525
Cdd:pfam03528 75 aeMENIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVR-----EYEVQfhrRLEQERAQWNQYRESAEREIADL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1526 RKQVNEeTQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEvAQKTAATQLQ 1605
Cdd:pfam03528 150 RRRLSE-GQEEENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELNHYLE-AEKSCRTDLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1606 AMSFSEKTTKLeeslkkeqgtvlQLQEEAEKLRKQEEEANKAREQAEKE---------------LETWRLKANEALRL-- 1668
Cdd:pfam03528 228 MYVAVLNTQKS------------VLQEDAEKLRKELHEVCHLLEQERQQhnqlkhtwqkandqfLESQRLLMRDMQRMes 295
|
330 340 350
....*....|....*....|....*....|...
gi 1655220527 1669 -----RLRAEEEAQRKSlaQEEAEKQKTEAERD 1696
Cdd:pfam03528 296 vltseQLRQVEEIKKKD--QEEHKRARTHKEKE 326
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2026-2634 |
1.31e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.67 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2026 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAK-EAAQKSTAAEQKAQ------DVLSKNKEDLLSQEK-LRDE 2097
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANsELTEARTERDQFSQesgnldDQLQKLLADLHKREKeLSLE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2098 FENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLK---KAAEDEAAKQAKAQKDAerlrkeaeaeaakraaaeaaaLKQ 2174
Cdd:pfam15921 397 KEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEallKAMKSECQGQMERQMAA---------------------IQG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2175 KQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNdavKQKAQVENELSKVKMQMDE 2254
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIE---ATNAEITKLRSRVDLKLQE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2255 LLKLK--------VRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARlsveaeetarqrkTAEAelaeqralaekM 2326
Cdd:pfam15921 533 LQHLKnegdhlrnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGR-------------TAGA-----------M 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2327 LKEKMQAIQEATKLKAEAEELqkqknqaqekakKLLEDKQEIQQRldketqgfqkSLEAeRKRQLEIsaeaEKLKLrvke 2406
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEF------------KILKDKKDAKIR----------ELEA-RVSDLEL----EKVKL---- 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2407 lssaqAKAEEEATRfkkqadeakvrlqetekqttetVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDaqeLQNKS 2486
Cdd:pfam15921 638 -----VNAGSERLR----------------------AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN---FRNKS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2487 KE---TASAQQEQMEQQKAMLQQTFLTekellLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEkkklqa 2563
Cdd:pfam15921 688 EEmetTTNKLKMQLKSAQSELEQTRNT-----LKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEA------ 756
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 2564 iMDEAvkkqkeaeaemkNKQKEMEALEKKRLEQE-KLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDK 2634
Cdd:pfam15921 757 -MTNA------------NKEKHFLKEEKNKLSQElSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1365-1695 |
1.32e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 61.04 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1365 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEghaksvakaelEAQELKLKMKEdasqrqglavdaekQKQNI 1444
Cdd:pfam02029 53 SGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDP-----------TIADEKESVAE--------------RKENN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1445 QLEltqlknlseqeirSKNQQLEEAQVSRRKLEEEIHliriqlQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAER 1524
Cdd:pfam02029 108 EEE-------------ENSSWEKEEKRDSRLGRYKEE------ETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1525 LRKQV-NEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQkhkmQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAAtq 1603
Cdd:pfam02029 169 VPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQ----NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEV-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1604 lqamsFSEKTTKLEESLKKEQGTVlqlQEEAEKLRKQEEEANKAREQAEKELEtWRLKANEALRLRlRAEEEAQRKSLAQ 1683
Cdd:pfam02029 243 -----FLEAEQKLEELRRRRQEKE---SEEFEKLRQKQQEAELELEELKKKRE-ERRKLLEEEEQR-RKQEEAERKLREE 312
|
330
....*....|..
gi 1655220527 1684 EEAEKQKTEAER 1695
Cdd:pfam02029 313 EEKRRMKEEIER 324
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1496-1735 |
1.39e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1496 TADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAE 1575
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1576 RRLKQAEeekvRQIKVVEEVAQ----KTAATQLQAMS-FSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQ 1650
Cdd:COG3883 93 RALYRSG----GSVSYLDVLLGsesfSDFLDRLSALSkIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1651 AEKELETwRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQ 1730
Cdd:COG3883 169 AKAELEA-QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
....*
gi 1655220527 1731 QKLSA 1735
Cdd:COG3883 248 GAGAA 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2281-2663 |
1.50e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.28 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2281 LAEEAEKMKSLaeeaaRLSVEAEetarqRKTAEAELAEQRALAEKMLK--EKMQAIQEATKLKAEaEELQKQKNQAQEK- 2357
Cdd:pfam05483 83 LYKEAEKIKKW-----KVSIEAE-----LKQKENKLQENRKIIEAQRKaiQELQFENEKVSLKLE-EEIQENKDLIKENn 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2358 -AKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSsAQAKAEEEATRFKKQADEAKVR-LQET 2435
Cdd:pfam05483 152 aTRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELR-VQAENARLEMHFKLKEDHEKIQhLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2436 EKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKR--DAQELQNKSKETASAQQE----QMEQQKAMLQQTFL 2509
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQleEKTKLQDENLKELIEKKDhltkELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2510 TEKELllkrERDVEDEKKKLQKHLED------EVNKAKA-------------------LKDEQQRQQKLMDEekkkLQAI 2564
Cdd:pfam05483 311 TQKAL----EEDLQIATKTICQLTEEkeaqmeELNKAKAahsfvvtefeattcsleelLRTEQQRLEKNEDQ----LKII 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2565 MDEAVKKQKEAEAEMKNKQ-KEMEALE-KKRLEQEKLLADENKKLREKLESLEVTSKQAAS--KTKEIEVQtdkvpeEQL 2640
Cdd:pfam05483 383 TMELQKKSSELEEMTKFKNnKEVELEElKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFllQAREKEIH------DLE 456
|
410 420
....*....|....*....|...
gi 1655220527 2641 VSMTTVETTKKVFNGSVEAVKKD 2663
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTE 479
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1544-1977 |
1.54e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1544 KRKSEAEKEAARQKQKALDELqkhkmqaEEAERRLKQAEEEKVRQIKVVEEVAQKTAatQLQAMSFSEKTTKLEESLKKE 1623
Cdd:COG4717 53 KEADELFKPQGRKPELNLKEL-------KELEEELKEAEEKEEEYAELQEELEELEE--ELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1624 QGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRlkanealrlRLRAEEEAQRKSLAQEEAEKQKTEAERDAKkkaka 1703
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELR---------ELEEELEELEAELAELQEELEELLEQLSLA----- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1704 eeaalkqkenAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQR--------- 1774
Cdd:COG4717 190 ----------TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaall 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1775 --RQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQR 1852
Cdd:COG4717 260 alLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1853 AEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEA--YQRKLLEDQAAQHKHDIQEKITQLQSSSVSEL 1930
Cdd:COG4717 340 LELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelRAALEQAEEYQELKEELEELEEQLEELLGELE 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1655220527 1931 DRQKNIVEETLRQK-KVVEEEIHIIRINFERASKEKSDLEVELKKLKG 1977
Cdd:COG4717 420 ELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEE 467
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1157-1586 |
1.67e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1157 QLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQL--AGSLLERWQAVFAQIDLRQRELSLLGRH 1234
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1235 MNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKdyefQILA 1314
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE----EELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1315 YRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFI-----------LETQRRLEDDEKASEKLKED 1383
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallfLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1384 EKKRM---AEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKnlSEQEIR 1460
Cdd:COG4717 311 PALEEleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE--DEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1461 SKNQQLEEaqvsRRKLEEEIHLIRIQLQTTIKQKSTADDELQK--LRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKN 1538
Cdd:COG4717 389 AALEQAEE----YQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1539 AE--DELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKV 1586
Cdd:COG4717 465 LEedGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
168-263 |
1.74e-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: 56.16 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 168 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ-----------------------EN 223
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 224 LEQAFSVAER-----------ELG-VTRLLDPEDVDVAHPDEKSIITYVSSL 263
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
39-145 |
1.76e-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: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 39 KTFTKWVNKHLMKA--QRHITDLYEDLRDGHNLISLLEVLSGETLPRERDLvrnvrlPREKGRMrfhkLQNVQIALDFLK 116
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGC------PRSQSQM----IENVDVCLSFLA 72
|
90 100
....*....|....*....|....*....
gi 1655220527 117 HRQVKLVNIRNDDIADGNPKLTLGLIWTI 145
Cdd:cd21286 73 ARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2172-2506 |
1.82e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.12 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2172 LKQKQEADAEMAKHKKEAEQalkQKSQVEKELGLVKLQLdeTDKQKALmdEELQRVKAQVNDAVKQKAQVENELskvkmQ 2251
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEA---RLEAAEEEVDSLKSQL--ADYQQAL--DVQQTRAIQYQQAVQALEKARALC-----G 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2252 MDELlklkvriEEENLrlmqknKDNTQKLLAEEAEKMKSLAEEAARLSVeAEETARQRktaEAELAEQRALAEKMlkEKM 2331
Cdd:COG3096 431 LPDL-------TPENA------EDYLAAFRAKEQQATEEVLELEQKLSV-ADAARRQF---EKAYELVCKIAGEV--ERS 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2332 QAIQEATKLKAEAEELQKQKNQAQEKAKKL--LEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSS 2409
Cdd:COG3096 492 QAWQTARELLRRYRSQQALAQRLQQLRAQLaeLEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2410 AQAKAEEEATRFKKQADEAKVRLQETEKQ-----TTETVVQKLETQRLQSTREADDLKKAIAE-LEKEREkLKRDAQELQ 2483
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAARapawlAAQDALERLREQSGEALADSQEVTAAMQQlLERERE-ATVERDELA 650
|
330 340
....*....|....*....|...
gi 1655220527 2484 nksketasAQQEQMEQQKAMLQQ 2506
Cdd:COG3096 651 --------ARKQALESQIERLSQ 665
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2245-2642 |
1.99e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2245 LSKVKMQMDELLKLKVRIEEENLRLMQKNkdntQKLLAEEAEKMKSLAEEAARLsveaEETARQRKTAEAELAEQRALae 2324
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREE-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2325 kmlKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRV 2404
Cdd:COG4717 118 ---LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2405 KELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIA------------------ 2466
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllslilt 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2467 -----------------ELEKEREKLKRDAQELQNKSKETASAQQEQMEQ----------QKAMLQQTFLTEKELLLKRE 2519
Cdd:COG4717 275 iagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELlaalglppdlSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2520 RDVEDEKKKLQKHLEDEVN---KAKALKDEQQRQQKLMDEEKKKlqaimdEAVKKQKEAEAEMKNKQKEMEALEKKRLEQ 2596
Cdd:COG4717 355 EAEELEEELQLEELEQEIAallAEAGVEDEEELRAALEQAEEYQ------ELKEELEELEEQLEELLGELEELLEALDEE 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1655220527 2597 EklLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVS 2642
Cdd:COG4717 429 E--LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELA 472
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2263-2535 |
2.81e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 59.88 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2263 EEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEaTKLKA 2342
Cdd:pfam02029 61 EEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETE-IREKE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2343 EAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFK 2422
Cdd:pfam02029 140 YQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2423 KQADEAKVRLQETEKQTTETVVQKLET-QRLQSTREADDlKKAIAELEKEREKLKRDAQELQ---NKSKETASAQQEQME 2498
Cdd:pfam02029 220 KVTTKRRQGGLSQSQEREEEAEVFLEAeQKLEELRRRRQ-EKESEEFEKLRQKQQEAELELEelkKKREERRKLLEEEEQ 298
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1655220527 2499 QQKAMLQQTFLTEKELLLKRERDVEDEK----KKLQKHLED 2535
Cdd:pfam02029 299 RRKQEEAERKLREEEEKRRMKEEIERRRaeaaEKRQKLPED 339
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1173-1619 |
2.91e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1173 DRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREA 1252
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1253 RLRQEKieaapvwdsKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQIlaYRALQDPiasplkKPKME 1332
Cdd:COG4717 129 PLYQEL---------EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL--EELLEQL------SLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1333 SASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKA 1412
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1413 ELEAQEL------------------KLKMKEDASQRQGLAVDAEKQKQNIQLELTQL---KNLSEQEIRSKNQQLEEAQV 1471
Cdd:COG4717 272 ILTIAGVlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1472 SRRKLEEEIHLIRIQ-LQTTIKQ-----KSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE-----ETQKKKNAE 1540
Cdd:COG4717 352 LLREAEELEEELQLEeLEQEIAAllaeaGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEleellEALDEEELE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1541 DELKRKSEAEKEAARQKQKALDELQ--KHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEE 1618
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAelEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
.
gi 1655220527 1619 S 1619
Cdd:COG4717 512 E 512
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2026-2376 |
3.70e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 59.52 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2026 RQRKAAQDEVERLKqkaAEANKLKDKAEKELEKQvilakEAAQKSTAAEQKAQDVLSKNKEDllSQEKLRDEFENAKKLA 2105
Cdd:pfam07888 73 RQRRELESRVAELK---EELRQSREKHEELEEKY-----KELSASSEELSEEKDALLAQRAA--HEARIRELEEDIKTLT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2106 QAAETAKEKAEKeaalLRQKAEEAEKLKKAAEDE-AAKQAKAQKDAERLRKEAE--AEAAKRAAAEAAALKQKQEADAEM 2182
Cdd:pfam07888 143 QRVLERETELER----MKERAKKAGAQRKEEEAErKQLQAKLQQTEEELRSLSKefQELRNSLAQRDTQVLQLQDTITTL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2183 AKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQ-------RVKAQVNDAVKQKAQVENELSKVKMQMDEL 2255
Cdd:pfam07888 219 TQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSsmaaqrdRTQAELHQARLQAAQLTLQLADASLALREG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2256 lKLKVRIEEENLRL-MQKNKDNTQKLLAEEAEKMKSLAEEAArlsveaeetarQRKTAEAELAEQRALAEKMLKEKMQAI 2334
Cdd:pfam07888 299 -RARWAQERETLQQsAEADKDRIEKLSAELQRLEERLQEERM-----------EREKLEVELGREKDCNRVQLSESRREL 366
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1655220527 2335 QEatkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKET 2376
Cdd:pfam07888 367 QE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1614-1975 |
3.80e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 59.52 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1614 TKLEESLKkEQGTVLQLQEEAEKLRKQEeeankaREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEA 1693
Cdd:pfam07888 34 NRLEECLQ-ERAELLQAQEAANRQREKE------KERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1694 ERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQ 1773
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1774 RRQLEDELAKVRSEMD----ALLQMKIQAEKVSQSNTEKSKQLLETEALK--MKQLAEEAARLRSVAEEAKkqRQLAEDE 1847
Cdd:pfam07888 187 LRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLeeLRSLQERLNASERKVEGLG--EELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1848 AARQRAEAEkILKEKLAAINEATRLkTEAEVALKAKEA----ENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQ 1923
Cdd:pfam07888 265 AQRDRTQAE-LHQARLQAAQLTLQL-ADASLALREGRArwaqERETLQQSAEADKDRIEKLSAELQRLEERLQEERMERE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 1924 SSSVsELDRQKNIveeTLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKL 1975
Cdd:pfam07888 343 KLEV-ELGREKDC---NRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1057-1582 |
4.51e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.92 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1057 SELEGLKKDLNSITEKTEEIlaspqqSSSAPMLRSELDVTLKKMDHVYGLSSVYLDKLKTIDIVIRNTKDAEDTVKSYES 1136
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENI------KKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYES 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1137 RLR--DVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKmTRLHSERDAELEHYRQlAGSLLERW 1214
Cdd:PRK01156 257 EIKtaESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENK-KQILSNIDAEINKYHA-IIKKLSVL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1215 QAVFAQIDLRQRE--------LSLLGRHMN--SYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLTQEKKLLEEI 1284
Cdd:PRK01156 335 QKDYNDYIKKKSRyddlnnqiLELEGYEMDynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1285 EKNKDQIENCQKDAKAYIDSLKDYEFQILAYRA-LQDPIASPLKKPKM-ESASDNIIQEYVTLRTRyselstltsqyikf 1362
Cdd:PRK01156 415 NVKLQDISSKVSSLNQRIRALRENLDELSRNMEmLNGQSVCPVCGTTLgEEKSNHIINHYNEKKSR-------------- 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1363 ILETQRRLEDDEKASEKLKEDEKKRMAEIQAQlETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDaekqkq 1442
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEYLESE-EINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKN------ 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1443 niqleltQLKNLSEQEIRSKNQQLEEAQVSRRKLeeEIHLIRIQLQTTIKQKSTADDELQKLR----DQAAEAEKVRKAA 1518
Cdd:PRK01156 554 -------RYKSLKLEDLDSKRTSWLNALAVISLI--DIETNRSRSNEIKKQLNDLESRLQEIEigfpDDKSYIDKSIREI 624
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 1519 QEEAERLRKQVNeETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAE 1582
Cdd:PRK01156 625 ENEANNLNNKYN-EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSR 687
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1762-2443 |
4.76e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.65 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1762 RLKNEVNAAEKQRRQLEDELAKVRSEM--------DALLQMKIQAEKVSQSNTE------KSKQL---LETEALKMKQLA 1824
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELknkekelkNLDKNLNKDEEKINNSNNKikileqQIKDLndkLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1825 EEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEaevaLKAKEAENERLKRQAEDEAYQRKLL 1904
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKKQKEELENELNLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1905 EDQaaqhKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFErASKEKSDLEVELKKLKGIADETQK 1984
Cdd:TIGR04523 179 EKE----KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQ-LKDNIEKKQQEINEKTTEISNTQT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1985 skakaeeeaeklkklaaeeerkrreaeeKVKKIAAAEEEAARQRKAAQDEVERLKQKAaeanklkdkaeKELEKQviLAK 2064
Cdd:TIGR04523 254 ----------------------------QLNQLKDEQNKIKKQLSEKQKELEQNNKKI-----------KELEKQ--LNQ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2065 EAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENA---------------KKLAQAAETAKEKAEKEAALLRQKAEEA 2129
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisqnnkiisqlneqiSQLKKELTNSESENSEKQRELEEKQNEI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2130 EKLKKAAED--EAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQ-KQEADAEMAKHKKEAEQALKQKSQVEKELGLV 2206
Cdd:TIGR04523 373 EKLKKENQSykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQeKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2207 KLQLDETDKQKALMDEELQRVKAQVNdavKQKAQVENELSKVKMQMDELLKLKvrieEENLRLMQKNKDNTQkllaeeae 2286
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSIN---KIKQNLEQKQKELKSKEKELKKLN----EEKKELEEKVKDLTK-------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2287 KMKSLAEEAARLSVEAEETARQRKTAEAELAE--QRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLED 2364
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2365 KQEIQQRLDKETQgfqksLEAERKRQLE-ISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETV 2443
Cdd:TIGR04523 598 KKDLIKEIEEKEK-----KISSLEKELEkAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESK 672
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2317-2542 |
4.77e-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: 58.62 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2317 AEQRALAEKMLKEKMQAIQEATK----LKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgFQKSLEAERKRQLE 2392
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKelaaLKKEEKALLKQLAALERRIAALARRIRALEQELAA----LEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2393 ISAEAEKLKLRVKE-LSSAQAKAEEEATRFKKQADEAK--VRLQETEKQTTETVVQKLETQRlqstREADDLKKAIAELE 2469
Cdd:COG4942 95 LRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLdaVRRLQYLKYLAPARREQAEELR----ADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 2470 KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKEL--LLKRERDVEDEKKKLQKHLEDEVNKAKA 2542
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELaeLQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1560-2153 |
5.13e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1560 ALDELQKHKMQAEEAERRLKQAEEeKVRQIKVVEEVAQKTAATQLQAmsfsektTKLEESlkKEQGTVLQLQEEAEKLRK 1639
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDARE-QIELLEPIRELAERYAAARERL-------AELEYL--RAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1640 QEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQ-EEAEKQKTEAERdakkkakaeeaalkQKENAEKEL 1718
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLER--------------ELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1719 EKQRTFAEQIAQQKLSAEQEYIRLKADfehAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmkiqa 1798
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER----- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1799 ekvSQSN-TEKSKQLLEteALKmKQLAEEAARLRSVAEEAkkqrQLAEDEAARQRAeAEKIL--------------KEKL 1863
Cdd:COG4913 434 ---RKSNiPARLLALRD--ALA-EALGLDEAELPFVGELI----EVRPEEERWRGA-IERVLggfaltllvppehyAAAL 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1864 AAINeATRLKTEAeVALKAKEAENERLKRQAEDEAYQRKL----------LEDQAAQHKHDIQ-EKITQL---------- 1922
Cdd:COG4913 503 RWVN-RLHLRGRL-VYERVRTGLPDPERPRLDPDSLAGKLdfkphpfrawLEAELGRRFDYVCvDSPEELrrhpraitra 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1923 ----QSSSVSELDRQKNIVEE------TLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEE 1992
Cdd:COG4913 581 gqvkGNGTRHEKDDRRRIRSRyvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1993 AEKLKKLaaeeerkrreaeekvkkiaaaeeeaaRQRKAAQDEVERLKqkaaEANKLKDKAEKELEKQVILAKEAAQKSTA 2072
Cdd:COG4913 661 IDVASAE--------------------------REIAELEAELERLD----ASSDDLAALEEQLEELEAELEELEEELDE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2073 AEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEE-AEKLKKAAEDEAAKQAKAQKDAE 2151
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElRENLEERIDALRARLNRAEEELE 790
|
..
gi 1655220527 2152 RL 2153
Cdd:COG4913 791 RA 792
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2184-2478 |
5.33e-08 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 58.28 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2184 KHKKEAEQALKQKSQvEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQK-------AQVENELSKVKmQMDELL 2256
Cdd:pfam15905 64 KSQKNLKESKDQKEL-EKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKtslsasvASLEKQLLELT-RVNELL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2257 KLKVrieeenlrlmqkNKDNTQKllaeeaeKMKSLAEEAARLsveaeetarqRKTAEAELAEQRALAEKMLKeKMQAIQe 2336
Cdd:pfam15905 142 KAKF------------SEDGTQK-------KMSSLSMELMKL----------RNKLEAKMKEVMAKQEGMEG-KLQVTQ- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2337 aTKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAErKRQLEISAEAEKLKLRVKELSSAQAKAEE 2416
Cdd:pfam15905 191 -KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVE-KYKLDIAQLEELLKEKNDEIESLKQSLEE 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 2417 EATRFKKQADEAKVRLQETEKQtTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRD 2478
Cdd:pfam15905 269 KEQELSKQIKDLNEKCKLLESE-KEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1341-1831 |
5.51e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 59.45 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1341 EYVTLRTRyseLSTLTSQYikfiletqrrlEDDEKASEKLKED---EKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQ 1417
Cdd:pfam10174 304 ELLALQTK---LETLTNQN-----------SDCKQHIEVLKESltaKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1418 ELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQeIRSKNQQLEEAQVSRRKLEEEihliriqlqttikqKSTA 1497
Cdd:pfam10174 370 DLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQ-LRDKDKQLAGLKERVKSLQTD--------------SSNT 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1498 DDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKmqAEEAERR 1577
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHA--SSLASSG 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1578 LKQAEEEKVRQIkvveEVAQKTaatqlqamsfsEKTTKLEESLKKEQGTVLQLQ---EEAEKLRKQEEEANKAREQAEK- 1653
Cdd:pfam10174 513 LKKDSKLKSLEI----AVEQKK-----------EECSKLENQLKKAHNAEEAVRtnpEINDRIRLLEQEVARYKEESGKa 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1654 ELETWRLKanEALRlRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEkELEKQRTfaEQIAQQKL 1733
Cdd:pfam10174 578 QAEVERLL--GILR-EVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQ-LLEEARR--REDNLADN 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1734 SAEQEYIRLKADFEHAEQQrglLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLL 1813
Cdd:pfam10174 652 SQQLQLEELMGALEKTRQE---LDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAISEKDANIALL 728
|
490
....*....|....*...
gi 1655220527 1814 ETEALKMKQLAEEAARLR 1831
Cdd:pfam10174 729 ELSSSKKKKTQEEVMALK 746
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1516-1702 |
6.12e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.28 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1516 KAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKaldelqkhkmQAEEAERRLKQAEEEKVRQIKVVEEV 1595
Cdd:PRK09510 75 KRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK----------QAEEAAKQAALKQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1596 AQKTAATQlqAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEA-NKAREQAEKELETwRLKANEALRLRLRAEE 1674
Cdd:PRK09510 145 AKAKAEAE--AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAaAKAAAEAKKKAEA-EAKKKAAAEAKKKAAA 221
|
170 180
....*....|....*....|....*...
gi 1655220527 1675 EAQRKSLAQEEAEKQKTEAERDAKKKAK 1702
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEK 249
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2027-2508 |
6.13e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2027 QRKAAQDEVERLKQKAAEANKLKDKAEkELEKQvilaKEAAQkstAAEQKAQDVLSKNKEDLLSQEKLRDEFEnakKLAQ 2106
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIE-RYEEQ----REQAR---ETRDEADEVLEEHEERREELETLEAEIE---DLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2107 AAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADA------ 2180
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAhneeae 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2181 ----EMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELl 2256
Cdd:PRK02224 346 slreDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2257 KLKVRIEEENLRLMQKNKDNTQKLLA-----------EEAEKMKSLAE--------EAARLSVEAEETARQRKTAEAE-- 2315
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEagkcpecgqpvEGSPHVETIEEdrerveelEAELEDLEEEVEEVEERLERAEdl 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2316 ---------LAEQRALAEKMLKEKMQAIQE-----------ATKLKAEAEELQKQKNQAQEKAKKLLE-------DKQEI 2368
Cdd:PRK02224 505 veaedrierLEERREDLEELIAERRETIEEkreraeelrerAAELEAEAEEKREAAAEAEEEAEEAREevaelnsKLAEL 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2369 QQRLDketqgfqkSLEAERKRQLEIsAEAEKLKLRVKELSSAQAKAEEE------ATRFKKQADEAKV---RLQE--TEK 2437
Cdd:PRK02224 585 KERIE--------SLERIRTLLAAI-ADAEDEIERLREKREALAELNDErrerlaEKRERKRELEAEFdeaRIEEarEDK 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2438 QTTETVVQKLETQRLQSTREADDLKKAI-------AELEKEREKLKR-------------DAQELQNKSKET-ASAQQEQ 2496
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIgavenelEELEELRERREAlenrvealealydEAEELESMYGDLrAELRQRN 735
|
570
....*....|..
gi 1655220527 2497 MEQQKAMLQQTF 2508
Cdd:PRK02224 736 VETLERMLNETF 747
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4060-4096 |
6.40e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 51.33 E-value: 6.40e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1655220527 4060 IRLLEAQIATGGIIDPQESHRLPVETAYERGLFDEEM 4096
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1716-2152 |
6.88e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1716 KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAE--KQRRQLEDELAKVRSEMDALLQ 1793
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1794 mkiqaekvsqsntekskqlletealKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLK 1873
Cdd:COG4717 154 -------------------------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1874 TEAEVALKAKEAENERLKRQAEDEayqRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHI 1953
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQL---ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1954 IRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQD 2033
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2034 EvERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEdLLSQEKLRDEFENAKKLAQAAETAKE 2113
Cdd:COG4717 366 E-ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGE-LEELLEALDEEELEEELEELEEELEE 443
|
410 420 430
....*....|....*....|....*....|....*....
gi 1655220527 2114 KAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAER 2152
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQELEELK 482
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2222-2614 |
7.26e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 59.30 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2222 EELQRVKAQVNDAvkQKAQVEnELSKVKMQMDELLKLKVRIEEenlrlMQKNKDNTQKLLAEEAEKMKSLAEEaaRLSVE 2301
Cdd:PRK10929 30 QELEQAKAAKTPA--QAEIVE-ALQSALNWLEERKGSLERAKQ-----YQQVIDNFPKLSAELRQQLNNERDE--PRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2302 AEETArqrktaeAELaEQRAL--AEKMLKEKMQAIQEATKLKAEAEELQkQKNQAQEKAKKLLedkQEIQQRLdkETQGF 2379
Cdd:PRK10929 100 PNMST-------DAL-EQEILqvSSQLLEKSRQAQQEQDRAREISDSLS-QLPQQQTEARRQL---NEIERRL--QTLGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2380 QKSLEAERKRQLeISAEAEKLKLRVKELSSAQAKA--EEEATR-----FKKQADEAKVRLQETEKQTTETVVQKLEtQRL 2452
Cdd:PRK10929 166 PNTPLAQAQLTA-LQAESAALKALVDELELAQLSAnnRQELARlrselAKKRSQQLDAYLQALRNQLNSQRQREAE-RAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2453 QSTR----EADDLKKAI-AELEKERE---KLKRDAQELqnkskETASAQQEQMEQQKAMLQQTFLTekellLKRERDVED 2524
Cdd:PRK10929 244 ESTEllaeQSGDLPKSIvAQFKINRElsqALNQQAQRM-----DLIASQQRQAASQTLQVRQALNT-----LREQSQWLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2525 EKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQaiMDEAVKKQKEaeaEMKNKQKEMEALEKkrlEQEKLLADEN 2604
Cdd:PRK10929 314 VSNALGEALRAQVARLPEMPKPQQLDTEMAQLRVQRLR--YEDLLNKQPQ---LRQIRQADGQPLTA---EQNRILDAQL 385
|
410
....*....|
gi 1655220527 2605 KKLREKLESL 2614
Cdd:PRK10929 386 RTQRELLNSL 395
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1604-1850 |
7.65e-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: 57.85 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1604 LQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwrlKANEALRlRLRAEEEAQRKSLAQ 1683
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA----ALARRIR-ALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1684 EEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELE---KQRTFAEqiAQQKLSAEQEYIRlkADFEHAEQQRGLLDnEL 1760
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllSPEDFLD--AVRRLQYLKYLAP--ARREQAEELRADLA-EL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1761 QRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQ 1840
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|
gi 1655220527 1841 RQLAEDEAAR 1850
Cdd:COG4942 243 TPAAGFAALK 252
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
159-263 |
7.87e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 53.56 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 159 QSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALL-DMSQVYRQSNQENLEQAFSVAERELGV 237
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*...
gi 1655220527 238 TRLLDPEDVdvAHPD--EKSIITYVSSL 263
Cdd:cd21313 80 PQVITPEEI--IHPDvdEHSVMTYLSQF 105
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2049-2490 |
8.22e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2049 KDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKlaqaaetakekaekEAALLRQKAEE 2128
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA--------------ELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2129 AEKLKKAAEDEAAKQAKAQKDAErlRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKS-QVEKELGLVK 2207
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAELAE--LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2208 LQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQmDELLKLKVRIEEENLRL----MQKNKDNTQKLLAE 2283
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAAALLallgLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2284 EAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQA--------IQEATKLKAEAEELQKQKNQAQ 2355
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlsPEELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2356 EKAKKLleDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVrlqET 2435
Cdd:COG4717 358 ELEEEL--QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL---EE 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220527 2436 EKQTTETVVQKLETQRLQSTREADDLKKAIAELEKERE--KLKRDAQELQNKSKETA 2490
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELA 489
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1502-1695 |
8.33e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 58.25 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1502 QKLRDQAAEAEKVRKAAQEEAERLRKQvneetqKKKNAEDE-LKRKSEAEKEAARQKQkaldELQKhkmqaeeAERRLKQ 1580
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKE------ALLEAKEEiHKLRNEFEKELRERRN----ELQK-------LEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1581 AEEEKVRQikvveevaqktaatqlqamsfSEKTTKLEESLKKEQGTVLQLQEEAEklrKQEEEANKAREQAEKELETW-R 1659
Cdd:PRK12704 94 KEENLDRK---------------------LELLEKREEELEKKEKELEQKQQELE---KKEEELEELIEEQLQELERIsG 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 1655220527 1660 LKANEA---LRLRLRAEEEAQRKSLAQEEAEKQKTEAER 1695
Cdd:PRK12704 150 LTAEEAkeiLLEKVEEEARHEAAVLIKEIEEEAKEEADK 188
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
37-148 |
8.81e-08 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 53.27 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 37 QKKTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRERDLVRNVRLPrekgrmrFHKLQNVQIALDFLK 116
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKPPIKMP-------FKKVENCNQVVKIGK 75
|
90 100 110
....*....|....*....|....*....|..
gi 1655220527 117 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 148
Cdd:cd21299 76 QLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1429-1627 |
8.91e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.89 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1429 QRQGLAVDAEKQKQNIQleltqlknlsEQEIRSKNQQLEEAQVSRRKLEEEihliRIQLQTTIKQKSTADDELQKLRDQA 1508
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKE----------QQQAEELQQKQAAEQERLKQLEKE----RLAAQEQKKQAEEAAKQAALKQKQA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1509 AEAEKV-----RKAAQEEAERLR---KQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQ 1580
Cdd:PRK09510 135 EEAAAKaaaaaKAKAEAEAKRAAaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAE 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1655220527 1581 AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEEslKKEQGTV 1627
Cdd:PRK09510 215 AKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA--AKAAAEV 259
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1488-1859 |
8.94e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 8.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1488 QTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQvneetqkkKNAEDELKRKSEAEKEAArQKQKALDELQKH 1567
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQER--------REALQRLAEYSWDEIDVA-SAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1568 KMQAEEAERRLKQAEEekvrqikvveevaqktaatQLQAmsfsekttkLEESLKKEQGTVLQLQEEAEKLRKQEEEANKA 1647
Cdd:COG4913 677 LERLDASSDDLAALEE-------------------QLEE---------LEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1648 REQAEKELETWRLKANEALRLRLraeeEAQRKSLAQEEAEKQKTEAERDakkkakAEEAALKQKENAEKELEKQRT---- 1723
Cdd:COG4913 729 LDELQDRLEAAEDLARLELRALL----EERFAAALGDAVERELRENLEE------RIDALRARLNRAEEELERAMRafnr 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1724 ---FAEQIAQQKLSAEQEYIRL------------KADFEHA--EQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRS 1786
Cdd:COG4913 799 ewpAETADLDADLESLPEYLALldrleedglpeyEERFKELlnENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIPF 878
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 1787 EMDALLQMKIQAEKVSQSNTEKSkqlletealKMKQLAEEAARLRSVAEEAKKQR------QLAEDEAARQRAEAEKIL 1859
Cdd:COG4913 879 GPGRYLRLEARPRPDPEVREFRQ---------ELRAVTSGASLFDEELSEARFAAlkrlieRLRSEEEESDRRWRARVL 948
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1506-1860 |
9.76e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 58.34 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1506 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQ--KHKMQAEEaERRLKQAEE 1583
Cdd:pfam02029 3 DEEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEafLDRTAKRE-ERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1584 EKVRQIKVVEEVAQKTAATQLQAMsfSEKTTKLEESLKKEQ-GTVLQLQEEAEKLRKQEEEANKAREQAEKeletwrlka 1662
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAERKE--NNEEEENSSWEKEEKrDSRLGRYKEEETEIREKEYQENKWSTEVR--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1663 nealrlrlRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKlsaeqEYIRL 1742
Cdd:pfam02029 151 --------QAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNG-----EEEVT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1743 KADFEHAEQQRGLLDNELQRLKNEV-----NAAEKQRRQLEDelaKVRSEMDALLQMKIQAEKVSQSNTEKSKQ---LLE 1814
Cdd:pfam02029 218 KLKVTTKRRQGGLSQSQEREEEAEVfleaeQKLEELRRRRQE---KESEEFEKLRQKQQEAELELEELKKKREErrkLLE 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1655220527 1815 TEALKMKQlaEEAARLRSVAEEAKKQRQlaedEAARQRAEA-EKILK 1860
Cdd:pfam02029 295 EEEQRRKQ--EEAERKLREEEEKRRMKE----EIERRRAEAaEKRQK 335
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2221-2440 |
9.98e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2221 DEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEEnLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSV 2300
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2301 EAEETARQRKTAEA--------ELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRL 2372
Cdd:COG3883 94 ALYRSGGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 2373 DK---ETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTT 2440
Cdd:COG3883 174 EAqqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1465-1695 |
1.05e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 58.04 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1465 QLEEAQVSRRKLEEEIHLIRiqlQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQE-------EAERLRKQ-VNEETQKK 1536
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMR---RLEVERKRREQEEQRRLQQEQLERAEKMREELEleqqrrfEEIRLRKQrLEEERQRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1537 KNAEDELKRKSEAEKEAARQKQ----KALDELQKHKMQaEEAERrlkqAEEEKVRQikvveevaqktaatqlqamsfsek 1612
Cdd:pfam15709 404 EEEERKQRLQLQAAQERARQQQeefrRKLQELQRKKQQ-EEAER----AEAEKQRQ------------------------ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1613 tTKLEESLKKEQGTVLQLQEEA--EKLRKQEEEANKAREQAEKeletwrlkanealrlRLRAEEEAQRksLAQEEAEKQK 1690
Cdd:pfam15709 455 -KELEMQLAEEQKRLMEMAEEErlEYQRQKQEAEEKARLEAEE---------------RRQKEEEAAR--LALEEAMKQA 516
|
....*
gi 1655220527 1691 TEAER 1695
Cdd:pfam15709 517 QEQAR 521
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2341-2592 |
1.09e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.42 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2341 KAEAEELQKQKNQAqEKAKKLLEDKQeiqQRLDKEtqgfqkslEAERKRQLEISAEAeklklRVKELSSAQAKAEEEATR 2420
Cdd:PRK05035 435 KAEIRAIEQEKKKA-EEAKARFEARQ---ARLERE--------KAAREARHKKAAEA-----RAAKDKDAVAAALARVKA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2421 FKKQADEAKVRLQETEKQTTETV-------VQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETA--- 2490
Cdd:PRK05035 498 KKAAATQPIVIKAGARPDNSAVIaarearkAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEvdp 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2491 --SAQQEQMEQQKAMLQQTFLTEKElllKRERDVEDEKKKLQkhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEA 2568
Cdd:PRK05035 578 kkAAVAAAIARAKAKKAAQQAASAE---PEEQVAEVDPKKAA--VAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI 652
|
250 260
....*....|....*....|....*
gi 1655220527 2569 VK-KQKEAEAEMKNKQKEMEALEKK 2592
Cdd:PRK05035 653 ARaKARKAAQQQANAEPEEAEDPKK 677
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1268-1815 |
1.11e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1268 KALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDPIASPLKKPKMESASDNIIqeYVTLRT 1347
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL--LSNLKK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1348 RYSELSTLTSQYIKFIlETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEda 1427
Cdd:TIGR04523 209 KIQKNKSLESQISELK-KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE-- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1428 sqrqglavdAEKQKQNIQLELTQLKNLSEQ--------EIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADD 1499
Cdd:TIGR04523 286 ---------LEKQLNQLKSEISDLNNQKEQdwnkelksELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1500 ELQKLRDQAAEA----EKVRKAAQ---EEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAE 1572
Cdd:TIGR04523 357 ENSEKQRELEEKqneiEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1573 EAERRLKQAEEEKVRQIKVVEEVAQKTAatqlqamSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAE 1652
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRE-------SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1653 KELETwrlkanealrlrLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRtfaEQIAQQK 1732
Cdd:TIGR04523 510 EKVKD------------LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN---KEIEELK 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1733 lsaeQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQL 1812
Cdd:TIGR04523 575 ----QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
|
...
gi 1655220527 1813 LET 1815
Cdd:TIGR04523 651 KET 653
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1407-1984 |
1.11e-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: 58.22 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1407 KSVAKAELEAQELKLKMKED--ASQRQGLAvdaekqKQNIQLELTQLKNLSEQ-EIRSKnqQLEEAqvsrRKLEEEIHLI 1483
Cdd:pfam07111 18 QDVLERRLDTQRPTVTMWEQdvSGDGQGPG------RRGRSLELEGSQALSQQaELISR--QLQEL----RRLEEEVRLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1484 RiqlQTTIKQKstaddelQKLRDQAAEAEKV---RKAAQEEAERLR-----------------------------KQVNE 1531
Cdd:pfam07111 86 R---ETSLQQK-------MRLEAQAMELDALavaEKAGQAEAEGLRaalagaemvrknleegsqreleeiqrlhqEQLSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1532 ETQKKKNAEDELKRKSEA-EKEAARQKQKALDELQKHKMQAEEAE---RRLKQAEEEKVRQIKVVEEVAQ---------- 1597
Cdd:pfam07111 156 LTQAHEEALSSLTSKAEGlEKSLNSLETKRAGEAKQLAEAQKEAEllrKQLSKTQEELEAQVTLVESLRKyvgeqvppev 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1598 KTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRK----QEEEANKARE-----------QAEKELETWRLKA 1662
Cdd:pfam07111 236 HSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHmlalQEEELTRKIQpsdslepefpkKCRSLLNRWREKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1663 NeALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIA-----------QQ 1731
Cdd:pfam07111 316 F-ALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMElsraqearrrqQQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1732 KLSAEQEYIRLKADFEHAEQQRglLDNELQRLKNEVNAAEKQRRQLEDELAKVRSeMDALLQMKIQAEKVSQSNTEKSKQ 1811
Cdd:pfam07111 395 QTASAEEQLKFVVNAMSSTQIW--LETTMTRVEQAVARIPSLSNRLSYAVRKVHT-IKGLMARKVALAQLRQESCPPPPP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1812 LLETEA---LKMKQLAEEAARLRSvaeEAKKQRQLAEDEA--ARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAE 1886
Cdd:pfam07111 472 APPVDAdlsLELEQLREERNRLDA---ELQLSAHLIQQEVgrAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1887 NERLKRQ--AEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRinfERASKE 1964
Cdd:pfam07111 549 VARQGQQesTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQ---HRATQE 625
|
650 660
....*....|....*....|
gi 1655220527 1965 KSDLEvELKKLKgiaDETQK 1984
Cdd:pfam07111 626 KERNQ-ELRRLQ---DEARK 641
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1710-1910 |
1.24e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1710 QKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAK------ 1783
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1784 ----VRSEMDALLQMKIQAEKVSQSntekskQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKIL 1859
Cdd:COG3883 97 rsggSVSYLDVLLGSESFSDFLDRL------SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 1860 KEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQ 1910
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1149-1949 |
1.33e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.52 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1149 KEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDA--------------ELEHYRQLAGSLLERW 1214
Cdd:TIGR00606 241 KSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELkmekvfqgtdeqlnDLYHNHQRTVREKERE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1215 QAVFaqidlrQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKI-EAAPVWDSKALKEQLTQEKKLLEEIEKNKDQIEN 1293
Cdd:TIGR00606 321 LVDC------QRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHqEHIRARDSLIQSLATRLELDGFERGPFSERQIKN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1294 CQKDAKAYIDSLKDYEFQILAyrALQDPIASPLK-----KPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQR 1368
Cdd:TIGR00606 395 FHTLVIERQEDEAKTAAQLCA--DLQSKERLKQEqadeiRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1369 RLEDDEKASEKLKEDEK-KRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQL- 1446
Cdd:TIGR00606 473 ILELDQELRKAERELSKaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIr 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1447 --------ELTQL-------KNLSE------QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADD------ 1499
Cdd:TIGR00606 553 kiksrhsdELTSLlgyfpnkKQLEDwlhsksKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvc 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1500 -------ELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAE 1572
Cdd:TIGR00606 633 gsqdeesDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLK 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1573 EAERRLKQAEEE-----------------KVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEA- 1634
Cdd:TIGR00606 713 STESELKKKEKRrdemlglapgrqsiidlKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVt 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1635 --EKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKE 1712
Cdd:TIGR00606 793 imERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1713 NAE--KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDA 1790
Cdd:TIGR00606 873 KLQigTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKN 952
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1791 LLQMKIQAEKVSQSNTEKSKQLLETEALKMK-QLAEEAARLRSVAEEAKKQRQLAEDEAARqraeaEKILKEKLaainea 1869
Cdd:TIGR00606 953 IHGYMKDIENKIQDGKDDYLKQKETELNTVNaQLEECEKHQEKINEDMRLMRQDIDTQKIQ-----ERWLQDNL------ 1021
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1870 TRLKTEAEValkaKEAENERlkRQAEDEAYQRKLLEDQAAQHKhdIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEE 1949
Cdd:TIGR00606 1022 TLRKRENEL----KEVEEEL--KQHLKEMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1339-1785 |
1.58e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1339 IQEYVTLRTRYSELSTLTSQYIKfILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAksvAKAELEAQE 1418
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA---LEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1419 LKL-KMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTA 1497
Cdd:COG4717 146 ERLeELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1498 DDELQKLRDQAAEAEKVRKAAQEEAE-RLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAER 1576
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLlLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1577 RLKQAEEEkvrqikvvEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQgtVLQLQEEAEKLRKQEEEANKAREQAEKE-- 1654
Cdd:COG4717 306 ELQALPAL--------EELEEEELEELLAALGLPPDLSPEELLELLDR--IEELQELLREAEELEEELQLEELEQEIAal 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1655 LETWRLKANEALRLRLRAEEEAQrkslaQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLS 1734
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQ-----ELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 1735 AEQEYIRLKADFEHAEQqrgllDNELQRLKNEVNAAEKQRRQLEDELAKVR 1785
Cdd:COG4717 451 LREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALK 496
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2453-2601 |
1.90e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 57.10 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2453 QSTREADDLKK-AIAELEKEREKLKRDAqELQNKSKETASAQQEQMEQQKamlqqtflteKELLLKRERDVEDEKKKLQK 2531
Cdd:PRK12704 46 EAKKEAEAIKKeALLEAKEEIHKLRNEF-EKELRERRNELQKLEKRLLQK----------EENLDRKLELLEKREEELEK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2532 HLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIM----DEA-------VKKQKEAEAEMKNKQKEMEALEKKRLEQEKLL 2600
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIEEQLQELERISgltaEEAkeillekVEEEARHEAAVLIKEIEEEAKEEADKKAKEIL 194
|
.
gi 1655220527 2601 A 2601
Cdd:PRK12704 195 A 195
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
164-261 |
1.99e-07 |
|
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: 52.48 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 164 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALL-DMSQVYRQSNQENLEQAFSVAERELGVTRLLD 242
Cdd:cd21315 16 TPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92
|
90
....*....|....*....
gi 1655220527 243 PEDVDVAHPDEKSIITYVS 261
Cdd:cd21315 93 PEEMVNPKVDELSMMTYLS 111
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2173-2616 |
2.32e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 57.06 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2173 KQKQEADAEMAK-HKKEAEQALKQKSQVEkELGLVKLQLDETDKQkalmdeeLQRVKAQVNDAVKQKAQVENELSKVKMQ 2251
Cdd:pfam05557 48 DRNQELQKRIRLlEKREAEAEEALREQAE-LNRLKKKYLEALNKK-------LNEKESQLADAREVISCLKNELSELRRQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2252 -MDELLKLKvRIEEENLRLMQKNKDNTQKllAEEAEKMKSLAEEAARLSVEAEEtarQRKTAEAELA--EQRALAEKMLK 2328
Cdd:pfam05557 120 iQRAELELQ-STNSELEELQERLDLLKAK--ASEAEQLRQNLEKQQSSLAEAEQ---RIKELEFEIQsqEQDSEIVKNSK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2329 EKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLEISAEAEKLKLRVK--E 2406
Cdd:pfam05557 194 SELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE----EKYREEAATLELEKEKLEQELQSWVKlaQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2407 LSSAQAKAEEEATRFKKQADEAKVRLQEtEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQnKS 2486
Cdd:pfam05557 270 DTGLNLRSPEDLSRRIEQLQQREIVLKE-ENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-RR 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2487 KETASAQQEQMeqqKAMLQQ--TFLTEKE---LLLKRERDVEDEKKKLQKHLEDEvnkakalkdEQQRQQKLMDEEKKKL 2561
Cdd:pfam05557 348 VLLLTKERDGY---RAILESydKELTMSNyspQLLERIEEAEDMTQKMQAHNEEM---------EAQLSVAEEELGGYKQ 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 2562 QAIMDEA---VKKQKEAEAEMKNKQKEMEALekkRLEQEKLLAdENKKLREKLESLEV 2616
Cdd:pfam05557 416 QAQTLERelqALRQQESLADPSYSKEEVDSL---RRKLETLEL-ERQRLREQKNELEM 469
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2179-2404 |
2.80e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2179 DAEMAKHKKEAEQALKQKSQVEKELGLVKL--QLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELL 2256
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2257 klkvrieeenlrlmqkNKDNTQKLLAEEAEKMKSLAEEAARLSveaeETARQRKTAEAELAEQRALAEKMLKEKMQAIQ- 2335
Cdd:COG3206 261 ----------------QSPVIQQLRAQLAELEAELAELSARYT----PNHPDVIALRAQIAALRAQLQQEAQRILASLEa 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 2336 EATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIqQRLDKETQGFQKSLEA--ERKRQLEISAEAEKLKLRV 2404
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAEL-RRLEREVEVARELYESllQRLEEARLAEALTVGNVRV 390
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2026-2640 |
2.96e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 57.36 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2026 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEqkaqdvLSKNKEDLLsqeklrDEFENAKKLA 2105
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSRE------IVKSYENEL------DPLKNRLKEI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2106 QAAETAKEKAEKEAALLRQKAEEAEKLKKaaEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEaaalKQKQEADAEMAKH 2185
Cdd:TIGR00606 258 EHNLSKIMKLDNEIKALKSRKKQMEKDNS--ELELKMEKVFQGTDEQLNDLYHNHQRTVREKE----RELVDCQRELEKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2186 KKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVN-DAVKQKAQVENELSKVKMQMDELLKLKVRIEE 2264
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLElDGFERGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2265 ENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIqeatklKAEA 2344
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR------KAER 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2345 EELQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgfqkSLEAERKRQLEISAEAEKLKlRVKELSSAQAKAEEEATRFKKQ 2424
Cdd:TIGR00606 486 ELSKAEKNSLTETLKKEVKSLQNEKADLDR-------KLRKLDQEMEQLNHHTTTRT-QMEMLTKDKMDKDEQIRKIKSR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2425 ADEAKVRLQE--TEKQTTETVVQKLETQRLQSTREADDLKKAIAELE-------KEREKLKRDAQELQNKSKETASAQQE 2495
Cdd:TIGR00606 558 HSDELTSLLGyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEqnknhinNELESKEEQLSSYEDKLFDVCGSQDE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2496 QMEQQKAMLQQTFLTEKELLLKRERDVEDEkkkLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEA 2575
Cdd:TIGR00606 638 ESDLERLKEEIEKSSKQRAMLAGATAVYSQ---FITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 2576 EAEMKNKQKEME---ALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKV-PEEQL 2640
Cdd:TIGR00606 715 ESELKKKEKRRDemlGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImPEEES 783
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1535-2247 |
2.97e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1535 KKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQaeeekvrQIKVVEevaQKTAATQLQAMSFSEKTT 1614
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNN-------KIKILE---QQIKDLNDKLKKNKDKIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1615 KLEESLKKeqgTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLrlraEEEAQRKSLAQEEAEKQKTEAE 1694
Cdd:TIGR04523 100 KLNSDLSK---INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK----EKELEKLNNKYNDLKKQKEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1695 RDAKKKAKAEEaalkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDN-------ELQRLKNEV 1767
Cdd:TIGR04523 173 NELNLLEKEKL----NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDniekkqqEINEKTTEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1768 NAAEKQRRQLEDELAKVRsemDALLQMKIQAEKVSQSNTEKSKQL--LETEALKMKQLAEEAArLRSVAEEAKKQRqlae 1845
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIK---KQLSEKQKELEQNNKKIKELEKQLnqLKSEISDLNNQKEQDW-NKELKSELKNQE---- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1846 deaaRQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKhdiqEKITQLQSS 1925
Cdd:TIGR04523 321 ----KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYK----QEIKNLESQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1926 SvSELDRQKNIVEETLRQKkvvEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEER 2005
Cdd:TIGR04523 393 I-NDLESKIQNQEKLNQQK---DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2006 KRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANK----LKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVL 2081
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEkvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2082 SKNKEdlLSQEKLRDEfenakklaqaaetakekaekeaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEA 2161
Cdd:TIGR04523 549 KDDFE--LKKENLEKE------------------------IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2162 AKRAAAEAAALKQKQEADAEMAKHKKEAEQALK---QKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQK 2238
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNiksKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELM 682
|
....*....
gi 1655220527 2239 AQVENELSK 2247
Cdd:TIGR04523 683 KDWLKELSL 691
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1330-1640 |
3.00e-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: 57.00 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1330 KMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLE----DDEKASEKLKEDEKKrMAEIQAQLETQKQLAEGH 1405
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleqEEEKLKERLEELEED-LSSLEQEIENVKSELKEL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1406 AKSVAKAELEAQELKLKMKE----------DASQRQGLAVDAEKQKQNIQL--------ELTQLKNLSEQEIRSKNQQLE 1467
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDlearlshsriPEIQAELSKLEEEVSRIEARLreieqklnRLTLEKEYLEKEIQELQEQRI 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1468 EAQVSRRKLEEEIHLIRIQ---LQTTIKQKSTADDELQK-----------LRDQAAEAEKVRKAAQEEAERLRKQVNEET 1533
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKkeeLEEELEELEAALRDLESrlgdlkkerdeLEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1534 QKKKNAEDELKRKSEAEKEAARQKQKALDeLQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAatqlqamSFSEKT 1613
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLD-------ELKEKR 995
|
330 340
....*....|....*....|....*..
gi 1655220527 1614 TKLEEslkkEQGTVLQLQEEAEKLRKQ 1640
Cdd:TIGR02169 996 AKLEE----ERKAILERIEEYEKKKRE 1018
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2032-2530 |
3.18e-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: 57.16 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2032 QDEVERLKQKAAEANKLK-DKAEKELEKQvilaKEAAQKSTAAEQKAQDVLSKNKEDLLSQEK--LRDEFENAKKLAQAA 2108
Cdd:pfam12128 374 TAKYNRRRSKIKEQNNRDiAGIKDKLAKI----REARDRQLAVAEDDLQALESELREQLEAGKleFNEEEYRLKSRLGEL 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2109 ETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAK--AQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHK 2186
Cdd:pfam12128 450 KLRLNQATATPELLLQLENFDERIERAREEQEAANAEveRLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2187 KEAEQAL-----KQKSQVEKELGLV--KLQLDETDKQKALMDE-------------ELQRVkaQVNDAVKQKAQVENELS 2246
Cdd:pfam12128 530 FPQAGTLlhflrKEAPDWEQSIGKVisPELLHRTDLDPEVWDGsvggelnlygvklDLKRI--DVPEWAASEEELRERLD 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2247 KVKMQMDELLKLKVRIEEEnLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEetARQRKTAEAELAEQRALAEKM 2326
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQ-LVQANGELEKASREETFARTALKNARLDLRRLFDEKQ--SEKDKKNKALAERKDSANERL 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2327 LKEKMQAIQEATKLKAEAEELQKQKNQA----QEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKrQLEISAEAEKLKL 2402
Cdd:pfam12128 685 NSLEAQLKQLDKKHQAWLEEQKEQKREArtekQAYWQVVEGALDAQLALLKAAIAARRSGAKAELK-ALETWYKRDLASL 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2403 RVKELSSAQAKAE--------EEATRFKKQADEAKVRLQET-------EKQTTETVVQKLETQRLQSTREADDLKKAIAE 2467
Cdd:pfam12128 764 GVDPDVIAKLKREirtlerkiERIAVRRQEVLRYFDWYQETwlqrrprLATQLSNIERAISELQQQLARLIADTKLRRAK 843
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 2468 LEKEREKLkRDAQELQNKSKETASAQQEQM---------EQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQ 2530
Cdd:pfam12128 844 LEMERKAS-EKQQVRLSENLRGLRCEMSKLatlkedansEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1373-1582 |
3.39e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.97 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1373 DEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHA-KSVAKAELEAQELKlKMKEDASQRQGLAVDAEKQKQNIQLELTQL 1451
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERlKQLEKERLAAQEQK-KQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1452 KNLSEQeirsknQQLEEAQvsrRKLEEEihliriqlqttikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE 1531
Cdd:PRK09510 148 KAEAEA------KRAAAAA---KKAAAE-------------AKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 1532 ETQKKKNAEDELKRKSEAEK--EAARQKQKALDELQKHKMQAEEAERRLKQAE 1582
Cdd:PRK09510 206 EAKKKAAAEAKKKAAAEAKAaaAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1744-2600 |
3.44e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1744 ADF-EHAEQQRGLLDNELQrLKNEVNAAEKQRRQLEDELAKVRSEMDALlqmkIQAEKVSQSNTEKSKQLLetealkmkQ 1822
Cdd:PRK04863 272 ADYmRHANERRVHLEEALE-LRRELYTSRRQLAAEQYRLVEMARELAEL----NEAESDLEQDYQAASDHL--------N 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1823 LAEEAARLRSvaeeaKKQRQLAEDEAARQRAEaekilkEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDeaYQRK 1902
Cdd:PRK04863 339 LVQTALRQQE-----KIERYQADLEELEERLE------EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD--YQQA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1903 LLEDQ--AAQHKHDIQ--EKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGI 1978
Cdd:PRK04863 406 LDVQQtrAIQYQQAVQalERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1979 ADETQKSKAKAEEEAEKLKKLAAEEERKRREaeekvkkiaaaeeeaarQRKAAQDEVERLKQKAAEANKLKDKAEKELEK 2058
Cdd:PRK04863 486 AGEVSRSEAWDVARELLRRLREQRHLAEQLQ-----------------QLRMRLSELEQRLRQQQRAERLLAEFCKRLGK 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2059 QVILAKEAAQKSTAAEQKAQDvLSKNKEDLLSQ-EKLRDEFENAKKLAQAaetakekaekeaalLRQKAEEAEKLKKAAE 2137
Cdd:PRK04863 549 NLDDEDELEQLQEELEARLES-LSESVSEARERrMALRQQLEQLQARIQR--------------LAARAPAWLAAQDALA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2138 DEAAKQAKAQKDAERLRkeaeaeaakraaaeaaalkqkqEADAEMAKHKKEAEQalkQKSQVEKELGLVKLQLDETDKQK 2217
Cdd:PRK04863 614 RLREQSGEEFEDSQDVT----------------------EYMQQLLERERELTV---ERDELAARKQALDEEIERLSQPG 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2218 ALMDEELQRVKAQVN--------------DAV--------KQKAQVENELSKVKMQM----------------------- 2252
Cdd:PRK04863 669 GSEDPRLNALAERFGgvllseiyddvsleDAPyfsalygpARHAIVVPDLSDAAEQLagledcpedlyliegdpdsfdds 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2253 ----DELLK-LKVRIEEENLR---------LMQKNKDNTQKLLAEEAEkmkSLAEEAARLSVEAEETARQRKTAEAELAE 2318
Cdd:PRK04863 749 vfsvEELEKaVVVKIADRQWRysrfpevplFGRAAREKRIEQLRAERE---ELAERYATLSFDVQKLQRLHQAFSRFIGS 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2319 QRALA-----EKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQR---LDKETqgFQKSLEAERKrQ 2390
Cdd:PRK04863 826 HLAVAfeadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRlnlLADET--LADRVEEIRE-Q 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2391 LEISAEAEK--------LKLRVKELSSAQAKAEEEATrFKKQADEAKVRLQETEKQT---TEtVVQKLEtqRLQSTREAD 2459
Cdd:PRK04863 903 LDEAEEAKRfvqqhgnaLAQLEPIVSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAfalTE-VVQRRA--HFSYEDAAE 978
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2460 DLKKAIAELEKEREKLKRdAQELQNKSKETASAQQEQMEQQKAMLQQtfltekellLKRERDV-EDEKKKLQKHLE---- 2534
Cdd:PRK04863 979 MLAKNSDLNEKLRQRLEQ-AEQERTRAREQLRQAQAQLAQYNQVLAS---------LKSSYDAkRQMLQELKQELQdlgv 1048
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 2535 --DEVNKAKALKDEQQRQQKLMDEEKKKlqaimDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLL 2600
Cdd:PRK04863 1049 paDSGAEERARARRDELHARLSANRSRR-----NQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2360-2631 |
3.46e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2360 KLLEDKQEIQQRLDKETQGFQKSLEAERKRQ---LEISAEA---EKLKLRVKELSSA---------QAKAEEEATRFKKQ 2424
Cdd:COG3206 104 NLDEDPLGEEASREAAIERLRKNLTVEPVKGsnvIEISYTSpdpELAAAVANALAEAyleqnlelrREEARKALEFLEEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2425 ADEAKVRLQETEKQttetvVQKLETQR--LQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKA 2502
Cdd:COG3206 184 LPELRKELEEAEAA-----LEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2503 MLQQTFLTEkelLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAimdeavkkqkEAEAEMKNK 2582
Cdd:COG3206 259 LLQSPVIQQ---LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA----------SLEAELEAL 325
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 2583 QKEMEALEKKRLEQEKLLADENKKLRE------KLESLEVTSKQAASKTKEIEVQ 2631
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAElrrlerEVEVARELYESLLQRLEEARLA 380
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2278-2502 |
3.76e-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: 55.62 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2278 QKLLAEEAEKMKSLAEEAAR----LSVEAEETARQRKTAEAelAEQRALAEkmLKEKMQAIQEATKLKAEAEELQKQKNQ 2353
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKkeqeRQKKLEQQAEEAEKQRA--AEQARQKE--LEQRAAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2354 AQEKAKKLLED--KQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEAtrfKKQADEAKVR 2431
Cdd:TIGR02794 121 AEEAKAKQAAEakAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEA---KAKAEEAKAK 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 2432 LQETEKQTTETVVQKletqrlqstreADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKA 2502
Cdd:TIGR02794 198 AEAAKAKAAAEAAAK-----------AEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAA 257
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2341-2583 |
4.14e-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: 55.62 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2341 KAEAEELQKQKNQAQEKAKKLLEDKQEIQQRldKETQGFQKSLEAERKRQLEISAEAEKLKlrvkelsSAQAKAEEEATR 2420
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQ--AEEAEKQRAAEQARQKELEQRAAAEKAA-------KQAEQAAKQAEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2421 FKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAqELQNKSKETASAQQEQMEQQ 2500
Cdd:TIGR02794 117 KQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKA-EAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2501 KAMLQQTFLTEKELLLKRERD------VEDEKKKLQKHLEDEVNKAKALKDEQQRQ--QKLMDEEKKKLQAIMDEAVKKQ 2572
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEaaaaaaAEAERKADEAELGDIFGLASGSNAEKQGGarGAAAGSEVDKYAAIIQQAIQQN 275
|
250
....*....|.
gi 1655220527 2573 KEAEAEMKNKQ 2583
Cdd:TIGR02794 276 LYDDPSFRGKT 286
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2251-2629 |
4.66e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.29 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2251 QMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSvEAEETARQRKTAEAELAEQRalaEKMLKEK 2330
Cdd:pfam05557 13 QLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLE-KREAEAEEALREQAELNRLK---KKYLEAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2331 MQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSA 2410
Cdd:pfam05557 89 NKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2411 QAKAEEEatrfkkqadEAKVRLQETEKQTTETVVQKLETqrlqstreaddlkkaIAELEKEREKLKRDAQELqNKSKETA 2490
Cdd:pfam05557 169 EQRIKEL---------EFEIQSQEQDSEIVKNSKSELAR---------------IPELEKELERLREHNKHL-NENIENK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2491 SAQQEQMEQQKAMLQQTFLTEKELLlkrerDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQaimDEAVK 2570
Cdd:pfam05557 224 LLLKEEVEDLKRKLEREEKYREEAA-----TLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQ---REIVL 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 2571 KQK--EAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2629
Cdd:pfam05557 296 KEEnsSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERD 356
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2254-2615 |
4.94e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2254 ELLKLKVRIEEENLRLMqknkdNTQKLLAEEAEKMKSLAE--EAAR----LSVEAEETARQRKTAEAELAEqralAEKML 2327
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLV-----EMARELAELNEAESDLEQdyQAASdhlnLVQTALRQQEKIERYQADLEE----LEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2328 KEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDkqeIQQRLD-KETQG--FQKSLEA-ERKRQL--EISAEAEKLK 2401
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD---YQQALDvQQTRAiqYQQAVQAlERAKQLcgLPDLTADNAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2402 LRVKELssaQAKaEEEATRFKKQAdEAKVRLQETEKQTTETVVQKLetQRLQSTREADDLKKAIAELEKEREKLKRDAQE 2481
Cdd:PRK04863 442 DWLEEF---QAK-EQEATEELLSL-EQKLSVAQAAHSQFEQAYQLV--RKIAGEVSRSEAWDVARELLRRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2482 LQNKSKETASAQQEQMEQQKAM-LQQTFLTEKELLLKRERDVED---EKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEE 2557
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQQQRAErLLAEFCKRLGKNLDDEDELEQlqeELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2558 KKKLQAI------MDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLE 2615
Cdd:PRK04863 595 IQRLAARapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALD 658
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1350-1624 |
5.18e-07 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 56.38 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1350 SELSTLTSQYIKFILE---TQRRLEDDEKA---SEKLKEDEKKRMAEI---QAQLETQKQLA---EGHAKSVA-KAELEA 1416
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERAeadRQRLEQEKQQQLAAIsgsQSQLESTDQNAletNGQAQRDAiLEESRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1417 --QELKlKMKEDASQRQGLAVDAEKQKQNIQLELTQ--LKNLSEQEIRSKnqqleeaQVSRRKLEEeihliriqlqttIK 1492
Cdd:NF012221 1618 vtKELT-TLAQGLDALDSQATYAGESGDQWRNPFAGglLDRVQEQLDDAK-------KISGKQLAD------------AK 1677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1493 QKSTadDELQKLRDQAAEAEkvrkAAQEEAERLRKQVNEETQKKKNAEDelKRKseaeKEAARQKQKALDELQKHKMQAE 1572
Cdd:NF012221 1678 QRHV--DNQQKVKDAVAKSE----AGVAQGEQNQANAEQDIDDAKADAE--KRK----DDALAKQNEAQQAESDANAAAN 1745
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 1573 EAERRLKQaeeekvrqikvvEEVAQKTAATQLQAmsfSEKTTKLEESLKKEQ 1624
Cdd:NF012221 1746 DAQSRGEQ------------DASAAENKANQAQA---DAKGAKQDESDKPNR 1782
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1417-1974 |
5.55e-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: 55.80 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1417 QELKlKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQ-EIRSKNQQLEEAQVsrrkleeeihliriqlqttiKQks 1495
Cdd:pfam05701 42 LELE-KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEElKLNLERAQTEEAQA--------------------KQ-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1496 taDDELQKLRDQAAE---AEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAE 1572
Cdd:pfam05701 99 --DSELAKLRVEEMEqgiADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1573 EAErrlKQAEEEKVRQIKVVEEVAQKTAAtQLQAmsfSEKttKLEESLKKEQGTvLQLQEEaekLRKQEEEANKAREQ-- 1650
Cdd:pfam05701 177 EIE---KTVEELTIELIATKESLESAHAA-HLEA---EEH--RIGAALAREQDK-LNWEKE---LKQAEEELQRLNQQll 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1651 AEKELETwRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAeeaalkqkENAEKELEKQRTFAEqiaq 1730
Cdd:pfam05701 244 SAKDLKS-KLETASALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAAL--------ASAKKELEEVKANIE---- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1731 qKLSAEQEYIRLKADFEHAEqqrglLDNE---LQRLKNEVNAAEKQRRQLEDELAKVRSEMdALLQMKiqaekvsqsnTE 1807
Cdd:pfam05701 311 -KAKDEVNCLRVAAASLRSE-----LEKEkaeLASLRQREGMASIAVSSLEAELNRTKSEI-ALVQAK----------EK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1808 KSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEA-- 1885
Cdd:pfam05701 374 EAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlq 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1886 ENERLKRQAEDEAYQRKLL----------------EDQAaqhKHDIQEKITQLQSSSVSELdRQKNIVEETLRQKKVVEE 1949
Cdd:pfam05701 454 ESESSAESTNQEDSPRGVTlsleeyyelskraheaEELA---NKRVAEAVSQIEEAKESEL-RSLEKLEEVNREMEERKE 529
|
570 580
....*....|....*....|....*
gi 1655220527 1950 EIHIIRINFERASKEKSDLEVELKK 1974
Cdd:pfam05701 530 ALKIALEKAEKAKEGKLAAEQELRK 554
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1749-1935 |
5.61e-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: 53.78 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1749 AEQQRGLLDneLQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmKIQAEKVSQSNTEKSKQLLETEalkMKQLAEEAA 1828
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELE---IEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1829 RLRSVAEEAKKQRQLA-----EDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQrkl 1903
Cdd:COG1579 77 KYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE--- 153
|
170 180 190
....*....|....*....|....*....|..
gi 1655220527 1904 LEDQAAQHKHDIQEKITQLQSSSVSELDRQKN 1935
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPELLALYERIRK 185
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1051-1776 |
5.73e-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: 56.23 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1051 EQMKVQSELEGLKKDL----NSITEKTEEILASPQQSSSAPMLRSELDVTLKKMDHVYGLSSVYLDKLKTIdivirnTKD 1126
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIasleRSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE------YAE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1127 AEDTVKSYESRLRDVSKVPAEEK-EVEAHRSQLKAMRAEAEADQATFDRLQDELK-----------AATSVSDKMTRLHS 1194
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRdELKDYREKLEKLKREINELKRELDRLQEELQrlseeladlnaAIAGIEAKINELEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1195 ERD---AELEHYRQLAGSLLERWQAVFAQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALK 1271
Cdd:TIGR02169 442 EKEdkaLEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1272 EQLTQEKKLLEEIEKNKDQIENC------------QKDAKAYIDSLKDYE---FQILAYRALQDPiASPLKKPKMESASD 1336
Cdd:TIGR02169 522 GVHGTVAQLGSVGERYATAIEVAagnrlnnvvvedDAVAKEAIELLKRRKagrATFLPLNKMRDE-RRDLSILSEDGVIG 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1337 NIIqEYVTLRTRYSELstltsqyIKFILETQRRLEDDEKASEKLkedEKKRMAEIQAQL------ETQKQLAEGHAKSVA 1410
Cdd:TIGR02169 601 FAV-DLVEFDPKYEPA-------FKYVFGDTLVVEDIEAARRLM---GKYRMVTLEGELfeksgaMTGGSRAPRGGILFS 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1411 KAEL-EAQELKLKMKEDASQRQGLAVDAEKQKQNIQlELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQT 1489
Cdd:TIGR02169 670 RSEPaELQRLRERLEGLKRELSSLQSELRRIENRLD-ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1490 TIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAA-RQKQKALDELQKHK 1568
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARlREIEQKLNRLTLEK 828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1569 MQAEEAerrlKQAEEEKVRQIKV-VEEVAQKTAATQLqamsfseKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKA 1647
Cdd:TIGR02169 829 EYLEKE----IQELQEQRIDLKEqIKSIEKEIENLNG-------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1648 REQAEKELETWRLKANealRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRtfaeq 1727
Cdd:TIGR02169 898 LRELERKIEELEAQIE---KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA----- 969
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1655220527 1728 IAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQ 1776
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1618-2063 |
5.96e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1618 ESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANealRLRLRAEEEAQRKSLAQEEAEKQKTEAERDA 1697
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ---LLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1698 KKKAKAeeaalkQKENAEKEL-EKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQ 1776
Cdd:COG4717 158 LRELEE------ELEELEAELaELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1777 LEDE--------------------------------LAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLA 1824
Cdd:COG4717 232 LENEleaaaleerlkearlllliaaallallglggsLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1825 EEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEA--YQRK 1902
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1903 LLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQK-KVVEEEIHIIRINFERASKEKSDLEVELKKLKGiade 1981
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEE---- 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1982 tqkskakaeeeaeklkklaaeeerkrreaeekvkkiaaaeeeaarqrkaaQDEVERLKQKAAEA-NKLKDKAEKELEKQV 2060
Cdd:COG4717 468 --------------------------------------------------DGELAELLQELEELkAELRELAEEWAALKL 497
|
...
gi 1655220527 2061 ILA 2063
Cdd:COG4717 498 ALE 500
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4163-4191 |
6.60e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.48 E-value: 6.60e-07
10 20
....*....|....*....|....*....
gi 1655220527 4163 IVDPESGKEMSVYEAYQKGLIDHQTYLEL 4191
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1498-1656 |
6.87e-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: 53.78 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1498 DDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKsEAEKEAARQKQKAL----------DELQKH 1567
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-ELEIEEVEARIKKYeeqlgnvrnnKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1568 KMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQlqamsfsEKTTKLEESLKKEQGtvlQLQEEAEKLRKQEEEANKA 1647
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELE-------AELAELEAELEEKKA---ELDEELAELEAELEELEAE 164
|
....*....
gi 1655220527 1648 REQAEKELE 1656
Cdd:COG1579 165 REELAAKIP 173
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1302-1606 |
8.73e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1302 IDSLKDYEFQILAYRALQDPIASPLKKPKMESASD-NIIQeyVTLRTRYSELS-----TLTSQYIKFILEtqRRLEDDEK 1375
Cdd:COG3206 100 VDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGsNVIE--ISYTSPDPELAaavanALAEAYLEQNLE--LRREEARK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1376 ASEKLKEdekkRMAEIQAQLEtqkqlaeghaksvaKAELEAQELKlkmkedasQRQGLaVDAEKQKQNIQLELTQLknls 1455
Cdd:COG3206 176 ALEFLEE----QLPELRKELE--------------EAEAALEEFR--------QKNGL-VDLSEEAKLLLQQLSEL---- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1456 eqeirskNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKST--ADDELQKLRDQAAEAEKVRKAAQE-------EAERLR 1526
Cdd:COG3206 225 -------ESQLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALR 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1527 KQVNEETQKKKNAEDELKRKSEAEKEAARQK----QKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAAT 1602
Cdd:COG3206 298 AQIAALRAQLQQEAQRILASLEAELEALQAReaslQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
....
gi 1655220527 1603 QLQA 1606
Cdd:COG3206 378 RLAE 381
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2268-2461 |
9.00e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2268 RLMQKNKDNT------QKLLAEEA-EKMKSLAEEAARL-SVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQ-EAT 2338
Cdd:PRK09510 66 RQQQQQKSAKraeeqrKKKEQQQAeELQQKQAAEQERLkQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAaAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2339 KLKAEAEE--LQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgfQKSLEAERKRQLEISAEAEKLKL-RVKELSSAQAKAE 2415
Cdd:PRK09510 146 KAKAEAEAkrAAAAAKKAAAEAKKKAEAEAAKKAAAEA-----KKKAEAEAAAKAAAEAKKKAEAEaKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1655220527 2416 EEATRFKKQADEAKVRLQETEKQTTEtvvqKLETQRLQSTREADDL 2461
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKA----AEKAAAAKAAAEVDDL 262
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1556-1773 |
9.24e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1556 QKQKALDELQKHKMQAEEAERRLKQ---AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQE 1632
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQkqaAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1633 EAEKLRkQEEEANKAREQAEKELETWRLKANEAlRLRLRAEEEAQRKslAQEEAEKQKTEAERDAKKKAKAEEAALKQKE 1712
Cdd:PRK09510 150 EAEAKR-AAAAAKKAAAEAKKKAEAEAAKKAAA-EAKKKAEAEAAAK--AAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 1713 NAEKELEKQRTFAEQIAQQKLSAEQEyirlkadfehAEQQRGLLDNELQRLKNEVNAAEKQ 1773
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAA----------AAKAAAEVDDLFGGLDSGKNAPKTG 276
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1710-1909 |
9.57e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.43 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1710 QKENAEKELEKQRTFAEQIAQQKLSAEQEyirlkadfehAEQQRglldneLQRLKNEVNAAEKQRRQLEDELAKvrsemd 1789
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQA----------AEQER------LKQLEKERLAAQEQKKQAEEAAKQ------ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1790 ALLQMKiQAEKVSQSNTEKSKQLLETEAlkmKQLAEEAARlrsVAEEAKKQrqlAEDEAARQRAEAEKILKEKLAAINEA 1869
Cdd:PRK09510 127 AALKQK-QAEEAAAKAAAAAKAKAEAEA---KRAAAAAKK---AAAEAKKK---AEAEAAKKAAAEAKKKAEAEAAAKAA 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1655220527 1870 TRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAA 1909
Cdd:PRK09510 197 AEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA 236
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2234-2438 |
9.93e-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: 54.38 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2234 AVKQKAQVENELSKVKMQMDELLKLKVRIEEEnLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAE 2313
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2314 AELAEQRALAEKML------------------KEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLledkQEIQQRLDKE 2375
Cdd:COG4942 97 AELEAQKEELAELLralyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL----AALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 2376 TQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ 2438
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1141-1821 |
9.98e-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: 55.61 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1141 VSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSvsDKMTRLHSERDAELEHYRQLAGSLL---ERWQAV 1217
Cdd:pfam12128 243 FTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSA--ELNQLLRTLDDQWKEKRDELNGELSaadAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1218 FAQID-LRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAapVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQK 1296
Cdd:pfam12128 321 RSELEaLEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA--LTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1297 DAKAYIDSLKDYEFQILAYRALQDPIasplkKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIkfiletqrrLEDDEKA 1376
Cdd:pfam12128 399 LAKIREARDRQLAVAEDDLQALESEL-----REQLEAGKLEFNEEEYRLKSRLGELKLRLNQAT---------ATPELLL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1377 SEKLKEDEKKRMAEIQAQlETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAvDAEKQKQNIQLELTQLKNLSE 1456
Cdd:pfam12128 465 QLENFDERIERAREEQEA-ANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSA-LDELELQLFPQAGTLLHFLRK 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1457 QEI---RSKNQQLEEAQVSRRKLEEEI----------------HLIRIQlqttIKQKSTADDELQKLRDQAAEAekvRKA 1517
Cdd:pfam12128 543 EAPdweQSIGKVISPELLHRTDLDPEVwdgsvggelnlygvklDLKRID----VPEWAASEEELRERLDKAEEA---LQS 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1518 AQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIkvveEVAQ 1597
Cdd:pfam12128 616 AREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSL----EAQL 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1598 KTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAE---KELETWR------LKANEALRL 1668
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKaelKALETWYkrdlasLGVDPDVIA 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1669 RLRAEEEAQRKSLAQEEAEKQKTEAERDakkkaKAEEAALKQKENAEKELEKQRTFAEQIaQQKLSAEQEYIRLKadfeh 1748
Cdd:pfam12128 772 KLKREIRTLERKIERIAVRRQEVLRYFD-----WYQETWLQRRPRLATQLSNIERAISEL-QQQLARLIADTKLR----- 840
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 1749 aeqqrglldneLQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEkVSQSNTEKSKQLLETEALKMK 1821
Cdd:pfam12128 841 -----------RAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDAN-SEQAQGSIGERLAQLEDLKLK 901
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1455-1654 |
1.05e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1455 SEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE--- 1531
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1532 ETQKKKNAEDELK------------RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKT 1599
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 1600 AATQLQAmsfsektTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKE 1654
Cdd:COG3883 174 EAQQAEQ-------EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
32-152 |
1.06e-06 |
|
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: 50.37 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 32 ERDRVQKKTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEVLSgetLPRERDLVRNVRLPREKGRMRfhKLQNVQIA 111
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMTR---VPVDWGHVNKPPYPALGGNMK--KIENCNYA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655220527 112 LDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21329 75 VELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2334-2547 |
1.06e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.43 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2334 IQEATKLKAEAEelQKQKNQAQEKAKKLLEDKQEIQQRLdketqgfqKSLEAERKRQLEISAEAEKLKLRVKElssAQAK 2413
Cdd:PRK09510 67 QQQQQKSAKRAE--EQRKKKEQQQAEELQQKQAAEQERL--------KQLEKERLAAQEQKKQAEEAAKQAAL---KQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2414 AEEEAtrfKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQ 2493
Cdd:PRK09510 134 AEEAA---AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2494 QEQMEQQKAmlqqtfltEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQ 2547
Cdd:PRK09510 211 AAAEAKKKA--------AAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1438-1849 |
1.09e-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: 54.90 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1438 EKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKA 1517
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1518 AQEEAERLRKQVNEETQKKKNAEDELKRKSEaekeaarQKQKALDELQKHKMQAEEAERRLKQAEEEKvrqikvvEEVAQ 1597
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQ-------RVLERETELERMKERAKKAGAQRKEEEAER-------KQLQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1598 KTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRlkaneALRLRLRAEE--- 1674
Cdd:pfam07888 179 KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELR-----SLQERLNASErkv 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1675 EAQRKSLAQEEAEKQKTEAErdakkkakaeeAALKQKENAEKELE-KQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQR 1753
Cdd:pfam07888 254 EGLGEELSSMAAQRDRTQAE-----------LHQARLQAAQLTLQlADASLALREGRARWAQERETLQQSAEADKDRIEK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1754 glLDNELQRLKNEVNAAEKQRRQLEDELAKVR-------SEMDALLQMKIQAEKVSQSntEKSKQLLETEALkMKQLAEE 1826
Cdd:pfam07888 323 --LSAELQRLEERLQEERMEREKLEVELGREKdcnrvqlSESRRELQELKASLRVAQK--EKEQLQAEKQEL-LEYIRQL 397
|
410 420
....*....|....*....|...
gi 1655220527 1827 AARLRSVAEEAKKQRQLAEDEAA 1849
Cdd:pfam07888 398 EQRLETVADAKWSEAALTSTERP 420
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1829-2640 |
1.26e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.05 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1829 RLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVAlKAKEAENERLK-RQAEDEAYQRKLledq 1907
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIV-KSYENELDPLKnRLKEIEHNLSKI---- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1908 aaqhkHDIQEKITQLQSSsvsELDRQKNIVEETLRQKKV---VEEEIHIIRINFERASKEKSDLEVEL-KKLKGIADETQ 1983
Cdd:TIGR00606 265 -----MKLDNEIKALKSR---KKQMEKDNSELELKMEKVfqgTDEQLNDLYHNHQRTVREKERELVDCqRELEKLNKERR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1984 kskakaeeeAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILA 2063
Cdd:TIGR00606 337 ---------LLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2064 KEAAQkstaaeqkaqdVLSKNKEDLLSQEKLRDEFENAKK-LAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAK 2142
Cdd:TIGR00606 408 KTAAQ-----------LCADLQSKERLKQEQADEIRDEKKgLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2143 QAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQeadAEMAKHKKEAEQALKQKSQVEKELGlvklQLDETDKQKALMDE 2222
Cdd:TIGR00606 477 DQELRKAERELSKAEKNSLTETLKKEVKSLQNEK---ADLDRKLRKLDQEMEQLNHHTTTRT----QMEMLTKDKMDKDE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2223 ELQRVKAQVNDAV----------KQKAQVENELSKVKMQMDELLKlKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLA 2292
Cdd:TIGR00606 550 QIRKIKSRHSDELtsllgyfpnkKQLEDWLHSKSKEINQTRDRLA-KLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2293 EEAArlSVEAEETARQRKTAEAELA-EQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQR 2371
Cdd:TIGR00606 629 FDVC--GSQDEESDLERLKEEIEKSsKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2372 LDKETQGFQKSLEAERKRQLEISAEAE----KLKLRVKELSSAQAKAEEEATRFKkqadEAKVRLQETEKQTtETVVQKL 2447
Cdd:TIGR00606 707 APDKLKSTESELKKKEKRRDEMLGLAPgrqsIIDLKEKEIPELRNKLQKVNRDIQ----RLKNDIEEQETLL-GTIMPEE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2448 ETQRLQSTrEADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLlkreRDVEDEKK 2527
Cdd:TIGR00606 782 ESAKVCLT-DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELN----RKLIQDQQ 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2528 KLQKHLEDEVNKAKALK-----DEQQRQQklMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLAD 2602
Cdd:TIGR00606 857 EQIQHLKSKTNELKSEKlqigtNLQRRQQ--FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET 934
|
810 820 830
....*....|....*....|....*....|....*...
gi 1655220527 2603 ENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2640
Cdd:TIGR00606 935 SNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYL 972
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2027-2204 |
1.38e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.04 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2027 QRKAAQDEVERL-----KQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEdllsqeklrdefENA 2101
Cdd:PRK09510 100 QERLKQLEKERLaaqeqKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA------------AEA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2102 KKLAQAAETAKEKAEKeaallRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAaAEAAALKQKQEADAE 2181
Cdd:PRK09510 168 KKKAEAEAAKKAAAEA-----KKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA-AAKAAAEAKAAAEKA 241
|
170 180
....*....|....*....|...
gi 1655220527 2182 MAKHKKEAEQALKQKSQVEKELG 2204
Cdd:PRK09510 242 AAAKAAEKAAAAKAAAEVDDLFG 264
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1364-1670 |
1.42e-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: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1364 LETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQN 1443
Cdd:pfam13868 45 LDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1444 IQLELTQLKNLSEQEIRSKNQQleeaqvsrrKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAE 1523
Cdd:pfam13868 125 QRQLREEIDEFNEEQAEWKELE---------KEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1524 RLRKQVNEETQKKKNAEDELKRKS-EAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKvvEEVAQKTAAT 1602
Cdd:pfam13868 196 AQDEKAERDELRAKLYQEEQERKErQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEF--ERMLRKQAED 273
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 1603 QLQAMSFSEKTTKLEESLKKEqgtVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRL 1670
Cdd:pfam13868 274 EEIEQEEAEKRRMKRLEHRRE---LEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1747-1873 |
1.51e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 54.64 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1747 EHAEQQ-RGLLdnELQRLKNEVnAAEKQRRqledelakvrsemdALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAE 1825
Cdd:PTZ00491 673 ELLEQEaRGRL--ERQKMHDKA-KAEEQRT--------------KLLELQAESAAVESSGQSRAEALAEAEARLIEAEAE 735
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220527 1826 -EAARLRSVAE--------EAKKQRQLAEDEAARQRAEAEkILKEKLAAINEATRLK 1873
Cdd:PTZ00491 736 vEQAELRAKALrieaeaelEKLRKRQELELEYEQAQNELE-IAKAKELADIEATKFE 791
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1511-1952 |
1.54e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 54.38 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1511 AEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAArQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIK 1590
Cdd:pfam09731 43 GEEVVLYALGEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEK-KQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1591 VVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEqgTVLQLQEEAEKLRKQEEEANKAREqaeKELETWRLKANealrlrl 1670
Cdd:pfam09731 122 SEQEKEKALEEVLKEAISKAESATAVAKEAKDD--AIQAVKAHTDSLKEASDTAEISRE---KATDSALQKAE------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1671 RAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAAlkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAE 1750
Cdd:pfam09731 190 ALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPE--HLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1751 qqrglldNELQRLKNEVNAAEKQRrqLEDELAKVRSEMDALlqmkiqaekvsqsntekSKQLLEtealkmKQLAEEAARL 1830
Cdd:pfam09731 268 -------PDIIPVLKEDNLLSNDD--LNSLIAHAHREIDQL-----------------SKKLAE------LKKREEKHIE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1831 RSVAEEAKKQRQLAEDEAARQRAEAEKILKEKlaaineatRLKTEAEVALKAKEAENE---RLKRQAED-EAYQRKLLED 1906
Cdd:pfam09731 316 RALEKQKEELDKLAEELSARLEEVRAADEAQL--------RLEFEREREEIRESYEEKlrtELERQAEAhEEHLKDVLVE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 1907 QAAQ----HKHDIQEKITQ---LQSSSVSELDRQKNIVEETLRQKKVVEEEIH 1952
Cdd:pfam09731 388 QEIElqreFLQDIKEKVEEeraGRLLKLNELLANLKGLEKATSSHSEVEDENR 440
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2026-2424 |
1.54e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2026 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAK-EAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFEN--AK 2102
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERLEELRELEEELEELEAelAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2103 KLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEAD--- 2179
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlli 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2180 -AEMAKHKKEAEQALKQKSQVEK----ELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKV----KM 2250
Cdd:COG4717 255 aAALLALLGLGGSLLSLILTIAGvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppDL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2251 QMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSL-------AEEAARLSVEAEETARQRKTAEAELAEQRALA 2323
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaeagveDEEELRAALEQAEEYQELKEELEELEEQLEEL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2324 EKMLKEKMQAIQEATkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLdkETQGFQKSLEAERKRQLEISAEAEKLKLR 2403
Cdd:COG4717 415 LGELEELLEALDEEE-LEEELEELEEELEELEEELEELREELAELEAEL--EQLEEDGELAELLQELEELKAELRELAEE 491
|
410 420
....*....|....*....|.
gi 1655220527 2404 VKELSSAQAKAEEEATRFKKQ 2424
Cdd:COG4717 492 WAALKLALELLEEAREEYREE 512
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1548-1912 |
1.70e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.10 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1548 EAEKEAARQKQKaldelqkhkmQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEqgtv 1627
Cdd:pfam02029 2 EDEEEAARERRR----------RAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDR---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1628 LQLQEEAEKLRKQEEEankareQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEaekqKTEAERDAKKKAKAEEAA 1707
Cdd:pfam02029 68 TAKREERRQKRLQEAL------ERQKEFDPTIADEKESVAERKENNEEEENSSWEKEE----KRDSRLGRYKEEETEIRE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1708 LKQKENAEKELEKQRtfAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQrLKNEVNAAEKQRRQLEDELAKVRSE 1787
Cdd:pfam02029 138 KEYQENKWSTEVRQA--EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKK-VKYESKVFLDQKRGHPEVKSQNGEE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1788 MDALLQMKIQAEKVSQSNT----EKSKQLLETEaLKMKQLAEEAARLRSVAEEAKKQRQLaedEAARQRAEAEKILKEKL 1863
Cdd:pfam02029 215 EVTKLKVTTKRRQGGLSQSqereEEAEVFLEAE-QKLEELRRRRQEKESEEFEKLRQKQQ---EAELELEELKKKREERR 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 1864 AAINEATRLKTEAEVALKAKEAENERL------KRQAEDEAYQRKLLEDQAAQHK 1912
Cdd:pfam02029 291 KLLEEEEQRRKQEEAERKLREEEEKRRmkeeieRRRAEAAEKRQKLPEDSSSEGK 345
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2176-2401 |
1.74e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 54.26 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2176 QEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVndavkqkAQVENELSKVKMQMDEL 2255
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNEEL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2256 LKlKVRIEEENLRLMQKNKDNTQKL---LAEEAEKMKSLAE--EAARLSVEAEETARQRKTAEAELAEQRALAE-KMLKE 2329
Cdd:pfam05667 383 EK-QYKVKKKTLDLLPDAEENIAKLqalVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEiKELRE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2330 KMQAIQEATKLKaeaEELQKQKNQAQEKAKKlleDKQ---------EIQQRLDKETQGFQKSLEAERKRQLEISAEAEKL 2400
Cdd:pfam05667 462 KIKEVAEEAKQK---EELYKQLVAEYERLPK---DVSrsaytrrilEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKL 535
|
.
gi 1655220527 2401 K 2401
Cdd:pfam05667 536 D 536
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1474-1794 |
1.93e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.38 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1474 RKLEEEIHLIRIQL----QTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEA 1549
Cdd:pfam13868 9 RELNSKLLAAKCNKerdaQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1550 EKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIK--VVEEVAQKTAATQLQAMSFSEKTTKLEESLK-KEQGT 1626
Cdd:pfam13868 89 RQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLReeIDEFNEEQAEWKELEKEEEREEDERILEYLKeKAERE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1627 VLQLQEEAEKLRKQEEEANKAREQAEKELETWRlkANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEA 1706
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQDEKA--ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1707 ALKQKENAEKELEKQ------RTFAEQIAQQKLSAEQEYIRLKAdfEHAEQQRGLLDNELQRL---KNEVNAAEKQRRQL 1777
Cdd:pfam13868 247 LKERRLAEEAEREEEefermlRKQAEDEEIEQEEAEKRRMKRLE--HRRELEKQIEEREEQRAaerEEELEEGERLREEE 324
|
330
....*....|....*..
gi 1655220527 1778 EDELAKVRSEMDALLQM 1794
Cdd:pfam13868 325 AERRERIEEERQKKLKE 341
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1573-1984 |
2.01e-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: 54.36 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1573 EAERRLKQAEEEKVRQikvveEVAQKTAATQLQAmsfseKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKA-REQA 1651
Cdd:pfam05557 6 ESKARLSQLQNEKKQM-----ELEHKRARIELEK-----KASALKRQLDRESDRNQELQKRIRLLEKREAEAEEAlREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1652 ekeletwrlkanEALRLRLRAEEEAQRKslaQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQ 1731
Cdd:pfam05557 76 ------------ELNRLKKKYLEALNKK---LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1732 klsaEQEYirlKADFEHAEQQRGLLDNELQRLKnevnAAEKQRRQLEDELAKvrSEMDALLQMKIQAEKVSQSNTEKSKQ 1811
Cdd:pfam05557 141 ----LDLL---KAKASEAEQLRQNLEKQQSSLA----EAEQRIKELEFEIQS--QEQDSEIVKNSKSELARIPELEKELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1812 LLETEALKMKQLAEEAARLRSVAEEAKkqRQLAEDEAARQRAEAEKILKEKLAA-INEATRLKTEAEVALKAKEAENERL 1890
Cdd:pfam05557 208 RLREHNKHLNENIENKLLLKEEVEDLK--RKLEREEKYREEAATLELEKEKLEQeLQSWVKLAQDTGLNLRSPEDLSRRI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1891 KRQAEDEAY--QRKLLEDQAAQHKH----DIQEKITQLQSSSVSE---LDRQKNIVEETLRQKKVVEEEIHIIRINFERA 1961
Cdd:pfam05557 286 EQLQQREIVlkEENSSLTSSARQLEkarrELEQELAQYLKKIEDLnkkLKRHKALVRRLQRRVLLLTKERDGYRAILESY 365
|
410 420
....*....|....*....|....*.
gi 1655220527 1962 SKEKSDLEVELKKL---KGIADETQK 1984
Cdd:pfam05557 366 DKELTMSNYSPQLLeriEEAEDMTQK 391
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2222-2467 |
2.18e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2222 EELQRVKAQVNDAVKQKAQveneLSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVE 2301
Cdd:COG4913 235 DDLERAHEALEDAREQIEL----LEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2302 AEETARQRKTAEAELaeqRALAEKMLKEKMQAIQEatkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQk 2381
Cdd:COG4913 311 LERLEARLDALREEL---DELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2382 sleaerkrqleisAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQttetvVQKLETQRLQSTREADDL 2461
Cdd:COG4913 384 -------------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE-----IASLERRKSNIPARLLAL 445
|
....*.
gi 1655220527 2462 KKAIAE 2467
Cdd:COG4913 446 RDALAE 451
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1138-1696 |
2.24e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1138 LRDVSKVPAEEKEVEAHRSQLKAMRAEAEAdQATFDRLQDELKAATSVS----DKMTRLHSERDAELEHYRQLAGSLLER 1213
Cdd:PRK04863 502 LRRLREQRHLAEQLQQLRMRLSELEQRLRQ-QQRAERLLAEFCKRLGKNlddeDELEQLQEELEARLESLSESVSEARER 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1214 wqavfaQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAapVWDSKALKEQLTQEKKLLEEIEKNKDQIEN 1293
Cdd:PRK04863 581 ------RMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEE--FEDSQDVTEYMQQLLERERELTVERDELAA 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1294 CQKDAKAYIDSL------KDYEFQILAYR----------------------ALQDPIASPLKKPKMESASDNIIQEYVTL 1345
Cdd:PRK04863 653 RKQALDEEIERLsqpggsEDPRLNALAERfggvllseiyddvsledapyfsALYGPARHAIVVPDLSDAAEQLAGLEDCP 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1346 RTRYselstltsqyikFILETQRRLEDDEKASEKLKEDEKKRMAEIQ------------------AQLETQKQLAEGHAK 1407
Cdd:PRK04863 733 EDLY------------LIEGDPDSFDDSVFSVEELEKAVVVKIADRQwrysrfpevplfgraareKRIEQLRAEREELAE 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1408 SVAKAELEAQELKlKMKEDASQRQG--LAV-----------DAEKQKQNIQLELTQLKNlSEQEIRSKNQQLEEAQVSRR 1474
Cdd:PRK04863 801 RYATLSFDVQKLQ-RLHQAFSRFIGshLAVafeadpeaelrQLNRRRVELERALADHES-QEQQQRSQLEQAKEGLSALN 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1475 KLEEEIHLIriqlqttikqkstADDELQklrDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAE---------DELKR 1545
Cdd:PRK04863 879 RLLPRLNLL-------------ADETLA---DRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSvlqsdpeqfEQLKQ 942
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1546 K---SEAEKEAARQKQKALDEL--QKHKMQAEEAERRLKQAEE--EKVRQIKVVEEVAQKTAATQL-----QAMSFSEKT 1613
Cdd:PRK04863 943 DyqqAQQTQRDAKQQAFALTEVvqRRAHFSYEDAAEMLAKNSDlnEKLRQRLEQAEQERTRAREQLrqaqaQLAQYNQVL 1022
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1614 TKLEESLKKEQGTVLQLQEEAEKLRKQ-----EEEANKAREQAEKELETWRLKANEALRLRLRAEEEAqrkslaqEEAEK 1688
Cdd:PRK04863 1023 ASLKSSYDAKRQMLQELKQELQDLGVPadsgaEERARARRDELHARLSANRSRRNQLEKQLTFCEAEM-------DNLTK 1095
|
....*...
gi 1655220527 1689 QKTEAERD 1696
Cdd:PRK04863 1096 KLRKLERD 1103
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2415-2609 |
2.25e-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: 53.80 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2415 EEEATRFKKQADEAKVRLQETEKQTTETvvqklETQRLQSTREADDLKKAIAELEKERE---------KLKRDAQELQNK 2485
Cdd:pfam15709 330 QEKASRDRLRAERAEMRRLEVERKRREQ-----EEQRRLQQEQLERAEKMREELELEQQrrfeeirlrKQRLEEERQRQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2486 SKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEdekkklqkhledEVNKAKALKDEQQRQQKLMDEEKKKLQAIM 2565
Cdd:pfam15709 405 EEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQE------------EAERAEAEKQRQKELEMQLAEEQKRLMEMA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1655220527 2566 DEA-VKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLRE 2609
Cdd:pfam15709 473 EEErLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1147-1696 |
2.30e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.96 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1147 EEKEVEAHRSQLKaMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQR 1226
Cdd:pfam05483 200 EELRVQAENARLE-MHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1227 elsLLGRHMNSYKQSYEWLIQWLREARLRQEKieaaPVWDSKALKEQLTQEKKLLEEIEKNKD-QIENCQKDAKAYIDSL 1305
Cdd:pfam05483 279 ---LQDENLKELIEKKDHLTKELEDIKMSLQR----SMSTQKALEEDLQIATKTICQLTEEKEaQMEELNKAKAAHSFVV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1306 KDYEFQILAYRALQDPiasplKKPKMESASDNIIQEYVTLRTRYSELSTLTS---------QYIKFILETQRRLEDDEKA 1376
Cdd:pfam05483 352 TEFEATTCSLEELLRT-----EQQRLEKNEDQLKIITMELQKKSSELEEMTKfknnkevelEELKKILAEDEKLLDEKKQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1377 SEKLKEDEK--------------KRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAE---- 1438
Cdd:pfam05483 427 FEKIAEELKgkeqelifllqareKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKeltq 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1439 ---------------------------KQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTI 1491
Cdd:pfam05483 507 easdmtlelkkhqediinckkqeermlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1492 KQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETqKKKNAEDELKRKSEAEKEAARQK-QKALDELQKH-KM 1569
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN-KQLNAYEIKVNKLELELASAKQKfEEIIDNYQKEiED 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1570 QAEEAERRLKQAEEEKV---RQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLqeeaekLRKQEEEANK 1646
Cdd:pfam05483 666 KKISEEKLLEEVEKAKAiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGL------YKNKEQEQSS 739
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1647 AREQAEKELETWRlkaNEALRLRLRAEEEaqrkslaQEEAEKQKTEAERD 1696
Cdd:pfam05483 740 AKAALEIELSNIK---AELLSLKKQLEIE-------KEEKEKLKMEAKEN 779
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1543-1804 |
2.91e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1543 LKRKSEAEKEAARQKQKALDElqkhkmQAEEAERRLKQAEEeKVRQIKvveevaqktaaTQLQAMSFSEKTTKLEESLKk 1622
Cdd:COG3206 162 LEQNLELRREEARKALEFLEE------QLPELRKELEEAEA-ALEEFR-----------QKNGLVDLSEEAKLLLQQLS- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1623 eqgtvlQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKak 1702
Cdd:COG3206 223 ------ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVI-- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1703 aeeaalkqkeNAEKELEKQRtfaEQIAQQklsAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEV---NAAEKQRRQLED 1779
Cdd:COG3206 295 ----------ALRAQIAALR---AQLQQE---AQRILASLEAELEALQAREASLQAQLAQLEARLaelPELEAELRRLER 358
|
250 260
....*....|....*....|....*
gi 1655220527 1780 ELAKVRSEMDALLQmKIQAEKVSQS 1804
Cdd:COG3206 359 EVEVARELYESLLQ-RLEEARLAEA 382
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1436-1694 |
3.04e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1436 DAEKQKQNIQLELTQLKnlseQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVR 1515
Cdd:COG1340 12 ELEEKIEELREEIEELK----EKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1516 KAAQEEAERLRKQVNEETQKKKNaEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEV 1595
Cdd:COG1340 88 NELREELDELRKELAELNKAGGS-IDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1596 AQkTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALR-------- 1667
Cdd:COG1340 167 AE-LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKelrelrke 245
|
250 260
....*....|....*....|....*...
gi 1655220527 1668 -LRLRAEEEAQRKSLAQEEAEKQKTEAE 1694
Cdd:COG1340 246 lKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1629-1873 |
3.11e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1629 QLQEEAEKLRKQEEEANKAREQAEKELEtwrlkanealrlrlraeeeaQRKSLAQEEAEKQKTEAERDakkkakaeeaal 1708
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDARE--------------------QIELLEPIRELAERYAAARE------------ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1709 kQKENAEKELEKQRTFAEQIAQQKLSAEQEyiRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLE-DELAKVRSE 1787
Cdd:COG4913 270 -RLAELEYLRAALRLWFAQRRLELLEAELE--ELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLERE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1788 MDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAIN 1867
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
....*.
gi 1655220527 1868 EATRLK 1873
Cdd:COG4913 427 EIASLE 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2124-2574 |
4.07e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2124 QKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKraaaeaaalKQKQEADAEMAKHKKEAEQALKQKSQVEKEL 2203
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---------LEELREELEKLEKLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2204 GLVKLQLDETDKQKalmdEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAE 2283
Cdd:COG4717 142 AELPERLEELEERL----EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2284 EAEKMKSLAEEAARLSVEAEETARQRKTAEAE--------------LAEQRALAEKMLKEKMQAIQEATKLKAEAEELQK 2349
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2350 QKNQAQEKAKKLLEDKQEIQQRldkETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRfKKQADEAK 2429
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEE---ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL-EELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2430 VRLQETEKQTTETVVQKLETQrlqstREADDLKKAIAELEKEREKLKRDAQE-LQNKSKETASAQQEQMEQQKAMLQQtf 2508
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQA-----EEYQELKEELEELEEQLEELLGELEElLEALDEEELEEELEELEEELEELEE-- 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 2509 ltEKELLLKRERDVEDEKKKLQKhlEDEVNKAKALKDEQQRQQKLMDEE---KKKLQAIMDEAVKKQKE 2574
Cdd:COG4717 447 --ELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEwaaLKLALELLEEAREEYRE 511
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2343-2629 |
4.32e-06 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 51.88 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2343 EAEELQKQKNQAQEKAKKLLEDKQEIQQrLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEE---EAT 2419
Cdd:pfam09728 2 AARELMQLLNKLDSPEEKLAALCKKYAE-LLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKlcrELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2420 RFKKQADEAKVRLQETEKQTTETVVQKLETqrlqstrEADDLKKAIAELEKEREKLKRDAQELQNKSKETAsAQQEQMEQ 2499
Cdd:pfam09728 81 KQNKKLKEESKKLAKEEEEKRKELSEKFQS-------TLKDIQDKMEEKSEKNNKLREENEELREKLKSLI-EQYELREL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2500 Q-KAMLQQTFLTEKELLLKRERDVEDEKKKLQkhlEDEVNKAKALkdeqQRQQKLMDEEKKKLQAIMDEAVKKQKEAE-- 2576
Cdd:pfam09728 153 HfEKLLKTKELEVQLAEAKLQQATEEEEKKAQ---EKEVAKAREL----KAQVQTLSETEKELREQLNLYVEKFEEFQdt 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 2577 ------------AEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2629
Cdd:pfam09728 226 lnksnevfttfkKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLE 290
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1359-1896 |
4.38e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.37 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1359 YIKFILETQRRLEDDEKaSEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEdasqrqglavdAE 1438
Cdd:PRK01156 195 SNLELENIKKQIADDEK-SHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKT-----------AE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1439 KQKQNIQLELTQLKNLSEQEIRSKNqqlEEAQVSRRKLEEEIHLIRiQLQTTIKQKSTADDELQKLRDQaaeaekVRKAA 1518
Cdd:PRK01156 263 SDLSMELEKNNYYKELEERHMKIIN---DPVYKNRNYINDYFKYKN-DIENKKQILSNIDAEINKYHAI------IKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1519 QEEAERlrkqvnEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVV----EE 1594
Cdd:PRK01156 333 VLQKDY------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQeidpDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1595 VAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQ-----------EEEANKAREQAEKELETWRLKAN 1663
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1664 EALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLK 1743
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1744 -ADFEHAEQQRGLLDNE-LQRLKNEVNA----AEKQRRQLEDELAKVRSEMDALLQmKIQAEkvsQSNTEKSKQLLETEA 1817
Cdd:PRK01156 567 rTSWLNALAVISLIDIEtNRSRSNEIKKqlndLESRLQEIEIGFPDDKSYIDKSIR-EIENE---ANNLNNKYNEIQENK 642
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 1818 LKMKQLAEEAARLRSVAEEaKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAED 1896
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAE-IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2426-2644 |
4.47e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 53.29 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2426 DEAKVRLQEtEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQ 2505
Cdd:PRK00409 505 EEAKKLIGE-DKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAK 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2506 QtfltEKELLLKRERDVEDEKKKLQkhledevnKAKALKDEQQRqqklMDEEKKKLQAIMDEAVKKQKEAEAEMKNK--- 2582
Cdd:PRK00409 584 K----EADEIIKELRQLQKGGYASV--------KAHELIEARKR----LNKANEKKEKKKKKQKEKQEELKVGDEVKyls 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2583 --QKeMEALEKKRlEQEKLLADENKKLREKLESLEVTSKQaasKTKEIEVQTDKVPEEQLVSMT 2644
Cdd:PRK00409 648 lgQK-GEVLSIPD-DKEAIVQAGIMKMKVPLSDLEKIQKP---KKKKKKKPKTVKPKPRTVSLE 706
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1788-2239 |
4.51e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1788 MDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEE-AKKQRQLAEDEAARQRAEAEKILKEKLAAI 1866
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1867 NEATRLKTEAEVALKAKEAENERLKRQAED-EAYQRKL--LEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQ 1943
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEElRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1944 KKVVEEEIHIIRINFERASKEKSDLEVELKKLK----------------------GIADETQKSKAKAEEEAEKLKKLAA 2001
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAAleerlkearlllliaaallallGLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2002 EEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEA-AQKSTAAEQKAQDV 2080
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELlREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2081 LSKNKEDLLSQEKLRDEFEnakklaqaaetakekaekeaalLRQKAEEAEKLKKAaedeaakQAKAQKDAERLRKEAEAE 2160
Cdd:COG4717 368 LEQEIAALLAEAGVEDEEE----------------------LRAALEQAEEYQEL-------KEELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2161 AAKRAAAEAAALKQK-QEADAEMAKHKKEAEQALKQKSQVEKELGLVklqldETDKQKALMDEELQRVKAQVNDAVKQKA 2239
Cdd:COG4717 419 EELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQL-----EEDGELAELLQELEELKAELRELAEEWA 493
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1299-1622 |
4.53e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.54 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1299 KAYIDSLKDYEFQILAYRalqdpIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIkfILETQRRLEDDEKASE 1378
Cdd:COG5022 813 RSYLACIIKLQKTIKREK-----KLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETI--YLQSAQRVELAERQLQ 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1379 KLKEDEKKRMAEIQAQLETQKQLAEgHAKSVAKAELEaqelKLKMKEDASQRqglavdAEKQKQNIQLELTQLKNLSEQE 1458
Cdd:COG5022 886 ELKIDVKSISSLKLVNLELESEIIE-LKKSLSSDLIE----NLEFKTELIAR------LKKLLNNIDLEEGPSIEYVKLP 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1459 IRsknQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLR------------ 1526
Cdd:COG5022 955 EL---NKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKelpvevaelqsa 1031
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1527 -KQVNEETQKKK--NAEDELKRKSEAEKEAARQKQKALdELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTaatq 1603
Cdd:COG5022 1032 sKIISSESTELSilKPLQKLKGLLLLENNQLQARYKAL-KLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNR---- 1106
|
330
....*....|....*....
gi 1655220527 1604 lQAMSFSEKTTKLEESLKK 1622
Cdd:COG5022 1107 -NLVKPANVLQFIVAQMIK 1124
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
23-156 |
4.60e-06 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 49.27 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 23 ENVREKYKDErdrvQKKTFTKWVNK---------HLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrERDLVRNVRL 93
Cdd:cd21323 15 EGTQHSYSEE----EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTID-ERAINKKKLT 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 94 PrekgrmrFHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 156
Cdd:cd21323 90 P-------FTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1389-1645 |
4.77e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.38 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1389 AEIQAQLET---QKQLAEghAKSVAKAELEaQELKL-----KMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIR 1460
Cdd:PRK11281 39 ADVQAQLDAlnkQKLLEA--EDKLVQQDLE-QTLALldkidRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1461 SKNQQLEEAQVSRRkLEEeihlIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAE 1540
Cdd:PRK11281 116 ETLSTLSLRQLESR-LAQ----TLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1541 DELKRKSEAE------KEAARQK------------QKALDELQKHKMQAEEA---------ERRLKQAEeekvrqiKVVE 1593
Cdd:PRK11281 191 PSQRVLLQAEqallnaQNDLQRKslegntqlqdllQKQRDYLTARIQRLEHQlqllqeainSKRLTLSE-------KTVQ 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 1594 EVAQKTAATQLQAMSFsekttkleesLKKEQGTVLQLqeeAEKLRKQEEEAN 1645
Cdd:PRK11281 264 EAQSQDEAARIQANPL----------VAQELEINLQL---SQRLLKATEKLN 302
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2254-2420 |
4.79e-06 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 52.70 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2254 ELLKLKVRIEEENLRLMQKNKDNTQKLlAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQA 2333
Cdd:pfam05262 199 DMTDLKERESQEDAKRAQQLKEELDKK-QIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2334 IQeatklKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDK--ETQGFQKSLEAERKRqLEISAEAEKLKLRVKelssAQ 2411
Cdd:pfam05262 278 NQ-----KREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKasEKEAEDKELEAQKKR-EPVAEDLQKTKPQVE----AQ 347
|
....*....
gi 1655220527 2412 AKAEEEATR 2420
Cdd:pfam05262 348 PTSLNEDAI 356
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2283-2611 |
4.95e-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: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2283 EEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEatKLKAEAEELQKQKNQAQEKAKKLL 2362
Cdd:pfam13868 6 DELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEE--EEEKEEERKEERKRYRQELEEQIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2363 EDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEakvRLQETEKQTTET 2442
Cdd:pfam13868 84 EREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE---EEREEDERILEY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2443 VVQKLETQrlqstreaddlkkaiAELEKEREKLKRDAQELQNKsketASAQQEQMEQQKAMLQqtfltekELLLKRERDv 2522
Cdd:pfam13868 161 LKEKAERE---------------EEREAEREEIEEEKEREIAR----LRAQQEKAQDEKAERD-------ELRAKLYQE- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2523 EDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQaimdEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLAD 2602
Cdd:pfam13868 214 EQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLA----EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL 289
|
....*....
gi 1655220527 2603 ENKKLREKL 2611
Cdd:pfam13868 290 EHRRELEKQ 298
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1734-1934 |
5.17e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.16 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1734 SAEQEYIRLKAdfehaeQQRGLLDNELQRLKNEVNAAE--KQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQ 1811
Cdd:TIGR02794 47 AVAQQANRIQQ------QKKPAAKKEQERQKKLEQQAEeaEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1812 LLETEA--LKMKQLAEEAARLRSVAEEAKKQRQL-----AEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKE 1884
Cdd:TIGR02794 121 AEEAKAkqAAEAKAKAEAEAERKAKEEAAKQAEEeakakAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEA 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1885 AENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQK 1934
Cdd:TIGR02794 201 AKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQG 250
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2174-2596 |
5.66e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.59 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2174 QKQEADAEMAKHKKEAEQAlkqKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVndavkqkAQVENELSKVKMQMD 2253
Cdd:pfam07888 35 RLEECLQERAELLQAQEAA---NRQREKEKERYKRDREQWERQRRELESRVAELKEEL-------RQSREKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2254 ELLKLKVRIEEENLRLMQKNKDNTQKLLaEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlAEKMLKEKMQA 2333
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIR-ELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEA-ERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2334 IQEatKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRqleisaeaeklklrvKELSSAQAK 2413
Cdd:pfam07888 183 TEE--ELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALL---------------EELRSLQER 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2414 AEeeatrfkkqadeakvrlqeTEKQTTETVVQKLETQRLQSTReaddlkkAIAELEKEReklkRDAQELQNKSKETASAQ 2493
Cdd:pfam07888 246 LN-------------------ASERKVEGLGEELSSMAAQRDR-------TQAELHQAR----LQAAQLTLQLADASLAL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2494 QE---QMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVK 2570
Cdd:pfam07888 296 REgraRWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV 375
|
410 420
....*....|....*....|....*.
gi 1655220527 2571 KQKEAEAEMKNKQKEMEALekKRLEQ 2596
Cdd:pfam07888 376 AQKEKEQLQAEKQELLEYI--RQLEQ 399
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
630-722 |
6.15e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.71 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 630 HTFVTAATKELMWLNEKEEEEVNYDWSDRNTNMTAKKDNYSGLMRELELREKKVNGVQTTGDKLLRDGHPGRKTIEAFTA 709
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1655220527 710 ALQTQWSWILQLC 722
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2445-2640 |
6.17e-06 |
|
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: 52.75 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2445 QKLETQ-RLQSTREA-DDLKKAIAELEKEREKLKRDA------QELQN-----------KSKETASAQQEQMEQQKAMLQ 2505
Cdd:TIGR02168 173 RRKETErKLERTRENlDRLEDILNELERQLKSLERQAekaeryKELKAelrelelallvLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2506 QTFLTEKELLLKRERDVEDEKKKLQKhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKN---- 2581
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSE-LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEElesk 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 2582 ---KQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2640
Cdd:TIGR02168 332 ldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2043-2599 |
6.52e-06 |
|
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: 52.92 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2043 AEANKLKDKAEKELEKQVI-LAKEAAQKSTAA--EQKAQDVLSKNKE---DLLSQEKLRDEFENAKKLAQAAETAKekae 2116
Cdd:pfam12128 275 ASRQEERQETSAELNQLLRtLDDQWKEKRDELngELSAADAAVAKDRselEALEDQHGAFLDADIETAAADQEQLP---- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2117 keaaLLRQKAEEAEKLKKAAED-----EAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKH----KK 2187
Cdd:pfam12128 351 ----SWQSELENLEERLKALTGkhqdvTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeselRE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2188 EAEQALK----QKSQVEKELGLVKLQLD------ETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDE--- 2254
Cdd:pfam12128 427 QLEAGKLefneEEYRLKSRLGELKLRLNqatatpELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQase 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2255 --------LLKLKVRIEEENLRLMQKN--------------KDNTQKLLAEEAEKMKSLAEEAARLSVEAEETAR----- 2307
Cdd:pfam12128 507 alrqasrrLEERQSALDELELQLFPQAgtllhflrkeapdwEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYgvkld 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2308 -QRKTAEAELAEQRALAEKMLKEKmQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQeiqqrldketQGFQKSleAE 2386
Cdd:pfam12128 587 lKRIDVPEWAASEEELRERLDKAE-EALQSAREKQAAAEEQLVQANGELEKASREETFAR----------TALKNA--RL 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2387 RKRQLEISAEAEKLKLRvKELSSAQAKAEEEATRFKKQAD----EAKVRLQETEKQTTETVVQKLETQRLQSTREADDLK 2462
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKN-KALAERKDSANERLNSLEAQLKqldkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLA 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2463 KAIAELEKEREKLKR--DAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVED-----------EKKKL 2529
Cdd:pfam12128 733 LLKAAIAARRSGAKAelKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwlqRRPRL 812
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2530 QKHLEDEVNKAKALKDEQQRQQKlmdEEKKKLQAIMdeavkkqKEAEAEMKNKQKEMEALEKKRLEQEKL 2599
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIA---DTKLRRAKLE-------MERKASEKQQVRLSENLRGLRCEMSKL 872
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1367-1564 |
6.77e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1367 QRRLEDDEKasEKLKEDEKKRMAEIQAQL--ETQKQLAEGHAKSVAKAeleaqelKLKMKEDASQRQGLAVDAEKQKQNI 1444
Cdd:PRK09510 100 QERLKQLEK--ERLAAQEQKKQAEEAAKQaaLKQKQAEEAAAKAAAAA-------KAKAEAEAKRAAAAAKKAAAEAKKK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1445 QLELTQLKnlseQEIRSKNQQLEEAQVsrrKLEEEihliriqlqttIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAEr 1524
Cdd:PRK09510 171 AEAEAAKK----AAAEAKKKAEAEAAA---KAAAE-----------AKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAA- 231
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1655220527 1525 lrkqvneetQKKKNAEDELKRKSEAEKEAARQKQKALDEL 1564
Cdd:PRK09510 232 ---------AEAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2030-2243 |
6.77e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2030 AAQDEVERLKQKAAEANKLKDKAEKELEKQvilAKEAAQKSTAAEQKAQDVlskNKEDLLSQEKLRDEFENAKKLAQAAE 2109
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQ---AEELQQKQAAEQERLKQL---EKERLAAQEQKKQAEEAAKQAALKQK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2110 TAKEKAEKEAALLRQKAEEAEK----LKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAemakh 2185
Cdd:PRK09510 133 QAEEAAAKAAAAAKAKAEAEAKraaaAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA----- 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 2186 KKEAEQALKQKSQVEKELGLVKlqldETDKQKALMDEELQRVKAQVNDAVKQKAQVEN 2243
Cdd:PRK09510 208 KKKAAAEAKKKAAAEAKAAAAK----AAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2444-2615 |
6.85e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2444 VQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETasaqqeqmeqqkamlqQTFLTEKELLLKrerDVE 2523
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL----------------EKEIKRLELEIE---EVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2524 DEKKKLQKHLeDEVNKAKALK------DEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQE 2597
Cdd:COG1579 73 ARIKKYEEQL-GNVRNNKEYEalqkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|....*...
gi 1655220527 2598 KLLADENKKLREKLESLE 2615
Cdd:COG1579 152 AELEAELEELEAEREELA 169
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2274-2507 |
6.99e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2274 KDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlaekmlkekmqaiqEATKLKAEAEELQKQKNQ 2353
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA--------------EIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2354 AQEKAKKLLEDKQEIQQRLDK-----ETQGFQ------KSLEAERKRQLEISAEAEKLKlrvKELSSAQAKAEEEATRFK 2422
Cdd:COG3883 84 RREELGERARALYRSGGSVSYldvllGSESFSdfldrlSALSKIADADADLLEELKADK---AELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2423 KQADEAKVRLQETEKQTTE--TVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQ 2500
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEqeALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
....*..
gi 1655220527 2501 KAMLQQT 2507
Cdd:COG3883 241 AAAASAA 247
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1711-1899 |
7.26e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1711 KENAEKELEKQRTFAEQIAQQKLS-AEQEYIRLKADFEhaeqqrglldNELQRLKNEVNAAEKQRRQLEDELAKvrsEMD 1789
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFE----------KELRERRNELQKLEKRLLQKEENLDR---KLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1790 ALLQMKIQAEKVSQSNTEKSKQLletealkmKQLAEEAARLRsvaeeaKKQRQLAEDEAARQRAEAEKILKEKLaainea 1869
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQEL--------EKKEEELEELI------EEQLQELERISGLTAEEAKEILLEKV------ 163
|
170 180 190
....*....|....*....|....*....|
gi 1655220527 1870 tRLKTEAEVALKAKEAENErLKRQAEDEAY 1899
Cdd:PRK12704 164 -EEEARHEAAVLIKEIEEE-AKEEADKKAK 191
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2276-2651 |
7.32e-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: 52.26 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2276 NTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKtAEAELAEQRalaEKMLKEKMQAIQEATKLKAEAEELQKQKNqAQ 2355
Cdd:pfam15709 170 HAERELIDKAKRRKGTKTDKTKTPKREREGKVHGE-AEAAVGKSR---ESKAEKKSELISKGKKTGAKRKRTQKERN-LE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2356 EKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQakaeeeatrfkkQADEAKVRLQET 2435
Cdd:pfam15709 245 VAAELSGPDVINSKETEDASERGAFSSDSVVEDPWLSSKYDAEESQVSIDGRSSPT------------QTFVVTGNMESE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2436 EKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELl 2515
Cdd:pfam15709 313 EERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRL- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2516 lkRERDVEDEKkklQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEmeaLEKKRLE 2595
Cdd:pfam15709 392 --RKQRLEEER---QRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKE---LEMQLAE 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 2596 QEKLLADENKKlrEKLESLEvtSKQAASKTKEIEVQTDKVPEEQLVSMTTVETTKK 2651
Cdd:pfam15709 464 EQKRLMEMAEE--ERLEYQR--QKQEAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
2173-2562 |
7.53e-06 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 51.60 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2173 KQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQM 2252
Cdd:pfam15742 6 KLKYQQQEEVQQLRQNLQRLQILCTSAEKELRYERGKNLDLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2253 dELLKLKVR-IEEENLRLMQKNKdnTQKLLAEE--AEKMKSLAEEAARLSVEAE-ETARQRKTAEAELAEQRALAEKM-- 2326
Cdd:pfam15742 86 -KHCQQKIReLELEVLKQAQSIK--SQNSLQEKlaQEKSRVADAEEKILELQQKlEHAHKVCLTDTCILEKKQLEERIke 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2327 -------LKEKMQAIQEATK-LKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLdKETQGFQKSLEAERKRQLEISAEAE 2398
Cdd:pfam15742 163 aseneakLKQQYQEEQQKRKlLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRI-QQQEAQLKQLENEKRKSDEHLKSNQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2399 KLKlrvKELSSAQAKAE---EEATRFKKQADeAKVRlQETEKQTTETVvqKLETQRLQSTREADDLKKAIAELEKEREKL 2475
Cdd:pfam15742 242 ELS---EKLSSLQQEKEalqEELQQVLKQLD-VHVR-KYNEKHHHHKA--KLRRAKDRLVHEVEQRDERIKQLENEIGIL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2476 krdaqelqnksketasaqQEQMEQQKAMlQQTFLTEKELLLKrerdvedEKKKLQKHLEDE---VNKAKALKDEQQRQQK 2552
Cdd:pfam15742 315 ------------------QQQSEKEKAF-QKQVTAQNEILLL-------EKRKLLEQLTEQeelIKNNKRTISSVQNRVN 368
|
410
....*....|
gi 1655220527 2553 LMDEEKKKLQ 2562
Cdd:pfam15742 369 FLDEENKQLQ 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1261-1529 |
7.84e-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: 51.69 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1261 AAPVWDSKALKEQLTQE-KKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRAlqdpiasplkkpkmesasdnii 1339
Cdd:COG4942 12 ALAAAAQADAAAEAEAElEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR---------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1340 qeyvTLRTRYSELSTLTSQyikfILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQEL 1419
Cdd:COG4942 70 ----RIRALEQELAALEAE----LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1420 KLKMKEDASQRQGLAVDAEkqkqniqlELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADD 1499
Cdd:COG4942 142 KYLAPARREQAEELRADLA--------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
250 260 270
....*....|....*....|....*....|
gi 1655220527 1500 ELQKLRDQAAEAEKVRKAAQEEAERLRKQV 1529
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1055-1584 |
7.98e-06 |
|
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: 52.53 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1055 VQSELEGLKKDLNSITEKTE--EILASPQQSSSAPMLRSELDVTLKKMDHVYGLSSVYLDKLKT-----IDIVIRNTKDA 1127
Cdd:pfam12128 359 LEERLKALTGKHQDVTAKYNrrRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESelreqLEAGKLEFNEE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1128 EDTVKSYES----RLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEhy 1203
Cdd:pfam12128 439 EYRLKSRLGelklRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLE-- 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1204 rQLAGSLLERWQAVFAQidlRQRELSLLGRHMNSYKQSYEWLI---QWLRE-------------------ARLRQEKIEA 1261
Cdd:pfam12128 517 -ERQSALDELELQLFPQ---AGTLLHFLRKEAPDWEQSIGKVIspeLLHRTdldpevwdgsvggelnlygVKLDLKRIDV 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1262 aPVW--DSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEfqILAYRALQDpiasplkkpkmesASDNII 1339
Cdd:pfam12128 593 -PEWaaSEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREE--TFARTALKN-------------ARLDLR 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1340 QEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEK----LKEDEKKRMAEIQAQLETQKQLAEGhAKSVA----K 1411
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKkhqaWLEEQKEQKREARTEKQAYWQVVEG-ALDAQlallK 735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1412 AELEAQELKLKMKEDASQRQ------GLAVDAE---KQKQNIQLELTQLKNLS--EQEIRSKNQQLEEAQVSRR------ 1474
Cdd:pfam12128 736 AAIAARRSGAKAELKALETWykrdlaSLGVDPDviaKLKREIRTLERKIERIAvrRQEVLRYFDWYQETWLQRRprlatq 815
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1475 --KLEEEIHLIRIQL-------QTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAE----- 1540
Cdd:pfam12128 816 lsNIERAISELQQQLarliadtKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGErlaql 895
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1655220527 1541 DELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE 1584
Cdd:pfam12128 896 EDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREED 939
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2286-2601 |
8.41e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2286 EKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlaekmlkEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDK 2365
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAE-------KRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2366 QEIQQRLdketqgfqKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEatrfkkqadeakvrlQETEKQTTE---T 2442
Cdd:COG1340 81 DELNEKL--------NELREELDELRKELAELNKAGGSIDKLRKEIERLEWR---------------QQTEVLSPEeekE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2443 VVQKLE--TQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETAsaqqEQMEQQKAMLQQTFLTEKELllkreR 2520
Cdd:COG1340 138 LVEKIKelEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELA----EEAQELHEEMIELYKEADEL-----R 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2521 DVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLL 2600
Cdd:COG1340 209 KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTEELK 288
|
.
gi 1655220527 2601 A 2601
Cdd:COG1340 289 L 289
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2187-2548 |
8.96e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 51.88 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2187 KEAEQALKQKSQVEKELGLVKLQLDETDKQKALMD-EELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEE 2265
Cdd:COG5185 196 KKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINiEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2266 NLRLMQKNKDNTQKLLAEEAEKMKSLAEE---------------AARLSVEAEETARQRKTAEAELAEQRALAEKMLKEK 2330
Cdd:COG5185 276 SSKRLNENANNLIKQFENTKEKIAEYTKSidikkatesleeqlaAAEAEQELEESKRETETGIQNLTAEIEQGQESLTEN 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2331 MQAIQEATK---LKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEisaeaeklklRVKEL 2407
Cdd:COG5185 356 LEAIKEEIEnivGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADR----------QIEEL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2408 SSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREaddLKKAIAELEKEREKLKRDAQELQNKSK 2487
Cdd:COG5185 426 QRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRS---VRSKKEDLNEELTQIESRVSTLKATLE 502
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 2488 ETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKhlEDEVNKAKALKDEQQ 2548
Cdd:COG5185 503 KLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIP--ASELIQASNAKTDGQ 561
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1553-1722 |
9.03e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1553 AARQKQKALDELQKHKMQAEEAERRLKQAEEEkvrqikvVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQE 1632
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAE-------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1633 EAEKLRKQEEEANKARE--QAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQ 1710
Cdd:COG1579 74 RIKKYEEQLGNVRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170
....*....|..
gi 1655220527 1711 KENAEKELEKQR 1722
Cdd:COG1579 154 LEAELEELEAER 165
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2172-2515 |
9.06e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.36 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2172 LKQK-QEADAEMAKHKKEAEQALKQKSQVEKElglVKLQLDETDKQKALMDE------ELQRVKAQVNDAVKQ--KAQVE 2242
Cdd:PRK10929 28 ITQElEQAKAAKTPAQAEIVEALQSALNWLEE---RKGSLERAKQYQQVIDNfpklsaELRQQLNNERDEPRSvpPNMST 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2243 NELSKvkmqmdELLKLKVRIEEENlRLMQKNKDNTQKLlAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAL 2322
Cdd:PRK10929 105 DALEQ------EILQVSSQLLEKS-RQAQQEQDRAREI-SDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2323 AekmlkekMQAiqEATKLKAEAEEL---QKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAE-AE 2398
Cdd:PRK10929 177 A-------LQA--ESAALKALVDELelaQLSANNRQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2399 KL-------------KLRV-KELSSA---QAKAEEEATRFKKQADEAKVRLQETEKQTTETvVQKL-------ETQRLQS 2454
Cdd:PRK10929 248 LLaeqsgdlpksivaQFKInRELSQAlnqQAQRMDLIASQQRQAASQTLQVRQALNTLREQ-SQWLgvsnalgEALRAQV 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 2455 TREAD-----DLKKAIAELEKER-------EKLKRDAQELQNKSKETASAQQEQMEQQKAmlqqtflTEKELL 2515
Cdd:PRK10929 327 ARLPEmpkpqQLDTEMAQLRVQRlryedllNKQPQLRQIRQADGQPLTAEQNRILDAQLR-------TQRELL 392
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1243-1657 |
9.35e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 51.88 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1243 EWLIQWLREARLRQEKIEAAPvwDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAY------- 1315
Cdd:COG5185 157 ETGIIKDIFGKLTQELNQNLK--KLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEiinieea 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1316 -RALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRleDDEKASEKLKEDEKKRMAEI-QA 1393
Cdd:COG5185 235 lKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIK--QFENTKEKIAEYTKSIDIKKaTE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1394 QLETQKQLAEGHAK-SVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVS 1472
Cdd:COG5185 313 SLEEQLAAAEAEQElEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKES 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1473 ----RRKLEEEIHLIRIQLQTTIKQKSTADDELQ----KLRDQAAEAEKVRKAAQEEAERLRKQVNEETQkkknaedelK 1544
Cdd:COG5185 393 ldeiPQNQRGYAQEILATLEDTLKAADRQIEELQrqieQATSSNEEVSKLLNELISELNKVMREADEESQ---------S 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1545 RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKE- 1623
Cdd:COG5185 464 RLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALEn 543
|
410 420 430
....*....|....*....|....*....|....*.
gi 1655220527 1624 --QGTVLQLQEEAEKLRKQEEEANKAREQAEKELET 1657
Cdd:COG5185 544 liPASELIQASNAKTDGQAANLRTAVIDELTQYLST 579
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1430-1778 |
9.72e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1430 RQGLAVDAEKQKQNIQLELTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAA 1509
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1510 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQI 1589
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1590 KVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLR 1669
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1670 LRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHA 1749
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
330 340
....*....|....*....|....*....
gi 1655220527 1750 EQQRGLLDNELQRLKNEVNAAEKQRRQLE 1778
Cdd:COG4372 338 ELADLLQLLLVGLLDNDVLELLSKGAEAG 366
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2172-2423 |
1.03e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2172 LKQKQEADAEMAKHKKE----AEQALKQKSQVEKELGLVKLQLDETDKQKALMDE---ELQRVKAQVNDAVKQKAQVENE 2244
Cdd:COG1340 14 EEKIEELREEIEELKEKrdelNEELKELAEKRDELNAQVKELREEAQELREKRDElneKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2245 LSKVKMQMDELL-------KLKVRIE-------------EENLRLMQKNKDNTQKLlaEEAEKMKSLAEEAARLSVEAEE 2304
Cdd:COG1340 94 LDELRKELAELNkaggsidKLRKEIErlewrqqtevlspEEEKELVEKIKELEKEL--EKAKKALEKNEKLKELRAELKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2305 TARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgFQKSLE 2384
Cdd:COG1340 172 LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE----LRKELK 247
|
250 260 270
....*....|....*....|....*....|....*....
gi 1655220527 2385 AERKRQLEISaeaeklklRVKELSSAQAKAEEEATRFKK 2423
Cdd:COG1340 248 KLRKKQRALK--------REKEKEELEEKAEEIFEKLKK 278
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3948-3986 |
1.06e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.01 E-value: 1.06e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1655220527 3948 YLEGVSCIAGVFVESTKERLSIYQAMKKNMIRPGTAFEL 3986
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1463-1651 |
1.08e-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: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1463 NQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKnAEDE 1542
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK-QAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1543 LKRKSEAEKEaarqkQKALDELQKhkmQAEEaERRLKQAEEEKVRQikvvEEVAQKTAATQLQAMSFSEKTTKLEESLKK 1622
Cdd:TIGR02794 132 AKAKAEAEAE-----RKAKEEAAK---QAEE-EAKAKAAAEAKKKA----EEAKKKAEAEAKAKAEAEAKAKAEEAKAKA 198
|
170 180
....*....|....*....|....*....
gi 1655220527 1623 EQGTVLQLQEEAEKLRKQEEEANKAREQA 1651
Cdd:TIGR02794 199 EAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2122-2629 |
1.10e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2122 LRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAakraaaeaaalKQKQEADAEMAKHKKEAEQALKQKSQVEK 2201
Cdd:PRK01156 192 LKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAM-----------DDYNNLKSALNELSSLEDMKNRYESEIKT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2202 ELGLVKLQLDETDKQKALmDEELQRVkaqVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEEnlrlMQKNKDNTQKLl 2281
Cdd:PRK01156 261 AESDLSMELEKNNYYKEL-EERHMKI---INDPVYKNRNYINDYFKYKNDIENKKQILSNIDAE----INKYHAIIKKL- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2282 aEEAEKMKSLAEEAARlsvEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKL 2361
Cdd:PRK01156 332 -SVLQKDYNDYIKKKS---RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2362 LEDKQEIQQRLDK---ETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQEtekq 2438
Cdd:PRK01156 408 KKELNEINVKLQDissKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEE---- 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2439 ttetvvqkletqrlqstrEADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKR 2518
Cdd:PRK01156 484 ------------------KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKH 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2519 ERDVEDEKKKLQKHLED------EVNKAKALKD--EQQRQQKLMDEEKKKLQAI---MDEAVKKQKEAEAEMKNKQKEME 2587
Cdd:PRK01156 546 DKYEEIKNRYKSLKLEDldskrtSWLNALAVISliDIETNRSRSNEIKKQLNDLesrLQEIEIGFPDDKSYIDKSIREIE 625
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1655220527 2588 AlEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2629
Cdd:PRK01156 626 N-EANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSII 666
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2206-2454 |
1.12e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2206 VKLQLDETDKQKALMDEELQRVKAQVNDAvkqkaqvENELSKVKMQMDEllklkVRIEEENLRLMQKNKDNTQKLLAEEA 2285
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEA-------EAALEEFRQKNGL-----VDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2286 EkmksLAEEAARLSvEAEETARQRKTAEAELAEQRALAekmlkekmQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDK 2365
Cdd:COG3206 234 E----LAEAEARLA-ALRAQLGSGPDALPELLQSPVIQ--------QLRAQLAELEAELAELSARYTPNHPDVIALRAQI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2366 QEIQQRLDKETQGFQKSLEAERkrqleisaeaEKLKLRVKELSSAQAKAEEEATRFKKQADEAKV--RLQETEKQTTETV 2443
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAEL----------EALQAREASLQAQLAQLEARLAELPELEAELRRleREVEVARELYESL 370
|
250
....*....|.
gi 1655220527 2444 VQKLETQRLQS 2454
Cdd:COG3206 371 LQRLEEARLAE 381
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2227-2590 |
1.15e-05 |
|
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: 52.15 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2227 VKAQVNDAVKQKAQVENELSKVKMQMDELLKlkvriEEENLRLMQKNKDNTQKLlAEEAEKMKSLAEEAARLSVEAEETA 2306
Cdd:pfam12128 198 VKSMIVAILEDDGVVPPKSRLNRQQVEHWIR-----DIQAIAGIMKIRPEFTKL-QQEFNTLESAELRLSHLHFGYKSDE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2307 RQrktaEAELAEQRALAEKMLKEKMQAiqeatkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQK----S 2382
Cdd:pfam12128 272 TL----IASRQEERQETSAELNQLLRT------LDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDadieT 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2383 LEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVvqkLETQRLQSTREADDLK 2462
Cdd:pfam12128 342 AAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKI---REARDRQLAVAEDDLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2463 KAIAELEKEREKLKRDAQELQNKSKETAsaqqeqmEQQKAMLQQTFLTEKELLLKRERDvedekkklqkhleDEVNKAKA 2542
Cdd:pfam12128 419 ALESELREQLEAGKLEFNEEEYRLKSRL-------GELKLRLNQATATPELLLQLENFD-------------ERIERARE 478
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1655220527 2543 LKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALE 2590
Cdd:pfam12128 479 EQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1365-1657 |
1.22e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 51.38 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1365 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQ-----LAEGHAKSVAKAELEAQ----ELKLKMKEDASQrQGLAV 1435
Cdd:PRK04778 116 LIEEDIEQILEELQELLESEEKNREEVEQLKDLYRElrkslLANRFSFGPALDELEKQlenlEEEFSQFVELTE-SGDYV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1436 DAEKQKQNIQLELTQLKNLSEQ--EIRSKNQ-----QLEEAQVSRRKLEEE-IHLIRIQLQTTIKQKSTADDELQKL--R 1505
Cdd:PRK04778 195 EAREILDQLEEELAALEQIMEEipELLKELQtelpdQLQELKAGYRELVEEgYHLDHLDIEKEIQDLKEQIDENLALleE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1506 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDEL----QKHKMQAEEAERRlKQA 1581
Cdd:PRK04778 275 LDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIdrvkQSYTLNESELESV-RQL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1582 EEEKVRQIKVVEEVAQKTAAtqlQAMSFSEKTTKLEESLK------KEQgtvLQLQEEAEKLRKQEEEANKAREQAEKEL 1655
Cdd:PRK04778 354 EKQLESLEKQYDEITERIAE---QEIAYSELQEELEEILKqleeieKEQ---EKLSEMLQGLRKDELEAREKLERYRNKL 427
|
..
gi 1655220527 1656 ET 1657
Cdd:PRK04778 428 HE 429
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2282-2507 |
1.32e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2282 AEEAEKMKSLAEEAARLSVEAEETARQRKTAEAE--LAEQRALAEKMLKEKMQAIQE------ATKLKAEAEELQKQKNQ 2353
Cdd:COG3206 144 SPDPELAAAVANALAEAYLEQNLELRREEARKALefLEEQLPELRKELEEAEAALEEfrqkngLVDLSEEAKLLLQQLSE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2354 AQEKAKKLLEDKQEIQQRLDKetqgFQKSLEAERKRQLEISAEAEKLKLRvKELSSAQAKAEEEATRFK------KQADE 2427
Cdd:COG3206 224 LESQLAEARAELAEAEARLAA----LRAQLGSGPDALPELLQSPVIQQLR-AQLAELEAELAELSARYTpnhpdvIALRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2428 AKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQ--EQMEQQKAMLQ 2505
Cdd:COG3206 299 QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARElyESLLQRLEEAR 378
|
..
gi 1655220527 2506 QT 2507
Cdd:COG3206 379 LA 380
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1502-1688 |
1.36e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.37 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1502 QKLRDQAAEAEKVRKaaqeEAERLRKQVNEETQKKKNAEDELKRKSEAE--------KEAARQKQKALDELQKHKM---- 1569
Cdd:PRK00409 530 RELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaikeaKKEADEIIKELRQLQKGGYasvk 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1570 --QAEEAERRLKQAEEEKVRQIKVveevaQKTAATQLQA------MSFSEKTTKLEESLKKEqgtvLQLQEEAEKLR--- 1638
Cdd:PRK00409 606 ahELIEARKRLNKANEKKEKKKKK-----QKEKQEELKVgdevkyLSLGQKGEVLSIPDDKE----AIVQAGIMKMKvpl 676
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 1639 KQEEEANKAREQAEKELETWRLKANEA---LRLR-LRAEEeaqrkslAQEEAEK 1688
Cdd:PRK00409 677 SDLEKIQKPKKKKKKKPKTVKPKPRTVsleLDLRgMRYEE-------ALERLDK 723
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2298-2636 |
1.38e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 51.68 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2298 LSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKL----------KAEAEELQK--------QKNQAQEKAK 2359
Cdd:pfam07111 61 LSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELdalavaekagQAEAEGLRAalagaemvRKNLEEGSQR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2360 KLLEDKQEIQQRLDKETQGFQKSLE--AERKRQLEISAEAEKLKL--RVKELSSAQAKAEEEATRFKKQAD--EAKVRLQ 2433
Cdd:pfam07111 141 ELEEIQRLHQEQLSSLTQAHEEALSslTSKAEGLEKSLNSLETKRagEAKQLAEAQKEAELLRKQLSKTQEelEAQVTLV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2434 ET-EKQTTETVVQKLETQRLQSTREadDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEK 2512
Cdd:pfam07111 221 ESlRKYVGEQVPPEVHSQTWELERQ--ELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2513 EL------LLKRERD-VEDEKKKLQKHLEDEVNKAKALKDE-QQRQQKLMDEEKKklQAIMDEAVK-KQKEAEAE---MK 2580
Cdd:pfam07111 299 EFpkkcrsLLNRWREkVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQVTSQSQE--QAILQRALQdKAAEVEVErmsAK 376
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 2581 NKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVP 2636
Cdd:pfam07111 377 GLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIP 432
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2321-2579 |
1.45e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2321 ALAEKMLKEKMQAIQEATK-----LKAEAEELQKQKNQAQEKAKKLLEDKQEIQqrLDKETQGFQKSLEAERKRQLEISA 2395
Cdd:COG3206 156 ALAEAYLEQNLELRREEARkalefLEEQLPELRKELEEAEAALEEFRQKNGLVD--LSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2396 EAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQttetvvQKLETQRLQSTREADDLKkaiaELEKEREKL 2475
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELE------AELAELSARYTPNHPDVI----ALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2476 KRDAQELQNKSKETASAQQEQMEQQKAMLQQTfltekelllkrerdvedekkklqkhLEDEVNKAKALKDEQQRQQKLMd 2555
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQAREASLQAQ-------------------------LAQLEARLAELPELEAELRRLE- 357
|
250 260
....*....|....*....|....
gi 1655220527 2556 EEKKKLQAIMDEAVKKQKEAEAEM 2579
Cdd:COG3206 358 REVEVARELYESLLQRLEEARLAE 381
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1406-1600 |
1.48e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1406 AKSVAKAEL-EAQELKLKMKEDASQRqglavdAEKQKQNIQL----ELTQLKNLSEQEIRSKNQQLEeaqvsrrkleeei 1480
Cdd:PRK12704 25 RKKIAEAKIkEAEEEAKRILEEAKKE------AEAIKKEALLeakeEIHKLRNEFEKELRERRNELQ------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1481 hliriQLQTTIKQK-STADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQkqk 1559
Cdd:PRK12704 86 -----KLEKRLLQKeENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKE--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1655220527 1560 aldelqkhkMQAEEAErrlKQAEEEKVRQIKVVEEVAQKTA 1600
Cdd:PRK12704 158 ---------ILLEKVE---EEARHEAAVLIKEIEEEAKEEA 186
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1410-1606 |
1.51e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1410 AKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEI-HLIRIQ-- 1486
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELgERARALyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1487 -------LQTTIKQKSTAD-----DELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAA 1554
Cdd:COG3883 98 sggsvsyLDVLLGSESFSDfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 1555 RQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQA 1606
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2487-2629 |
1.61e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2487 KETASAQQEQMEQQ-KAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKalKDEQQRQQKLMDEE---KKKLQ 2562
Cdd:PRK12704 26 KKIAEAKIKEAEEEaKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERR--NELQKLEKRLLQKEenlDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2563 AImdeaVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLrEKLESL--------------EVTSKQAASKTKEI 2628
Cdd:PRK12704 104 LL----EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLtaeeakeillekveEEARHEAAVLIKEI 178
|
.
gi 1655220527 2629 E 2629
Cdd:PRK12704 179 E 179
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2173-2360 |
1.63e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2173 KQKQEADAEMAKHKKEAEQA--LKQKSQVE----KELGLVKLQLDETDKQKAlmDEELQRVKAQVNDAVKQKAQVENELS 2246
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAeeLQQKQAAEqerlKQLEKERLAAQEQKKQAE--EAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2247 KVKMQMDELLKLKVRIEEENLRL----MQKNKDNTQKLLAEEAEKMKSLAEEAARlsveAEETARQRKTAEaelAEQRAL 2322
Cdd:PRK09510 148 KAEAEAKRAAAAAKKAAAEAKKKaeaeAAKKAAAEAKKKAEAEAAAKAAAEAKKK----AEAEAKKKAAAE---AKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 1655220527 2323 AEKmlkeKMQAIQEATKLKAEAEELQKQKNQAQEKAKK 2360
Cdd:PRK09510 221 AEA----KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2301-2441 |
1.68e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2301 EAEETARQRKTAEAELAEQRalaekmlKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLD-----KE 2375
Cdd:COG1579 18 ELDRLEHRLKELPAELAELE-------DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 2376 TQGFQKSLEAERKRQ-------LEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTE 2441
Cdd:COG1579 91 YEALQKEIESLKRRIsdledeiLELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
2305-2628 |
1.70e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.62 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2305 TARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKK-LLEDKQEI----QQRL-DKETQG 2378
Cdd:COG5022 805 LLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRfSLLKKETIylqsAQRVeLAERQL 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2379 FQKSLEAERKRQL-EISAEAEKLKLRVK--ELSSAQAKAE---EEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRL 2452
Cdd:COG5022 885 QELKIDVKSISSLkLVNLELESEIIELKksLSSDLIENLEfktELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVES 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2453 QSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEqqkamlqqtfLTEKELLLKRERDVEDEKKKLQKH 2532
Cdd:COG5022 965 KLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGA----------LQESTKQLKELPVEVAELQSASKI 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2533 LEDEVNKAKALKDEQQrQQKLMDEEKKKLQAIMdEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLE 2612
Cdd:COG5022 1035 ISSESTELSILKPLQK-LKGLLLLENNQLQARY-KALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPA 1112
|
330
....*....|....*.
gi 1655220527 2613 SLEVTSKQAASKTKEI 2628
Cdd:COG5022 1113 NVLQFIVAQMIKLNLL 1128
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1428-1638 |
1.70e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.37 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1428 SQRQGLAVD----AEKQKQNIQLELTQL-KNLSEQEIRSKnQQLEEAQvsrrKLEEEIHLIRIQLQttiKQKSTADDELQ 1502
Cdd:PRK00409 494 AKRLGLPENiieeAKKLIGEDKEKLNELiASLEELERELE-QKAEEAE----ALLKEAEKLKEELE---EKKEKLQEEED 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1503 KLRDQAA-EAEKVRKAAQEEAERLRKQVNEETQKKKNAedelkRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQA 1581
Cdd:PRK00409 566 KLLEEAEkEAQQAIKEAKKEADEIIKELRQLQKGGYAS-----VKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVG 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 1582 EEEKVRQIK----VVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLR 1638
Cdd:PRK00409 641 DEVKYLSLGqkgeVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1679-1880 |
1.72e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1679 KSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDN 1758
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1759 ELQ--RLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALK-------MKQLAEEAAR 1829
Cdd:COG4717 124 LLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslateeeLQDLAEELEE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 1830 LRSVAEEAKKQRQLAEDEAARQRAEAEKiLKEKLAAINEATRLKTEAEVAL 1880
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQ-LENELEAAALEERLKEARLLLL 253
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1224-1775 |
1.81e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.89 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1224 RQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLT---QEKKLLEEIEKNKDQIENCQKDAKA 1300
Cdd:pfam05557 25 HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrLKKKYLEALNKKLNEKESQLADARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1301 YIDSLKD--YEFQILAYRALQDPIASPLKKPKMESASDNI---IQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEK 1375
Cdd:pfam05557 105 VISCLKNelSELRRQIQRAELELQSTNSELEELQERLDLLkakASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1376 ASEKLK--EDEKKRMAEIQAQLETQ----KQLAEGHA-KSVAKAELEAQELKLKMKEDAsqrQGLAVDAEKQKQNIQLEL 1448
Cdd:pfam05557 185 DSEIVKnsKSELARIPELEKELERLrehnKHLNENIEnKLLLKEEVEDLKRKLEREEKY---REEAATLELEKEKLEQEL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1449 TQLKNLSEQ---EIRSK---NQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEA 1522
Cdd:pfam05557 262 QSWVKLAQDtglNLRSPedlSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1523 ERLRKQVNEETQKK-------KNAEDELKrKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEV 1595
Cdd:pfam05557 342 RRLQRRVLLLTKERdgyrailESYDKELT-MSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1596 AQKTAATQLQAMSFSEKTTKLE-ESLKKEQGTvLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKAnealrLRLRAEE 1674
Cdd:pfam05557 421 ERELQALRQQESLADPSYSKEEvDSLRRKLET-LELERQRLREQKNELEMELERRCLQGDYDPKKTKV-----LHLSMNP 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1675 EAQRKSLAQEEAEKQKTEAERdakkkakaeeaALKQKENAEKELEKQRTFAEQIAQQklsAEQEYIRLKADFEHAEQQrg 1754
Cdd:pfam05557 495 AAEAYQQRKNQLEKLQAEIER-----------LKRLLKKLEDDLEQVLRLPETTSTM---NFKEVLDLRKELESAELK-- 558
|
570 580
....*....|....*....|.
gi 1655220527 1755 lldneLQRLKNEVNAAEKQRR 1775
Cdd:pfam05557 559 -----NQRLKEVFQAKIQEFR 574
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1727-1944 |
1.81e-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: 50.23 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1727 QIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRqlEDELAKVrsemdALLQMKIQAEKVSQSNT 1806
Cdd:TIGR02794 58 QKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ--AEQAAKQ-----AEEKQKQAEEAKAKQAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1807 EKSKQLletEALKMKQLAEEAAR------LRSVAEEAKKQRQLAEDEA---ARQRAEAE-KILKEKLAAINEATRLKTEA 1876
Cdd:TIGR02794 131 EAKAKA---EAEAERKAKEEAAKqaeeeaKAKAAAEAKKKAEEAKKKAeaeAKAKAEAEaKAKAEEAKAKAEAAKAKAAA 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 1877 EVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQK 1944
Cdd:TIGR02794 208 EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1555-1739 |
1.83e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1555 RQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVvEEVAQKTAATQLQAmsfsekttkleeslKKEQGTVLQLQEEA 1634
Cdd:COG2268 180 EDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAI-AQANREAEEAELEQ--------------EREIETARIAEAEA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1635 EKLRKQEE---EANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQK 1711
Cdd:COG2268 245 ELAKKKAEerrEAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE 324
|
170 180
....*....|....*....|....*....
gi 1655220527 1712 ENAEKELEKQRTFAEQIAQQKLS-AEQEY 1739
Cdd:COG2268 325 AEAEAEAIRAKGLAEAEGKRALAeAWNKL 353
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1629-1903 |
1.90e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 50.42 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1629 QLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQktEAERdakkkakAEEAAL 1708
Cdd:pfam15558 43 KRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQ--ENQR-------QEKLER 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1709 KQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEM 1788
Cdd:pfam15558 114 ARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1789 DALLqMKIQAEKVSQSNTEKSKQLLETEALKMKQLA----EEAARLRSVAEEAKKQRQ--------LAEDEAARQRAEAE 1856
Cdd:pfam15558 194 EELL-RRLSLEQSLQRSQENYEQLVEERHRELREKAqkeeEQFQRAKWRAEEKEEERQehkealaeLADRKIQQARQVAH 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1655220527 1857 KILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKL 1903
Cdd:pfam15558 273 KTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKE 319
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3079-3112 |
1.94e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.94e-05
10 20 30
....*....|....*....|....*....|....
gi 1655220527 3079 LLEAQAATGFVIDPVKNEKVSVDDAVKSGLVGPE 3112
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1289-1562 |
1.95e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.77 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1289 DQIENCQKDAKAYIDSLKDYEFQ--------ILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYI 1360
Cdd:pfam05262 79 DHILNLRRILAGYLMAAYGYERSdaetiakfITIYNAVYRGDLDYFKEFYKEVVTKSLTKENAGLARRYDQWPGKTQIVI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1361 KFileTQRRLED-----------DEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKsvaKAELEAQELKLKMKEDASQ 1429
Cdd:pfam05262 159 PL---KKNILSGnvsdvdtdsisDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAK---RAQQLKEELDKKQIDADKA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1430 RQGLAV---DAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEeihliriQLQTTIKQKstaDDELQKLRD 1506
Cdd:pfam05262 233 QQKADFaqdNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIE-------KAQIEIKKN---DEEALKAKD 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 1507 QAAEAEKvRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALD 1562
Cdd:pfam05262 303 HKAFDLK-QESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAID 357
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1758-1918 |
2.04e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.19 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1758 NELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQA-EKVSQSNTEKSKQLLET---EALKMKQLAEEAARLRSV 1833
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQlEKERLAAQEQKKQAEEAakqAALKQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1834 AEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKH 1913
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAK 224
|
....*
gi 1655220527 1914 DIQEK 1918
Cdd:PRK09510 225 AAAAK 229
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3946-3983 |
2.08e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.08e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1655220527 3946 KKYLEGVSCIAGVFVESTKERLSIYQAMKKNMIRPGTA 3983
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2526-2635 |
2.10e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2526 KKKLQKHLEDEVNKAKALKDEQQRQQKlmDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENK 2605
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAE--AIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110
....*....|....*....|....*....|
gi 1655220527 2606 KLREKLESLEVTSKQAASKTKEIEVQTDKV 2635
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEEL 133
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2826-2862 |
2.16e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.16e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1655220527 2826 TKFLDVQLATGGIIDPVNSHRLPLQTAYKQGQFDPDM 2862
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2174-2438 |
2.19e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 50.72 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2174 QKQEAD-AEMAKHKKEAEQALKQKSQVEKElglvklqldETDKQKAlmdeelQRVKAQVNDAVKQ-----KAQVENELSK 2247
Cdd:PRK05035 441 IEQEKKkAEEAKARFEARQARLEREKAARE---------ARHKKAA------EARAAKDKDAVAAalarvKAKKAAATQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2248 VKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSlAEEAARLSVEAEETARQRKTAEAELAE-----QRAL 2322
Cdd:PRK05035 506 IVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKA-AVAAAIARAKAKKAAQQAANAEAEEEVdpkkaAVAA 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2323 AEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfqKSLEAERKRQLEISAEAEKLKL 2402
Cdd:PRK05035 585 AIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEP-----EEPVDPRKAAVAAAIARAKARK 659
|
250 260 270
....*....|....*....|....*....|....*.
gi 1655220527 2403 RVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ 2438
Cdd:PRK05035 660 AAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1147-1677 |
2.19e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1147 EEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEhyrqlagSLLERWQAVFAQIDLRQR 1226
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE-------TLEAEIEDLRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1227 ELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLK 1306
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAD 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1307 DYEFQILAYRALQDPIASPLKKP-----KMESASDNIIQEYVTLRTRYSELSTL---TSQYIKFILETQRRLEDDEKASE 1378
Cdd:PRK02224 353 DLEERAEELREEAAELESELEEAreaveDRREEIEELEEEIEELRERFGDAPVDlgnAEDFLEELREERDELREREAELE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1379 KLKEDEKKRMAEIQAQLETQK-----QLAEG--HAKSVA-----KAELEAQELKLKMK-EDASQRQGLAVDAEKQKQNIQ 1445
Cdd:PRK02224 433 ATLRTARERVEEAEALLEAGKcpecgQPVEGspHVETIEedrerVEELEAELEDLEEEvEEVEERLERAEDLVEAEDRIE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1446 lELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERL 1525
Cdd:PRK02224 513 -RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1526 RKqVNEETQKKKNAEDEL-----KRKSEAEKEaaRQKQKALDELQKHKMQAEEA--ERRLKQAEEEKVRQIKVVEEVAQK 1598
Cdd:PRK02224 592 ER-IRTLLAAIADAEDEIerlreKREALAELN--DERRERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEK 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1599 TaatqlqamsfsEKTTKLEESLKKEQGTVLQLQEEAEKLRKqEEEANKAREQAekeLETWRLKAN--EALRLRLRAEEEA 1676
Cdd:PRK02224 669 L-----------DELREERDDLQAEIGAVENELEELEELRE-RREALENRVEA---LEALYDEAEelESMYGDLRAELRQ 733
|
.
gi 1655220527 1677 Q 1677
Cdd:PRK02224 734 R 734
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1455-1942 |
2.35e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1455 SEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLrKQVNEETQ 1534
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDL-SMELEKNN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1535 KKKNAEDELKRkseAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEekvrQIKVVEEVAQKTAATQLQAMSFSEKTT 1614
Cdd:PRK01156 274 YYKELEERHMK---IINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA----EINKYHAIIKKLSVLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1615 KLEEsLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLR------LRAEEEAQRKSLAQEEAEK 1688
Cdd:PRK01156 347 RYDD-LNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQeidpdaIKKELNEINVKLQDISSKV 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1689 QKTEAERDAKKKAKAEEAALKQKENAEKEL---------EKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNE 1759
Cdd:PRK01156 426 SSLNQRIRALRENLDELSRNMEMLNGQSVCpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1760 LQRL-KNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKqlLETEALKMKqlaeeaarlRSVAEEAK 1838
Cdd:PRK01156 506 KEYLeSEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKS--LKLEDLDSK---------RTSWLNAL 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1839 KQRQLAEDEAARQRAEaekilkEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAY----QRKLLEDQAAQhKHD 1914
Cdd:PRK01156 575 AVISLIDIETNRSRSN------EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANnlnnKYNEIQENKIL-IEK 647
|
490 500
....*....|....*....|....*...
gi 1655220527 1915 IQEKITQLQSSSVSELDRQKNIVEETLR 1942
Cdd:PRK01156 648 LRGKIDNYKKQIAEIDSIIPDLKEITSR 675
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4406-4443 |
2.90e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 2.90e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1655220527 4406 QRFLEVQYLTGGLIEPDTTGRVSIDEAVKKGSLDARTA 4443
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1049-1584 |
2.94e-05 |
|
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: 50.82 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1049 TAEQMK--VQSELEGLKKDLNSITEKTEEILASPQQSSSAPMLRSELDVTLKKMDHVYGLSSVYLDKLKTI--------- 1117
Cdd:TIGR00606 602 SLEQNKnhINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLtdenqsccp 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1118 --DIVIRNTKDAEDTVKSYESRLRDV-SKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHS 1194
Cdd:TIGR00606 682 vcQRVFQTEAELQEFISDLQSKLRLApDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1195 ERDAELEHYRQLAGSL---LERWQAVFAQIDLRQRelslLGRHMNSYKQSYEWLIQWLREARLRQEKIEAapvwdSKALK 1271
Cdd:TIGR00606 762 RLKNDIEEQETLLGTImpeEESAKVCLTDVTIMER----FQMELKDVERKIAQQAAKLQGSDLDRTVQQV-----NQEKQ 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1272 EQLTQEKKLLEEIEKNKDQIENCQKDA---KAYIDSLKDYEFQILAYRALQDPIAsplkkpkmesasdniiQEYVTLRTR 1348
Cdd:TIGR00606 833 EKQHELDTVVSKIELNRKLIQDQQEQIqhlKSKTNELKSEKLQIGTNLQRRQQFE----------------EQLVELSTE 896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1349 YSELSTLTSQYIKFILETQRRLEDDEKASEKL--KEDEKKRMAEIQAQLetqkqlaeghaksvakaeleaqelklkMKED 1426
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELisSKETSNKKAQDKVND---------------------------IKEK 949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1427 ASQRQGLAVDAEKQkqnIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRD 1506
Cdd:TIGR00606 950 VKNIHGYMKDIENK---IQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKR 1026
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 1507 QAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKAldELQKHKMQAEEAERRLKQAEEE 1584
Cdd:TIGR00606 1027 ENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGY--EKEIKHFKKELREPQFRDAEEK 1102
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
32-152 |
3.00e-05 |
|
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: 46.52 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 32 ERDRVQKKTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEVLSgetLPRERDLVRNVRLPREKGRMRfhKLQNVQIA 111
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIK---VPVDWNRVNKPPYPKLGENMK--KLENCNYA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655220527 112 LDFLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 152
Cdd:cd21330 82 VELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1631-1766 |
3.05e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.87 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1631 QEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKS---LAQEEAEKQKTEAERDakkKAKAEEAA 1707
Cdd:COG2268 210 RETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETaraEAEAAYEIAEANAERE---VQRQLEIA 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 1708 LKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADfEHAEQQ----RGLLDNELQRLKNE 1766
Cdd:COG2268 287 EREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE-AEAEAEairaKGLAEAEGKRALAE 348
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1386-1673 |
3.13e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.87 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1386 KRMAEIQAQLEtqkQLAEGHAKSVAKaeleaqelKLKMKEDASQRQGLAvdaEKQKQNIQLELT----QLKNLSEQEIRS 1461
Cdd:COG2268 116 RDPEEIEELAE---EKLEGALRAVAA--------QMTVEELNEDREKFA---EKVQEVAGTDLAknglELESVAITDLED 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1462 KNQQLEeAQvSRRKLEEeihLIRIQlqttIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKnAED 1541
Cdd:COG2268 182 ENNYLD-AL-GRRKIAE---IIRDA----RIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAK-KKA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1542 ELKRKSEAEKeaArqkqkaldelqkhkmqaeEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSfsekttkLEESLK 1621
Cdd:COG2268 252 EERREAETAR--A------------------EAEAAYEIAEANAEREVQRQLEIAEREREIELQEKE-------AEREEA 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 1622 KEQGTVlQLQEEAEKLRKQEE---EANKAREQAEKELETWRLKA------NEALRLRLRAE 1673
Cdd:COG2268 305 ELEADV-RKPAEAEKQAAEAEaeaEAEAIRAKGLAEAEGKRALAeawnklGDAAILLMLIE 364
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1671-1872 |
3.34e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1671 RAEEEAQRKSLAQEEAEKQKTEAERDAkkkakaeeaalkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAE 1750
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQQKQAAEQER------------LKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1751 QQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAllqMKIQAEKVSQSNTEKSKQLLETEAlkmKQLAEEAARL 1830
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1655220527 1831 RSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRL 1872
Cdd:PRK09510 218 KAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2324-2502 |
3.65e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.00 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2324 EKMLKEKMQAI---QEATKLKA-EAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLEISAEAEK 2399
Cdd:pfam05262 184 EALREDNEKGVnfrRDMTDLKErESQEDAKRAQQLKEELDKKQIDADKAQQKADFA----QDNADKQRDEVRQKQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2400 lklrvkelssAQAKAEEEATRFKKQADEAKVRLQETEKQTTEtvvQKLETQRLQSTREADDLKKAIAELEKEREKLKRDA 2479
Cdd:pfam05262 260 ----------LPKPADTSSPKEDKQVAENQKREIEKAQIEIK---KNDEEALKAKDHKAFDLKQESKASEKEAEDKELEA 326
|
170 180
....*....|....*....|...
gi 1655220527 2480 QElqnKSKETASAQQEQMEQQKA 2502
Cdd:pfam05262 327 QK---KREPVAEDLQKTKPQVEA 346
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2239-2633 |
3.69e-05 |
|
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: 50.22 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2239 AQVENELSKVKMQMDELLKLKVRIEEENLRL--MQKNKDNTQKLLAEE-AEKMKSLAEEAARLSVE--AEETARQRKTAE 2313
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIasRQEERQETSAELNQLlRTLDDQWKEKRDELNGElsAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2314 AELAEQRALA------EKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEA-- 2385
Cdd:pfam12128 324 LEALEDQHGAfldadiETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKir 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2386 -ERKRQL-EISAEAEKLK--LRvKELSSAQAKAEEEATRFKKQADEAKVRLQE--------TEKQTTETVVQKLETQRLQ 2453
Cdd:pfam12128 404 eARDRQLaVAEDDLQALEseLR-EQLEAGKLEFNEEEYRLKSRLGELKLRLNQatatpellLQLENFDERIERAREEQEA 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2454 STREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQ--------------QKAMLQQTF--LTEKELLLK 2517
Cdd:pfam12128 483 ANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhflrkEAPDWEQSIgkVISPELLHR 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2518 RERDVE------------------------DEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQK 2573
Cdd:pfam12128 563 TDLDPEvwdgsvggelnlygvkldlkridvPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREET 642
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2574 EAEAEMKNKQKEMEAL----EKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTD 2633
Cdd:pfam12128 643 FARTALKNARLDLRRLfdekQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQK 706
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1710-1895 |
3.74e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1710 QKENAEKELEKqrtfAEQiAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMD 1789
Cdd:COG3206 183 QLPELRKELEE----AEA-ALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1790 ALLQmkiqaekvSQSNTEKSKQLLETEAlkmkQLAEEAARL-------RSVAEEAKKQRQLAEDEAARQRAEAE---KIL 1859
Cdd:COG3206 258 ELLQ--------SPVIQQLRAQLAELEA----ELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQRILASLEaelEAL 325
|
170 180 190
....*....|....*....|....*....|....*..
gi 1655220527 1860 KEKLAAINEA-TRLKTEAEvALKAKEAENERLKRQAE 1895
Cdd:COG3206 326 QAREASLQAQlAQLEARLA-ELPELEAELRRLEREVE 361
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4156-4184 |
3.75e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 3.75e-05
10 20
....*....|....*....|....*....
gi 1655220527 4156 VRKRRVVIVDPESGKEMSVYEAYQKGLID 4184
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
23-157 |
3.75e-05 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 46.97 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 23 ENVREKYKDErdrvQKKTFTKWVNK---------HLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrERDLVRNVRL 93
Cdd:cd21325 15 EGTQHSYSEE----EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTID-ERAINKKKLT 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 94 PrekgrmrFHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 157
Cdd:cd21325 90 P-------FIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2359-2625 |
4.05e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 49.69 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2359 KKLLEDKQEIQQR---LDKetqgfQKSLEAERKRQLEisAEAEKLKLRVKELSSAQAKAEEEATRF---KKQADEakvrL 2432
Cdd:pfam05622 3 SEAQEEKDELAQRcheLDQ-----QVSLLQEEKNSLQ--QENKKLQERLDQLESGDDSGTPGGKKYlllQKQLEQ----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2433 QEtekqttetvvqklETQRLQSTReaDDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQE-----QMEQQKAMLQQT 2507
Cdd:pfam05622 72 QE-------------ENFRLETAR--DDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEmdilrESSDKVKKLEAT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2508 FLTEKELL-----LKR------ERDVEDEKKKLQkhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKkqkeAE 2576
Cdd:pfam05622 137 VETYKKKLedlgdLRRqvklleERNAEYMQRTLQ--LEEELKKANALRGQLETYKRQVQELHGKLSEESKKADK----LE 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1655220527 2577 AEMKNKQKEMEALEKkrlEQEKLLAdENKKLREKLESLEVTSKQAASKT 2625
Cdd:pfam05622 211 FEYKKLEEKLEALQK---EKERLII-ERDTLRETNEELRCAQLQQAELS 255
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1268-1657 |
4.29e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 49.85 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1268 KALKEQLTQEKKLLEEIEKNKDQIENCQKdakayidslkdyefQILAYRALQDPIASPLkkpkmesasDNIIQEYVTLRT 1347
Cdd:pfam06160 107 EELDELLESEEKNREEVEELKDKYRELRK--------------TLLANRFSYGPAIDEL---------EKQLAEIEEEFS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1348 RYSELSTlTSQYIK---FILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLEtqkQLAEGHAksvakaELEAQELKLKmk 1424
Cdd:pfam06160 164 QFEELTE-SGDYLEareVLEKLEEETDALEELMEDIPPLYEELKTELPDQLE---ELKEGYR------EMEEEGYALE-- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1425 edasqrqglavdaekqKQNIQLELTQLKN-LSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQK 1503
Cdd:pfam06160 232 ----------------HLNVDKEIQQLEEqLEENLALLENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1504 LRDQAAEAEKVRKAAQEEAERLRK--QVNEEtqkkknaedelkrkseaEKEAARQKQKALDELQKhkmqaeeaerrlkqa 1581
Cdd:pfam06160 296 IEDYLEHAEEQNKELKEELERVQQsyTLNEN-----------------ELERVRGLEKQLEELEK--------------- 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220527 1582 eeekvRQIKVVEEVAQKTAA-TQLQAMsFSEKTTKLEEsLKKEQgtvLQLQEEAEKLRKQEEEANKAREQAEKELET 1657
Cdd:pfam06160 344 -----RYDEIVERLEEKEVAySELQEE-LEEILEQLEE-IEEEQ---EEFKESLQSLRKDELEAREKLDEFKLELRE 410
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1512-1687 |
4.52e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 49.62 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1512 EKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKV 1591
Cdd:pfam05262 180 KKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1592 VEEVAQKTAA---TQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRl 1668
Cdd:pfam05262 260 LPKPADTSSPkedKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQ- 338
|
170
....*....|....*....
gi 1655220527 1669 RLRAEEEAQRKSLAQEEAE 1687
Cdd:pfam05262 339 KTKPQVEAQPTSLNEDAID 357
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1671-1862 |
4.68e-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: 49.56 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1671 RAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEK-----ELEKQRTFAE-QIAQQKLSAEQE------ 1738
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKmreelELEQQRRFEEiRLRKQRLEEERQrqeeee 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1739 ---YIRLKADFEHAEQQRGLLDNELQRLknevnaaEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLlet 1815
Cdd:pfam15709 408 rkqRLQLQAAQERARQQQEEFRRKLQEL-------QRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERL--- 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1655220527 1816 EALKMKQLAEEAARLrsvaeEAKKQRQLAEDEAARQRAEAEKILKEK 1862
Cdd:pfam15709 478 EYQRQKQEAEEKARL-----EAEERRQKEEEAARLALEEAMKQAQEQ 519
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2302-2588 |
4.73e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2302 AEETARQRKTAEAELAEQRAlaekmlkekmqaiqEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQK 2381
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARF--------------EARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2382 SLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEE----EATRFKK---QADEAKVRLQETEKQTTETvvqkletqrlqS 2454
Cdd:PRK05035 502 ATQPIVIKAGARPDNSAVIAAREARKAQARARQAEkqaaAAADPKKaavAAAIARAKAKKAAQQAANA-----------E 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2455 TREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKhLE 2534
Cdd:PRK05035 571 AEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA-VA 649
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2535 DEVNKAKALKDEQQRQQklmdeekkkLQAIMDEAVKKQKEAEAEMKNKQKEMEA 2588
Cdd:PRK05035 650 AAIARAKARKAAQQQAN---------AEPEEAEDPKKAAVAAAIARAKAKKAAQ 694
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1506-1851 |
4.92e-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: 49.56 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1506 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSE---AEKEAARQKQKALDELQKHKMQAEEAERRLKqaE 1582
Cdd:pfam15709 218 EKKSELISKGKKTGAKRKRTQKERNLEVAAELSGPDVINSKETedaSERGAFSSDSVVEDPWLSSKYDAEESQVSID--G 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1583 EEKVRQIKVV-------EEVAQKTAATQLQAMSFSEKTTKleESLKKEQGTVLQLQEEaeklRKQEEEANKAREQAEKEL 1655
Cdd:pfam15709 296 RSSPTQTFVVtgnmeseEERSEEDPSKALLEKREQEKASR--DRLRAERAEMRRLEVE----RKRREQEEQRRLQQEQLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1656 ETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEaerdakkkakaeeaalkqkenaekelEKQRTFAEQIAQQKLSA 1735
Cdd:pfam15709 370 RAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEE--------------------------ERKQRLQLQAAQERARQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1736 EQEYIRLKAdfehAEQQRGLLDNELQRLknevnAAEKQRR-QLEDELAKvrsEMDALLQMKIQAEKVSQSNTEKSKQLLE 1814
Cdd:pfam15709 424 QQEEFRRKL----QELQRKKQQEEAERA-----EAEKQRQkELEMQLAE---EQKRLMEMAEEERLEYQRQKQEAEEKAR 491
|
330 340 350
....*....|....*....|....*....|....*..
gi 1655220527 1815 TEALKMKQLAEEAARLrsVAEEAKKQRQlaedEAARQ 1851
Cdd:pfam15709 492 LEAEERRQKEEEAARL--ALEEAMKQAQ----EQARQ 522
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1457-1727 |
4.94e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.75 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1457 QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEaekVRKAAQEEAERlRKQVNEETQKK 1536
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE---LREEAQELREK-RDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1537 KNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE-------KVRQIKVVEEVAQKtaATQLQAMsf 1609
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRqqtevlsPEEEKELVEKIKEL--EKELEKA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1610 sEKTTKLEESLKKEQGTVLQLQEEAEKLRKQ----EEEANKAREQ---AEKELETWRLKANEALRLRLRAEEEAQRksLA 1682
Cdd:COG1340 153 -KKALEKNEKLKELRAELKELRKEAEEIHKKikelAEEAQELHEEmieLYKEADELRKEADELHKEIVEAQEKADE--LH 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1655220527 1683 QEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQ 1727
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2470-2615 |
5.01e-05 |
|
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: 48.44 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2470 KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMlQQTFLTEKELLLKRERDVEDEKKKlqkhlEDEVNKAKALKDEQQR 2549
Cdd:pfam02841 155 EERDKLEAKYNQVPRKGVKAEEVLQEFLQSKEAV-EEAILQTDQALTAKEKAIEAERAK-----AEAAEAEQELLREKQK 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 2550 QQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMeALEKKRLEQEKLLadeNKKLREKLESLE 2615
Cdd:pfam02841 229 EEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQER-MLEHKLQEQEELL---KEGFKTEAESLQ 290
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1486-1901 |
5.65e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 49.13 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1486 QLQTTIKQKSTADDELQKLRDQ----AAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKAL 1561
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAggleAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1562 DELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQE 1641
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1642 EEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQ 1721
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1722 RTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKV 1801
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1802 SQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALK 1881
Cdd:COG5278 431 ALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLL 510
|
410 420
....*....|....*....|
gi 1655220527 1882 AKEAENERLKRQAEDEAYQR 1901
Cdd:COG5278 511 AAAEAALAAALAAALASAEL 530
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1564-2343 |
5.82e-05 |
|
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: 49.84 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1564 LQKHKMQAEEAERRLKQA-EEEKVRQIKVVEEVAQ-KTAATQLQAMSFSEKTTK-LEESLKKEQGTvlQLQEEAEKLRKQ 1640
Cdd:pfam12128 218 LNRQQVEHWIRDIQAIAGiMKIRPEFTKLQQEFNTlESAELRLSHLHFGYKSDEtLIASRQEERQE--TSAELNQLLRTL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1641 EEEANKAREQAEKELETWRLKANEAlRLRLRAEEEaQRKSLAQEEAEKQKTEAERdakkkakaEEAALKQKENAEKELEK 1720
Cdd:pfam12128 296 DDQWKEKRDELNGELSAADAAVAKD-RSELEALED-QHGAFLDADIETAAADQEQ--------LPSWQSELENLEERLKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1721 QRTfaeqiAQQKLSAEQEYIRLKADFEHAeqqRGLLDNElQRLKNEVNAAEKQRRQLEDELAKVRSEMDallqmkiqaEK 1800
Cdd:pfam12128 366 LTG-----KHQDVTAKYNRRRSKIKEQNN---RDIAGIK-DKLAKIREARDRQLAVAEDDLQALESELR---------EQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1801 VSQSNTEKSKQLLETEAlkmkQLAEEAARLRSV--AEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEV 1878
Cdd:pfam12128 428 LEAGKLEFNEEEYRLKS----RLGELKLRLNQAtaTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1879 ALKAKEAENERL-KRQAEDEAYQRKLleDQAAQHKHDIQEKITQLQSSSV-----SELDRQKNIVEETLRQKKVVEEEIH 1952
Cdd:pfam12128 504 ASEALRQASRRLeERQSALDELELQL--FPQAGTLLHFLRKEAPDWEQSIgkvisPELLHRTDLDPEVWDGSVGGELNLY 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1953 IIRINFERAS-KEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAeeerkrreaeekvKKIAAAEEEAARQRKAA 2031
Cdd:pfam12128 582 GVKLDLKRIDvPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQAN-------------GELEKASREETFARTAL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2032 QDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKsTAAEQKAQDvlskNKEDLLSQEKLRDEFENAKKLAQAaeta 2111
Cdd:pfam12128 649 KNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNS-LEAQLKQLD----KKHQAWLEEQKEQKREARTEKQAY---- 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2112 kekaekeaallRQKAEEAEKLKKAAEDEAAKQAKAQKDAErlrkeaeaeaakraaaeaaaLKQ-KQEADAEMAKHKKEAE 2190
Cdd:pfam12128 720 -----------WQVVEGALDAQLALLKAAIAARRSGAKAE--------------------LKAlETWYKRDLASLGVDPD 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2191 QALKQKSQVEKElgLVKLQLDETDKQKAL-MDEELQRVKAQVNDAVK-QKAQVENELSKVKMQMDELLKlKVRIEEENLR 2268
Cdd:pfam12128 769 VIAKLKREIRTL--ERKIERIAVRRQEVLrYFDWYQETWLQRRPRLAtQLSNIERAISELQQQLARLIA-DTKLRRAKLE 845
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 2269 LMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEEtarqrKTAEAELAEQRALAEKmLKEKMQAIQEATKLKAE 2343
Cdd:pfam12128 846 MERKASEKQQVRLSENLRGLRCEMSKLATLKEDANS-----EQAQGSIGERLAQLED-LKLKRDYLSESVKKYVE 914
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
28-145 |
5.82e-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: 45.72 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 28 KYKDERDRVQKKTFTKWVNKHLMKA--QRHITDLYEDLRDGHNLISLLEVLSGETLPRERDLVRNvrlprekgrmRFHKL 105
Cdd:cd21285 2 KSWEAENGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKN----------RSQMI 71
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1655220527 106 QNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTI 145
Cdd:cd21285 72 ENIDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1386-1797 |
5.91e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1386 KRMAEIQAQLEtqkQLAEGHAKsvakAELEAQELKlKMKEDASQ--RQGLAV----DAEKQKQNIQLELTQLKNL----- 1454
Cdd:COG3096 785 KRLEELRAERD---ELAEQYAK----ASFDVQKLQ-RLHQAFSQfvGGHLAVafapDPEAELAALRQRRSELERElaqhr 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1455 -SEQEIRSKNQQLEEAQVSRRKLEEEIHLIriqlqttikqkstADDELQklrDQAAEAEKVRKAAQEeAERlrkqvneET 1533
Cdd:COG3096 857 aQEQQLRQQLDQLKEQLQLLNKLLPQANLL-------------ADETLA---DRLEELREELDAAQE-AQA-------FI 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1534 QKKKNAEDELKRKSEAekeaARQKQKALDELQKHKMQAEEAERRLKQaeeekvrQIKVVEEVAQKtaatqLQAMSFSEKT 1613
Cdd:COG3096 913 QQHGKALAQLEPLVAV----LQSDPEQFEQLQADYLQAKEQQRRLKQ-------QIFALSEVVQR-----RPHFSYEDAV 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1614 TKLEESlkkeqgtvlqlQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLR--LRAEEEAQRKSLAQEEAEKQK- 1690
Cdd:COG3096 977 GLLGEN-----------SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLasLKSSRDAKQQTLQELEQELEEl 1045
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1691 -----TEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAE---QIAQQKLS-AEQEY-----------------IRLKA 1744
Cdd:COG3096 1046 gvqadAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEaemDSLQKRLRkAERDYkqereqvvqakagwcavLRLAR 1125
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1745 D-------------FEHAEQQRGLLDNELQRLKNEVNAAEKQR---RQLED------------------------ELAKV 1784
Cdd:COG3096 1126 DndverrlhrrelaYLSADELRSMSDKALGALRLAVADNEHLRdalRLSEDprrperkvqfyiavyqhlrerirqDIIRT 1205
|
490
....*....|...
gi 1655220527 1785 RSEMDALLQMKIQ 1797
Cdd:COG3096 1206 DDPVEAIEQMEIE 1218
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2268-2442 |
5.99e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2268 RLMQKNKDNTQKLLAEEaeKMKSLAEEAARlsvEAEETARQRKT-AEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEE 2346
Cdd:PRK12704 22 YFVRKKIAEAKIKEAEE--EAKRILEEAKK---EAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2347 LQKQKNQAQEKAKKLLEDKQEIQQRLdketqgfQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKA------EEEATR 2420
Cdd:PRK12704 97 NLDRKLELLEKREEELEKKEKELEQK-------QQELEKKEEELEELIEEQLQELERISGLTAEEAKEillekvEEEARH 169
|
170 180
....*....|....*....|..
gi 1655220527 2421 fkkqadEAKVRLQETEKQTTET 2442
Cdd:PRK12704 170 ------EAAVLIKEIEEEAKEE 185
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1466-2445 |
6.01e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1466 LEEAQVSRRKLEEEIHLIriqlqtTIKQKSTADD------ELQKLRDQAAEAEKVRKAAqeeaerlRKQVNEETQKKKNA 1539
Cdd:COG3096 245 LEAIRVTQSDRDLFKHLI------TEATNYVAADymrhanERRELSERALELRRELFGA-------RRQLAEEQYRLVEM 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1540 EDELKRKSEAEKEAARQKQKALDELQKHKM---QAEEAERR---LKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKT 1613
Cdd:COG3096 312 ARELEELSARESDLEQDYQAASDHLNLVQTalrQQEKIERYqedLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1614 TKL-------EESLKKEQGTVLQLQEEAEKLRKQE---EEANKAREQAEKELETWRLKANEALRLRLRAEeeaQRKSLAQ 1683
Cdd:COG3096 392 DSLksqladyQQALDVQQTRAIQYQQAVQALEKARalcGLPDLTPENAEDYLAAFRAKEQQATEEVLELE---QKLSVAD 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1684 EEAEkqkteaerdakkkakaeeaalkQKENAEKELEK-----QRTFAEQIAQQKLSaeqEYIRLKADFEHAEQQRGLLdN 1758
Cdd:COG3096 469 AARR----------------------QFEKAYELVCKiagevERSQAWQTARELLR---RYRSQQALAQRLQQLRAQL-A 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1759 ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKvsqsntekskqlletealkmkQLAEEAARLRSVAEEAK 1838
Cdd:COG3096 523 ELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEA---------------------QLEELEEQAAEAVEQRS 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1839 KQRQlAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAyQRKLLEDQAAQHKHDIQEK 1918
Cdd:COG3096 582 ELRQ-QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERER-EATVERDELAARKQALESQ 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1919 ITQLQSSSVSELDRQKNIVEetlRQKKVVEEEIhiirinFERASKEK-----------------SDLEVELKKLKGIADe 1981
Cdd:COG3096 660 IERLSQPGGAEDPRLLALAE---RLGGVLLSEI------YDDVTLEDapyfsalygparhaivvPDLSAVKEQLAGLED- 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1982 tqkSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAaeeeaaRQ-RKAAQDEVERLKQKAAEANKLKDKAEKElekqv 2060
Cdd:COG3096 730 ---CPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSD------RQwRYSRFPEVPLFGRAAREKRLEELRAERD----- 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2061 ILAKEAAQksTAAEQKAQDVLSKNKEDLLSQEkLRDEFEnakklaqaaetakekaekeaallrqkaeeaeklkkaAEDEA 2140
Cdd:COG3096 796 ELAEQYAK--ASFDVQKLQRLHQAFSQFVGGH-LAVAFA------------------------------------PDPEA 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2141 AKQAKAQK--DAERlrkeaeaeaakraaaeaaalkQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKA 2218
Cdd:COG3096 837 ELAALRQRrsELER---------------------ELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRL 895
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2219 lmdEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELlklkvR---IEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEA 2295
Cdd:COG3096 896 ---EELREELDAAQEAQAFIQQHGKALAQLEPLVAVL-----QsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRR 967
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2296 ARLSVEaeetarqrkTAEAELAEQRALAEKmLKEKM-QAIQEATKLKAEAEELQK---QKNQAQEKAKKLLEDKQEIQQR 2371
Cdd:COG3096 968 PHFSYE---------DAVGLLGENSDLNEK-LRARLeQAEEARREAREQLRQAQAqysQYNQVLASLKSSRDAKQQTLQE 1037
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2372 LDKETQ--GFQKSLEAE---RKRQLEISAEAEKLKLRVKELssaqakaEEEATRFKKQADEAKVRLQETEK---QTTETV 2443
Cdd:COG3096 1038 LEQELEelGVQADAEAEeraRIRRDELHEELSQNRSRRSQL-------EKQLTRCEAEMDSLQKRLRKAERdykQEREQV 1110
|
..
gi 1655220527 2444 VQ 2445
Cdd:COG3096 1111 VQ 1112
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2176-2329 |
6.45e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2176 QEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVK------ 2249
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2250 ---MQMDELLKLKVRIEEENLRLMQKnKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKM 2326
Cdd:COG1579 93 alqKEIESLKRRISDLEDEILELMER-IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
...
gi 1655220527 2327 LKE 2329
Cdd:COG1579 172 IPP 174
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2278-2425 |
6.45e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 48.94 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2278 QKLLAEEAEKMKSLAEEAARLSVEAEETARQ---RKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQA 2354
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAKellLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 2355 QEKAKKLLEDKQEIQQRLDKETQGFQK--SLEAERKRQ-----LEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQA 2425
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRvaGLTPEQARKlllklLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2277-2586 |
6.59e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2277 TQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQE 2356
Cdd:COG4372 22 TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2357 KAKKLLEDKQEIQQRLdKETQGFQKSLEAERKrqlEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETE 2436
Cdd:COG4372 102 ELESLQEEAEELQEEL-EELQKERQDLEQQRK---QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2437 KQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLL 2516
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2517 KRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEM 2586
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1148-1541 |
6.80e-05 |
|
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: 49.28 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1148 EKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQRE 1227
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1228 LsllgrhmnsykqsyewliqwlreARLRQEKIEAApvwdsKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAyidslkd 1307
Cdd:TIGR02168 756 L-----------------------TELEAEIEELE-----ERLEEAEEELAEAEAEIEELEAQIEQLKEELKA------- 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1308 yefQILAYRALQDpiasplkkpkmesasdniiqEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKE----- 1382
Cdd:TIGR02168 801 ---LREALDELRA--------------------ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdiesl 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1383 -----DEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQglavDAEKQKQNIQLELTQLkNLSEQ 1457
Cdd:TIGR02168 858 aaeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS----ELRRELEELREKLAQL-ELRLE 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1458 EIRSKNQQLEEAQVSRRKLEEEIHliriqlqttIKQKSTADDELQKLRDQAAEAEKVRKA-----------AQEEAER-- 1524
Cdd:TIGR02168 933 GLEVRIDNLQERLSEEYSLTLEEA---------EALENKIEDDEEEARRRLKRLENKIKElgpvnlaaieeYEELKERyd 1003
|
410
....*....|....*...
gi 1655220527 1525 -LRKQVNEETQKKKNAED 1541
Cdd:TIGR02168 1004 fLTAQKEDLTEAKETLEE 1021
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2365-2597 |
6.81e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2365 KQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLrvKELSSAQAKAEEEatrfKKQADEAKVRLQETEKQTTETVV 2444
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERL--KQLEKERLAAQEQ----KKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2445 QKLETQRLqstrEADDLKKAIAELEK--EREKLKRDAQELQNKSKETASAQQEQMEQQKAmlqqtfltekelllkrerdv 2522
Cdd:PRK09510 140 KAAAAAKA----KAEAEAKRAAAAAKkaAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKA-------------------- 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 2523 edekkklqkhleDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQE 2597
Cdd:PRK09510 196 ------------AAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1347-1903 |
6.94e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.41 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1347 TRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQ-LAEGHAKSVAKAELEA-QELKLKMK 1424
Cdd:PRK10246 297 ERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTwLAEHDRFRQWNNELAGwRAQFSQQT 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1425 EDASQRQGLA--VDAEKQKQNIQLELTQlkNLSEQEIRSKNQQLEEAQVSRRKLeeeihlirIQLQTTIKQkstaddeLQ 1502
Cdd:PRK10246 377 SDREQLRQWQqqLTHAEQKLNALPAITL--TLTADEVAAALAQHAEQRPLRQRL--------VALHGQIVP-------QQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1503 KLRDQAAEAekvRKAAQEEaerlrkqvneetQKKKNAEDELKRKSEAEKEAARQKQKALDELqkhkmqaeeaERRLKQAE 1582
Cdd:PRK10246 440 KRLAQLQVA---IQNVTQE------------QTQRNAALNEMRQRYKEKTQQLADVKTICEQ----------EARIKDLE 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1583 EEKVR----QIKVVEEVAQKTAATQLQAMSFSEKTTKLE------ESLKKEQGTVL-QLQEEAEKLRKQEEEANKAREQA 1651
Cdd:PRK10246 495 AQRAQlqagQPCPLCGSTSHPAVEAYQALEPGVNQSRLDalekevKKLGEEGAALRgQLDALTKQLQRDESEAQSLRQEE 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1652 EKELETWRlKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAeRDAKKKAKAEEAALKQKENAEKELEKQR-TFAEQIAQ 1730
Cdd:PRK10246 575 QALTQQWQ-AVCASLNITLQPQDDIQPWLDAQEEHERQLRLL-SQRHELQGQIAAHNQQIIQYQQQIEQRQqQLLTALAG 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1731 QKLS-----AEQEYIRLKADFEHAEQQRgllDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQ--MKIQAEKVS- 1802
Cdd:PRK10246 653 YALTlpqedEEASWLATRQQEAQSWQQR---QNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDnwRQVHEQCLSl 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1803 --QSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKlaAINEATRLKTEAEVAL 1880
Cdd:PRK10246 730 hsQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLEN--QRQQAQTLVTQTAQAL 807
|
570 580
....*....|....*....|....
gi 1655220527 1881 KAKEAEN-ERLKRQAEDEAYQRKL 1903
Cdd:PRK10246 808 AQHQQHRpDGLDLTVTVEQIQQEL 831
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1437-1606 |
7.47e-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: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1437 AEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRK 1516
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1517 AAQE-----EAERLRKQvNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKhkmqAEEAERrlKQAEEEKVRQIKV 1591
Cdd:TIGR02794 128 QAAEakakaEAEAERKA-KEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA----KAEAEA--KAKAEEAKAKAEA 200
|
170
....*....|....*
gi 1655220527 1592 VEEVAQKTAATQLQA 1606
Cdd:TIGR02794 201 AKAKAAAEAAAKAEA 215
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3484-3521 |
7.67e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 7.67e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1655220527 3484 LPLLEAQFATGGIIDPVSSHRVPNDVAIQRGYLSKQMV 3521
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2383-2616 |
8.63e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.33 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2383 LEAERKRQL-EISAEAEKLKlrvkelSSAQAKAEEEATRFKKQADEAKVRlQETEKQTTETVVQKLETQRlqstreaddl 2461
Cdd:COG2268 186 LDALGRRKIaEIIRDARIAE------AEAERETEIAIAQANREAEEAELE-QEREIETARIAEAEAELAK---------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2462 KKAIAELEKEREKLKRDAQelqnksketASAQQEQMEQQKAMLQQTFLTEKELLLKRERdvedEKKKLQKHLEDEVNKAK 2541
Cdd:COG2268 249 KKAEERREAETARAEAEAA---------YEIAEANAEREVQRQLEIAEREREIELQEKE----AEREEAELEADVRKPAE 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 2542 ALKDEQQRQQKLmDEEKKKLQAIMdEAVKKQKEAEAEMKNKQkemEALEKKRLEQEKLLADENKKLREKLESLEV 2616
Cdd:COG2268 316 AEKQAAEAEAEA-EAEAIRAKGLA-EAEGKRALAEAWNKLGD---AAILLMLIEKLPEIAEAAAKPLEKIDKITI 385
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1266-1566 |
8.72e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1266 DSKALKEQLTQEKKLLEEIEKNKDQIENCQK----------DAKAYIDSLKDYE-------FQILAYRALQDPIASPLKK 1328
Cdd:PRK11281 57 EDKLVQQDLEQTLALLDKIDRQKEETEQLKQqlaqapaklrQAQAELEALKDDNdeetretLSTLSLRQLESRLAQTLDQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1329 pkMESASDNIIQ---EYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRM-AE---IQAQLETQKQL 1401
Cdd:PRK11281 137 --LQNAQNDLAEynsQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLqAEqalLNAQNDLQRKS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1402 AEGH--------------AKSVAKAELEAQEL-------KLKMKE----------DASQRQGLAVDAEKQKQNIQL---- 1446
Cdd:PRK11281 215 LEGNtqlqdllqkqrdylTARIQRLEHQLQLLqeainskRLTLSEktvqeaqsqdEAARIQANPLVAQELEINLQLsqrl 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1447 -ELTQLKN-LSEQEIRSKNQqLEEAQVSRRKLEEEIH-------LIRIQLQTtiKQKSTADDELQKLRDQAAEaekvrka 1517
Cdd:PRK11281 295 lKATEKLNtLTQQNLRVKNW-LDRLTQSERNIKEQISvlkgsllLSRILYQQ--QQALPSADLIEGLADRIAD------- 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1518 aqeeaerLRKQVNEETQKKknaeDELKRKSE-AEKEAARQKQKALDELQK 1566
Cdd:PRK11281 365 -------LRLEQFEINQQR----DALFQPDAyIDKLEAGHKSEVTDEVRD 403
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1448-1693 |
9.33e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.77 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1448 LTQLKNLSEQEIRSKNQQLEEAQVsRRKLEEEIHLIRI--QLQTTIKQKSTADDELQKLRDQaaEAEKVRKAAQEEAERL 1525
Cdd:PRK05771 22 LEALHELGVVHIEDLKEELSNERL-RKLRSLLTKLSEAldKLRSYLPKLNPLREEKKKVSVK--SLEELIKDVEEELEKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1526 RKQVNEETQKKKNAEDELKRKsEAEKEAArQKQKALD-ELQK--------------HKMQAEEAERRLKQAEEEKVRQIK 1590
Cdd:PRK05771 99 EKEIKELEEEISELENEIKEL-EQEIERL-EPWGNFDlDLSLllgfkyvsvfvgtvPEDKLEELKLESDVENVEYISTDK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1591 -------VVEEVAQKTAATQLQAMSFSEKTTKLEESLKkeqgtvlqlqEEAEKLRKQEEEANKAREQAEKELETWrlkAN 1663
Cdd:PRK05771 177 gyvyvvvVVLKELSDEVEEELKKLGFERLELEEEGTPS----------ELIREIKEELEEIEKERESLLEELKEL---AK 243
|
250 260 270
....*....|....*....|....*....|
gi 1655220527 1664 EALRLRLRAEEEAqrkslaqeEAEKQKTEA 1693
Cdd:PRK05771 244 KYLEELLALYEYL--------EIELERAEA 265
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1374-1612 |
9.37e-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: 47.92 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1374 EKASEKLKEDEKKRMAEIQAQLETQKQLAEghaksvaKAELEAQELKLKMKEDASQrqglavdAEKQKQNIQLEltqlkn 1453
Cdd:TIGR02794 58 QKKPAAKKEQERQKKLEQQAEEAEKQRAAE-------QARQKELEQRAAAEKAAKQ-------AEQAAKQAEEK------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1454 lSEQEIRSKNQQLEEAqvsrrkleeeihliriqlqttiKQKSTADDELQKLRDQAAEAEKVRKA-----AQEEAERLRKQ 1528
Cdd:TIGR02794 118 -QKQAEEAKAKQAAEA----------------------KAKAEAEAERKAKEEAAKQAEEEAKAkaaaeAKKKAEEAKKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1529 VNEETQKKKNAE-----DELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQ 1603
Cdd:TIGR02794 175 AEAEAKAKAEAEakakaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
|
....*....
gi 1655220527 1604 LQAMSFSEK 1612
Cdd:TIGR02794 255 AAAGSEVDK 263
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1788-2104 |
9.70e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.58 E-value: 9.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1788 MDALLQMKIQAEKVSQSNTEKSKQLLETEalKMKQLAEEAARlrsvaeEAKKQRQLAEDEAARQRAeaekiLKEKLAAIN 1867
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQE--RLRQEKEEKAR------EVERRRKLEEAEKARQAE-----MDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1868 EATRLKTEAE-----VALKAKEAENERLKRQ--AEDEAYQRKL--LEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVE 1938
Cdd:pfam17380 338 EQERMAMERErelerIRQEERKRELERIRQEeiAMEISRMRELerLQMERQQKNERVRQELEAARKVKILEEERQRKIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1939 ETLRQKKVVEEEIHIIRINFERASKEKsdlevelkklkgiADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIA 2018
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRRLEEER-------------AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2019 AAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELE-KQVILAKEAAQKSTAAEQKAQDVLSKNKEdllSQEKLRDE 2097
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEeRQKAIYEEERRREAEEERRKQQEMEERRR---IQEQMRKA 561
|
....*..
gi 1655220527 2098 FENAKKL 2104
Cdd:pfam17380 562 TEERSRL 568
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1453-1908 |
9.70e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.80 E-value: 9.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1453 NLSEQEIRSKNQQLEEAQVSRRKLEEE----IHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQ 1528
Cdd:COG5185 130 IVALKDELIKVEKLDEIADIEASYGEVetgiIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1529 VNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMS 1608
Cdd:COG5185 210 SETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1609 FSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEAlrlrlraeeeaqrKSLAQEEAEK 1688
Cdd:COG5185 290 QFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIE-------------QGQESLTENL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1689 QKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIR-LKADFEHAEQQRGLLDNELQRLKNEV 1767
Cdd:COG5185 357 EAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAtLEDTLKAADRQIEELQRQIEQATSSN 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1768 NAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKqlLETEALKMKQLAEEAARLRSVAEE--AKKQRQL-- 1843
Cdd:COG5185 437 EEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSK--KEDLNEELTQIESRVSTLKATLEKlrAKLERQLeg 514
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 1844 ---AEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAK---EAENERLKRQAEDEAYQRKLLEDQA 1908
Cdd:COG5185 515 vrsKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKtdgQAANLRTAVIDELTQYLSTIESQQA 585
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1409-1653 |
9.72e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.79 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1409 VAKAELEAQELKLKMKEDASQR--------------------QGLAVDAEKQKQNIQ--LELTQLKNLSEQEIRSKNQQL 1466
Cdd:PRK05035 433 QAKAEIRAIEQEKKKAEEAKARfearqarlerekaarearhkKAAEARAAKDKDAVAaaLARVKAKKAAATQPIVIKAGA 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1467 EEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLrdQAAEAE-KVRKAAQEEAErlRKQVNEETQKKKNAEDEL-- 1543
Cdd:PRK05035 513 RPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAV--AAAIARaKAKKAAQQAAN--AEAEEEVDPKKAAVAAAIar 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1544 -KRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAAtqLQAMSFSEKTTkleeslKK 1622
Cdd:PRK05035 589 aKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA--VAAAIARAKAR------KA 660
|
250 260 270
....*....|....*....|....*....|.
gi 1655220527 1623 EQGTVLQLQEEAEKLRKQEEEANKAREQAEK 1653
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAKAKK 691
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1473-1859 |
1.03e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1473 RRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEkvRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKE 1552
Cdd:PRK04863 781 RAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFS--RFIGSHLAVAFEADPEAELRQLNRRRVELERALADHES 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1553 AARQKQKALDELQKHKMQAEEAERRLKQAEEEKVrqIKVVEEVAQKTAATQlQAMSFSEKTTKLEESLKKEQGTVLQLQE 1632
Cdd:PRK04863 859 QEQQQRSQLEQAKEGLSALNRLLPRLNLLADETL--ADRVEEIREQLDEAE-EAKRFVQQHGNALAQLEPIVSVLQSDPE 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1633 EAEKLRKQEEEANKAREQAEKeletwrlkanealRLRLRAEEEAQRKSLAQEEAEKQKTEAerdakkkAKAEEAALKQKE 1712
Cdd:PRK04863 936 QFEQLKQDYQQAQQTQRDAKQ-------------QAFALTEVVQRRAHFSYEDAAEMLAKN-------SDLNEKLRQRLE 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1713 NAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQ-------------------RLKNEVNAAEKQ 1773
Cdd:PRK04863 996 QAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvpadsgaeerararrdELHARLSANRSR 1075
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1774 RRQLEDELAKVRSEMDALLQmkiQAEKVsqsnTEKSKQLLE--TEALKMKQLAEEAARLRSVaEEAKKQRQLAEDEAARQ 1851
Cdd:PRK04863 1076 RNQLEKQLTFCEAEMDNLTK---KLRKL----ERDYHEMREqvVNAKAGWCAVLRLVKDNGV-ERRLHRRELAYLSADEL 1147
|
....*...
gi 1655220527 1852 RAEAEKIL 1859
Cdd:PRK04863 1148 RSMSDKAL 1155
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1456-1869 |
1.03e-04 |
|
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: 48.60 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1456 EQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKlrDQAAEAEKVRKAAQEEAERLRKQVNEETQK 1535
Cdd:pfam09731 88 QVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLK--EAISKAESATAVAKEAKDDAIQAVKAHTDS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1536 KKNAEDELKRKSEAEKEAARQKQKALDELQKHKM-------------QAEEAERRLKQAEEEKVRQIKVVEEVAQKTA-A 1601
Cdd:pfam09731 166 LKEASDTAEISREKATDSALQKAEALAEKLKEVInlakqseeeaappLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKlV 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1602 TQLQAMSFSEKTTKLEESLKKEQGTVLQLQE----EAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQ 1677
Cdd:pfam09731 246 DQYKELVASERIVFQQELVSIFPDIIPVLKEdnllSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEEL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1678 RKslaQEEAEKQKTEAERDAkkkakaeeaalkQKENAEKELEKQRTFAEQIAQQKLSAEQeyirlkadfehaEQQRGLLD 1757
Cdd:pfam09731 326 DK---LAEELSARLEEVRAA------------DEAQLRLEFEREREEIRESYEEKLRTEL------------ERQAEAHE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1758 nelQRLKNEV--NAAEKQRRQLEDELAKVRSE-------MDALLQMKIQAEKVSQSNTEkskqlLETEALKMKQLAEEAA 1828
Cdd:pfam09731 379 ---EHLKDVLveQEIELQREFLQDIKEKVEEEragrllkLNELLANLKGLEKATSSHSE-----VEDENRKAQQLWLAVE 450
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1655220527 1829 RLRSVAEEAKKQRQLA----EDEAARQRAEAEKILKEKLAAINEA 1869
Cdd:pfam09731 451 ALRSTLEDGSADSRPRplvrELKALKELASDDEVVKAALASLPEE 495
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1483-1622 |
1.04e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.54 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1483 IRIQLQTTIKQKSTADDELQKLRDQAAEAEK-VRKAAQEEAERLRKQVneetQKKKNAEDELKRKSEAEKEAARQKQKAL 1561
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKeQDEASFERLAELRDEL----AELEEELEALKARWEAEKELIEEIQELK 477
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 1562 DELQKHKMQAEEAERRLKQAEEEKVRQIKVVEE----------VAQKTA--ATQLQAmSFSEKTTKLEESLKK 1622
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLREevteediaevVSRWTGipVGKLLE-GEREKLLNLEEELHE 549
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1361-1553 |
1.04e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1361 KFILETQrrLEDDEKASEKLKEDEKKRMaeiqaqlETQKQlaeghaksvaKAELEAQELKLKMKEdasqrqglavDAEKQ 1440
Cdd:PRK12704 26 KKIAEAK--IKEAEEEAKRILEEAKKEA-------EAIKK----------EALLEAKEEIHKLRN----------EFEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1441 KQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKlrdQAAEAEKVRKAAQE 1520
Cdd:PRK12704 77 LRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELERISGLTAE 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1655220527 1521 EA-ERLRKQVNEETQKKKNA---EDELKRKSEAEKEA 1553
Cdd:PRK12704 154 EAkEILLEKVEEEARHEAAVlikEIEEEAKEEADKKA 190
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2180-2625 |
1.05e-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: 48.49 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2180 AEMAKHKKEAEQALKQKSQVEKEL----GLV---KLQLD--ETDKQKALMDEELQRVKAQ-------VNDAVKQKAQVEN 2243
Cdd:pfam05701 49 EEIPEYKKQSEAAEAAKAQVLEELestkRLIeelKLNLEraQTEEAQAKQDSELAKLRVEemeqgiaDEASVAAKAQLEV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2244 ELSKVKMQMDELLKLKvrieeENLRLMQKNKDntqkLLAEEAEKMKSLAEEAARLSVEAEETARQrktAEAELAEQRALA 2323
Cdd:pfam05701 129 AKARHAAAVAELKSVK-----EELESLRKEYA----SLVSERDIAIKRAEEAVSASKEIEKTVEE---LTIELIATKESL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2324 EKM----LKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLledKQEIQQRLDKETQgfqksLEAERKRQLEISAE-AE 2398
Cdd:pfam05701 197 ESAhaahLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRL---NQQLLSAKDLKSK-----LETASALLLDLKAElAA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2399 KLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQET----EKQTTETVVQKLETQRLQStreaddlkkaiaELEKEREK 2474
Cdd:pfam05701 269 YMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVkaniEKAKDEVNCLRVAAASLRS------------ELEKEKAE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2475 LKrDAQELQNKSKETASAQQEQMEQQKamlqqtflTEKELLLKRERDVEDEKKKLQKHLED---EVNKAKALKDEQQrqq 2551
Cdd:pfam05701 337 LA-SLRQREGMASIAVSSLEAELNRTK--------SEIALVQAKEKEAREKMVELPKQLQQaaqEAEEAKSLAQAAR--- 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2552 klmdEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEkkrlEQEKLLADENKKLREKLESLEVTSKQAASKT 2625
Cdd:pfam05701 405 ----EELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAK----ASEKLALAAIKALQESESSAESTNQEDSPRG 470
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1632-1853 |
1.08e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.92 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1632 EEAEKLRKQEEEANKAREQAEKELEtwrlKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQK 1711
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLE----QQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1712 ENAEKELEKQR-TFAEQIAQQKLSAEQEYIRLKADFEHAEQQRgllDNELQRLKNEVNAAEKQRRQLEDELAKVRSEmda 1790
Cdd:TIGR02794 126 AKQAAEAKAKAeAEAERKAKEEAAKQAEEEAKAKAAAEAKKKA---EEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE--- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 1791 llQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRA 1853
Cdd:TIGR02794 200 --AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1251-1690 |
1.11e-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: 48.49 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1251 EARLRQEKIEAAPVWDSKALKEqLTQEKKLLEEIEKNKDQIENCQKDAKayidslKDYEFQILAYRALQDPIA---SPLK 1327
Cdd:pfam05701 50 EIPEYKKQSEAAEAAKAQVLEE-LESTKRLIEELKLNLERAQTEEAQAK------QDSELAKLRVEEMEQGIAdeaSVAA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1328 KPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKkRMAEIQAQLETQKQL------ 1401
Cdd:pfam05701 123 KAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEK-TVEELTIELIATKESlesaha 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1402 ----AEGHAKSVA---------------KAELEAQELK--------LKMKEDASQRQGLAVDAE---------KQKQNIQ 1445
Cdd:pfam05701 202 ahleAEEHRIGAAlareqdklnwekelkQAEEELQRLNqqllsakdLKSKLETASALLLDLKAElaaymesklKEEADGE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1446 LELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRI---QLQ----------TTIKQKSTA--------DDELQKL 1504
Cdd:pfam05701 282 GNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVaaaSLRselekekaelASLRQREGMasiavsslEAELNRT 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1505 RDQAAEAEKVRKAAQEEAERLRKQVNEETQkkknaedelkrksEAEkEAARQKQKALDELQKHKMQAEEAERRLKQAE-- 1582
Cdd:pfam05701 362 KSEIALVQAKEKEAREKMVELPKQLQQAAQ-------------EAE-EAKSLAQAAREELRKAKEEAEQAKAAASTVEsr 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1583 -EEKVRQIKVVEEvAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAE---KLRKQEEEANKAREQAEKELETW 1658
Cdd:pfam05701 428 lEAVLKEIEAAKA-SEKLALAAIKALQESESSAESTNQEDSPRGVTLSLEEYYElskRAHEAEELANKRVAEAVSQIEEA 506
|
490 500 510
....*....|....*....|....*....|....*.
gi 1655220527 1659 RLKANEAL-RLRLRAEEEAQRKS---LAQEEAEKQK 1690
Cdd:pfam05701 507 KESELRSLeKLEEVNREMEERKEalkIALEKAEKAK 542
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2332-2640 |
1.11e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2332 QAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEI---SAEAEKLKLRVKELS 2408
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELeslQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2409 SAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKE 2488
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2489 TASAQQEQMEQQkamlqqtfltEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEA 2568
Cdd:COG4372 202 LAEAEKLIESLP----------RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 2569 VKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2640
Cdd:COG4372 272 DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2335-2507 |
1.17e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 45.72 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2335 QEATKLKAEAEELQKQ-KNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKR-QLEISAEAEKLKLRVKELssaqa 2412
Cdd:pfam01442 4 DSLDELSTYAEELQEQlGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEElQAKLGQNVEELRQRLEPY----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2413 kAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAE-LEKEREKLKRDAQELQNKSKETAS 2491
Cdd:pfam01442 79 -TEELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAErLEELKESLAPYAEEVQAQLSQRLQ 157
|
170
....*....|....*.
gi 1655220527 2492 AQQEQMEQQKAMLQQT 2507
Cdd:pfam01442 158 ELREKLEPQAEDLREK 173
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2278-2639 |
1.26e-04 |
|
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: 48.21 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2278 QKLLAEEAEKMKSLAEEaaRLSVEAEETarqRKTAEAELAEQRALAEKMLKEKMQAIQEAtklkaeAEELQKQKNQAQEK 2357
Cdd:pfam09731 79 SKEPKEEKKQVKIPRQS--GVSSEVAEE---EKEATKDAAEAKAQLPKSEQEKEKALEEV------LKEAISKAESATAV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2358 AKKLLEDKQE-IQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQAdeakvrLQETE 2436
Cdd:pfam09731 148 AKEAKDDAIQaVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDA------APETP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2437 KQTTETvvqklETQRLQSTREADDLKKAIAELEKEREKLKRD-AQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELL 2515
Cdd:pfam09731 222 PKLPEH-----LDNVEEKVEKAQSLAKLVDQYKELVASERIVfQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2516 LKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAimdeaVKKQKEAEAEMKNKQKEMEalEKKRLE 2595
Cdd:pfam09731 297 DQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADE-----AQLRLEFEREREEIRESYE--EKLRTE 369
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1655220527 2596 QEKLLADENKKLREKLESLEVTSKQAAskTKEIEvqtDKVPEEQ 2639
Cdd:pfam09731 370 LERQAEAHEEHLKDVLVEQEIELQREF--LQDIK---EKVEEER 408
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
1501-1695 |
1.29e-04 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 48.45 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1501 LQKLRDQAAEAEKVRK----AAQEEAERLRKQVNEETQKKknAEDELKRKSEAEKEAARQKqkaldelqKHKMQAEEAer 1576
Cdd:PRK14900 834 LAGVIDLAAETARVDKeigkVDQDLAVLERKLQNPSFVQN--APPAVVEKDRARAEELREK--------RGKLEAHRA-- 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1577 RLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEA--------EKLRKQEEEANK-- 1646
Cdd:PRK14900 902 MLSGSEANSARRDTMEIQNEQKPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQAatavasgiEKVAEAVRKTVRrs 981
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1655220527 1647 AREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKqKTEAER 1695
Cdd:PRK14900 982 VKKAAATRAAMKKKVAKKAPAKKAAAKKAAAKKAAAKKKVAK-KAPAKK 1029
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2422-2627 |
1.31e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 48.09 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2422 KKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLK-KAIAELEKEREKLKrdaQELQNKSKETASAQQEQMEQQ 2500
Cdd:NF033838 57 KEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKtEYLYELNVLKEKSE---AELTSKTKKELDAAFEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2501 KAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALK-DEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEM 2579
Cdd:NF033838 134 TLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEiAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKV 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1655220527 2580 KNKQKEMEALEKKRLEQEKllADENKKLREKLESLEVTSKQAASKTKE 2627
Cdd:NF033838 214 ESKKAEATRLEKIKTDREK--AEEEAKRRADAKLKEAVEKNVATSEQD 259
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2255-2429 |
1.39e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.28 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2255 LLKLKVRIEEENLRLmQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQrKTAEAELAEQRALAEKMLKEKMQAI 2334
Cdd:PRK00409 525 LEELERELEQKAEEA-EALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ-AIKEAKKEADEIIKELRQLQKGGYA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2335 QEATKlkaEAEELQKQKNQAQEKAKKLLEDKQEIQQRLD-----KETQGFQKS--LEAERKRQLEISAEAEKLKLRVKEL 2407
Cdd:PRK00409 603 SVKAH---ELIEARKRLNKANEKKEKKKKKQKEKQEELKvgdevKYLSLGQKGevLSIPDDKEAIVQAGIMKMKVPLSDL 679
|
170 180
....*....|....*....|..
gi 1655220527 2408 SSAQAKAEEEATRFKKQADEAK 2429
Cdd:PRK00409 680 EKIQKPKKKKKKKPKTVKPKPR 701
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
36-149 |
1.39e-04 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 44.33 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 36 VQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerdlVRNVRLPREKGRmrfHKLQNVQIALDFL 115
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVP-----LHSFHLTPTSFE---QKVHNVQFAFELM 87
|
90 100 110
....*....|....*....|....*....|....
gi 1655220527 116 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 149
Cdd:cd21306 88 QDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
2127-2279 |
1.41e-04 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 48.21 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2127 EEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAAL-KQKQEADAEMAKHKKEAEQA---LKQKSQVEKE 2202
Cdd:COG1193 521 EELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILeKAREEAEEILREARKEAEELireLREAQAEEEE 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2203 LGLVKLQLDETDKQkalMDEELQRVKA-----------QVNDAVK-----QKAQVENELSK--VKMQMDEllkLKVRIEE 2264
Cdd:COG1193 601 LKEARKKLEELKQE---LEEKLEKPKKkakpakppeelKVGDRVRvlslgQKGEVLEIPKGgeAEVQVGI---LKMTVKL 674
|
170
....*....|....*
gi 1655220527 2265 ENLRLMQKNKDNTQK 2279
Cdd:COG1193 675 SDLEKVEKKKPKKPK 689
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1424-1666 |
1.47e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 47.92 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1424 KEDASQRqgLAVDAEKqkqnIQLELTQLKNLsEQEIRSKNQQLEEAQVSRR----KLEEEIHLIRIQLQTTIKQKstadd 1499
Cdd:pfam09726 393 KPDALVR--LEQDIKK----LKAELQASRQT-EQELRSQISSLTSLERSLKselgQLRQENDLLQTKLHNAVSAK----- 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1500 elQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETqkkknaedelKRKSEAEKEAARQKQKALD------ELQKHKMQAEE 1573
Cdd:pfam09726 461 --QKDKQTVQQLEKRLKAEQEARASAEKQLAEEK----------KRKKEEEATAARAVALAAAsrgectESLKQRKRELE 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1574 AERRLKQAE----EEKVRQIKV-VEEVAQ--------KTAATQLQAMsfSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQ 1640
Cdd:pfam09726 529 SEIKKLTHDiklkEEQIRELEIkVQELRKykesekdtEVLMSALSAM--QDKNQHLENSLSAETRIKLDLFSALGDAKRQ 606
|
250 260
....*....|....*....|....*.
gi 1655220527 1641 EEEANKAREQAEKELETWRLKANEAL 1666
Cdd:pfam09726 607 LEIAQGQIYQKDQEIKDLKQKIAEVM 632
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
59-146 |
1.49e-04 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 44.36 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 59 LYEDLRDGHNLISLLEVLSGETLPRErdlVRNVRLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLT 138
Cdd:cd21294 38 LFDECKDGLVLSKLINDSVPDTIDER---VLNKPPRKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLI 114
|
....*...
gi 1655220527 139 LGLIWTII 146
Cdd:cd21294 115 LGLIWQII 122
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2284-2498 |
1.55e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.56 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2284 EAEKMKSLAE---EAARLSVEAE-ETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKnQAQEKAK 2359
Cdd:COG2268 187 DALGRRKIAEiirDARIAEAEAErETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAE-TARAEAE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2360 KLLEDKQEIQQRldketqgfqksleaERKRQLEIsAEAEKlKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQt 2439
Cdd:COG2268 266 AAYEIAEANAER--------------EVQRQLEI-AERER-EIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE- 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 2440 tetvvqkLETQRLQSTREADDLKKAIAELEKEREKLKRDAqeLQNKSKETASAQQEQME 2498
Cdd:COG2268 329 -------AEAIRAKGLAEAEGKRALAEAWNKLGDAAILLM--LIEKLPEIAEAAAKPLE 378
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1492-1799 |
1.58e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1492 KQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQA 1571
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1572 EEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQA 1651
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1652 EKELetwRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQ 1731
Cdd:COG4372 191 EANR---NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 1732 KLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAE 1799
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1523-1718 |
1.64e-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: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1523 ERLRKQVNEETQKKKNAEDELKRKSEaekEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEvaqktaat 1602
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERESQ---EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ-------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1603 QLQAMSFSEKTTKLEESLKKEQgtvlqLQEEaeklrkQEEEANKAREQAEKeletwrlKANEALRLRLRAEEEAQRKSLA 1682
Cdd:pfam05262 253 KQQEAKNLPKPADTSSPKEDKQ-----VAEN------QKREIEKAQIEIKK-------NDEEALKAKDHKAFDLKQESKA 314
|
170 180 190
....*....|....*....|....*....|....*..
gi 1655220527 1683 QEEAEKQKT-EAERDAKKKAKAEEAALKQKENAEKEL 1718
Cdd:pfam05262 315 SEKEAEDKElEAQKKREPVAEDLQKTKPQVEAQPTSL 351
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1612-1772 |
1.66e-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: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1612 KTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEeeAQRKSLAQEEAEKQKT 1691
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPAD--TSSPKEDKQVAENQKR 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1692 EAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKlsaeqeyirlkadfeHAEQQRGLLD--NELQRLKNEVNA 1769
Cdd:pfam05262 282 EIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDK---------------ELEAQKKREPvaEDLQKTKPQVEA 346
|
...
gi 1655220527 1770 AEK 1772
Cdd:pfam05262 347 QPT 349
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2456-2631 |
1.69e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 46.87 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2456 READDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQqtfltekellLKRERDvedekkklqkHLED 2535
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQ----------LQKEKD----------QLQS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2536 EVNKAKALKD-------EQQRQQKLMDEEKKKLqaiMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLR 2608
Cdd:pfam09728 61 ELSKAILAKSkleklcrELQKQNKKLKEESKKL---AKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELR 137
|
170 180
....*....|....*....|....*....
gi 1655220527 2609 EKLESL----EVTSKQAAS--KTKEIEVQ 2631
Cdd:pfam09728 138 EKLKSLieqyELRELHFEKllKTKELEVQ 166
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2335-2627 |
1.77e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2335 QEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLdketqgfqKSLEAERKrqlEISAEAEKLKLRVKELSSAQAKA 2414
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEEL--------KELAEKRD---ELNAQVKELREEAQELREKRDEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2415 EEEATRFKKQADEAKVRLQETEKQTTEtvVQKLETQRLQSTREADDLKKAIAELEKEreklkrdaQELQNKSKEtasAQQ 2494
Cdd:COG1340 70 NEKVKELKEERDELNEKLNELREELDE--LRKELAELNKAGGSIDKLRKEIERLEWR--------QQTEVLSPE---EEK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2495 EQMEQQKAMLQQTFLTEKELLLKRE-RDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAvkkqK 2573
Cdd:COG1340 137 ELVEKIKELEKELEKAKKALEKNEKlKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEA----D 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2574 EAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKE 2627
Cdd:COG1340 213 ELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2392-2615 |
1.82e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2392 EISAEAEKLKLRVKELSSAQAKAEEEatrfKKQAdEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKE 2471
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDA----REQI-ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2472 REKLKRDAQELQnksketasaqqEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQ 2551
Cdd:COG4913 297 LEELRAELARLE-----------AELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220527 2552 KLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREK---LESLE 2615
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaeIASLE 432
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1438-1573 |
1.96e-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: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1438 EKQKQNIQLELTQLKNL---SEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADD---------ELQKLR 1505
Cdd:COG1579 23 EHRLKELPAELAELEDElaaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyealqkEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 1506 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEE 1573
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2332-2472 |
1.97e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 47.70 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2332 QAIQEATKLKAEAEElQKQKNQAQEKAKKLledKQEIQQRLDKetQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQ 2411
Cdd:PTZ00491 647 DSLQKSVQLAIEITT-KSQEAAARHQAELL---EQEARGRLER--QKMHDKAKAEEQRTKLLELQAESAAVESSGQSRAE 720
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2412 AKAEEEATRFKKQA--DEAKVRLqETEKQTTETVVQKLETQR---LQSTREADDL----KKAIAELEKER 2472
Cdd:PTZ00491 721 ALAEAEARLIEAEAevEQAELRA-KALRIEAEAELEKLRKRQeleLEYEQAQNELeiakAKELADIEATK 789
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1629-1859 |
1.97e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1629 QLQEEAEKLRKQEEEANKAREQAEKELETwrlKANEALRLRlraEEEAQRksLAQEEAEKQKTEAERdakkkakaeeaal 1708
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQK---QAAEQERLK---QLEKER--LAAQEQKKQAEEAAK------------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1709 kQKENAEKELEKQRtfAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQrrqleDELAKVRSEM 1788
Cdd:PRK09510 126 -QAALKQKQAEEAA--AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKA-----EAEAAAKAAA 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 1789 DALLQMKIQAEKVSQSNTEKskqllETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKIL 1859
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKK-----KAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1565-1738 |
2.04e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1565 QKHKMQAEEAERRLKQAEEEKvrqikvvEEVAQKTAATQlqamsfsekttkleESLKKEQGTVLQLQEEaeklRKQEEEA 1644
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQA-------EELQQKQAAEQ--------------ERLKQLEKERLAAQEQ----KKQAEEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1645 NKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAErdakkkakaeeaalKQKENAEKELEKQrtf 1724
Cdd:PRK09510 124 AKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEA--------------EAAKKAAAEAKKK--- 186
|
170
....*....|....
gi 1655220527 1725 AEQIAQQKLSAEQE 1738
Cdd:PRK09510 187 AEAEAAAKAAAEAK 200
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1810-1967 |
2.05e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1810 KQLLETEALKMKQLAE---EAARLRsvAEEAKKQRQL-AEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEA 1885
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKE--AEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1886 ENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQS--SSVSELDRQ--KNIVEETLRqKKVVEEEIHIIRiNFERA 1961
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLTAEeaKEILLEKVE-EEARHEAAVLIK-EIEEE 181
|
....*.
gi 1655220527 1962 SKEKSD 1967
Cdd:PRK12704 182 AKEEAD 187
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1717-2356 |
2.07e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1717 ELEKQRTFAEQIAQQKLSAEQEYIRlKADFEHAEQQRGLLDNELQRLKNEVNAAEKQrrqLEDELAKVRSEMDALlqmKI 1796
Cdd:pfam12128 257 ELRLSHLHFGYKSDETLIASRQEER-QETSAELNQLLRTLDDQWKEKRDELNGELSA---ADAAVAKDRSELEAL---ED 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1797 QAEKVSQSNTEKSKQLLETEALKMKQLAEEAARL-------RSVAEEAKKQRQLAEDEAARQRAEaekiLKEKLAAINEA 1869
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQLPSWQSELENLEERLkaltgkhQDVTAKYNRRRSKIKEQNNRDIAG----IKDKLAKIREA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1870 -TRLKTEAEVALKAKEAEnerlkrqaedeayqrklLEDQAAQHKHDIQEKITQLQSSsVSELDRQKN---IVEETLRQKK 1945
Cdd:pfam12128 406 rDRQLAVAEDDLQALESE-----------------LREQLEAGKLEFNEEEYRLKSR-LGELKLRLNqatATPELLLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1946 VVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAA 2025
Cdd:pfam12128 468 NFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDW 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2026 RQRK---------------------------------------------AAQDEVERLKQKAAEANKLKDKAEKELEKQV 2060
Cdd:pfam12128 548 EQSIgkvispellhrtdldpevwdgsvggelnlygvkldlkridvpewaASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2061 ILAKEAAQKSTAAEQKAQDVLSKNKEDLlsqEKLRDEFENAKklaqaaetakekaekeaallRQKAEEAEKLKKAAEDEA 2140
Cdd:pfam12128 628 VQANGELEKASREETFARTALKNARLDL---RRLFDEKQSEK--------------------DKKNKALAERKDSANERL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2141 AKQAKAQKdaerlrkeaeaeaakraaaeaAALKQKQEADAEMAKHKKEAEQALKQKSQVEKElglvklqldETDKQKALM 2220
Cdd:pfam12128 685 NSLEAQLK---------------------QLDKKHQAWLEEQKEQKREARTEKQAYWQVVEG---------ALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2221 DEELQrvkaqvndavKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLlaEEAEKMKSlaeEAARLSV 2300
Cdd:pfam12128 735 KAAIA----------ARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKI--ERIAVRRQ---EVLRYFD 799
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 2301 EAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQE 2356
Cdd:pfam12128 800 WYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQ 855
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2791-2825 |
2.09e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.09e-04
10 20 30
....*....|....*....|....*....|....*
gi 1655220527 2791 LSAERAATGFKDPYTGAKISVFEAMQKGLIEKDLA 2825
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2123-2500 |
2.17e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2123 RQKaEEAEKLKKAAEDEAAKQAKAQKDAERLrkeaeaeaakraaaeaaalkQKQEADAEMAKHKKEAEQALKQK-SQVEK 2201
Cdd:PRK11281 77 RQK-EETEQLKQQLAQAPAKLRQAQAELEAL--------------------KDDNDEETRETLSTLSLRQLESRlAQTLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2202 ELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKmqmdellklkvrIEEENLRLMQKNKDNT-QKL 2280
Cdd:PRK11281 136 QLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGK------------VGGKALRPSQRVLLQAeQAL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2281 LAEEAEKMKSLAEEAARLSVEAEEtarQRktaeAELAEQRALAEKMLkekmQAIQEA--TKLKAEAEELQKQKNQAQEKA 2358
Cdd:PRK11281 204 LNAQNDLQRKSLEGNTQLQDLLQK---QR----DYLTARIQRLEHQL----QLLQEAinSKRLTLSEKTVQEAQSQDEAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2359 K--------KLLEDKQEIQQRLDKETQG----FQKSLEAerKRQLEISAEAEK-LKLRVKELSSA---------QAKAEE 2416
Cdd:PRK11281 273 RiqanplvaQELEINLQLSQRLLKATEKlntlTQQNLRV--KNWLDRLTQSERnIKEQISVLKGSlllsrilyqQQQALP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2417 EATRFKKQADE-AKVRLQ--ETEKQ-----TTETVVQKLETQrlQSTREADDLKKAIAELEKEREKLKRD---------- 2478
Cdd:PRK11281 351 SADLIEGLADRiADLRLEqfEINQQrdalfQPDAYIDKLEAG--HKSEVTDEVRDALLQLLDERRELLDQlnkqlnnqln 428
|
410 420
....*....|....*....|....*.
gi 1655220527 2479 -AQELQNKSKE---TASAQQEQMEQQ 2500
Cdd:PRK11281 429 lAINLQLNQQQllsVSDSLQSTLTQQ 454
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1744-2592 |
2.34e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1744 ADF-EHAEQQRGLLDNELQrLKNEVNAAEKQRRQLEDELAKVRSEMDALlqmkiqaekvsqsntEKSKQLLETE---ALK 1819
Cdd:COG3096 271 ADYmRHANERRELSERALE-LRRELFGARRQLAEEQYRLVEMARELEEL---------------SARESDLEQDyqaASD 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1820 MKQLAEEAARlrsvAEEAKKQRQLAEDEAARQRAEAEKILKEklaaineATRLKTEAEVALKAKEAENERLKRQAEDeaY 1899
Cdd:COG3096 335 HLNLVQTALR----QQEKIERYQEDLEELTERLEEQEEVVEE-------AAEQLAEAEARLEAAEEEVDSLKSQLAD--Y 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1900 QRKLLEDQ--AAQHKHDIQ--EKITQLqsSSVSELDrQKNIvEETLRQKKVVEEEIHIIRINFER----ASKEKSDLEVE 1971
Cdd:COG3096 402 QQALDVQQtrAIQYQQAVQalEKARAL--CGLPDLT-PENA-EDYLAAFRAKEQQATEEVLELEQklsvADAARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1972 LKKLKGIADETQKSKAKAEEEAEKLKKlaaeeerkrreaeekvkkiaaaeeeaaRQRKAAQDEVERLKQKAAEANKLKDK 2051
Cdd:COG3096 478 YELVCKIAGEVERSQAWQTARELLRRY---------------------------RSQQALAQRLQQLRAQLAELEQRLRQ 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2052 AEKELEKQVILAKEAAQKSTAAEQKaqdvlsknkEDLLS-QEKLRDEFENAKKLAQAAETAkekaekeaalLRQKAEEAE 2130
Cdd:COG3096 531 QQNAERLLEEFCQRIGQQLDAAEEL---------EELLAeLEAQLEELEEQAAEAVEQRSE----------LRQQLEQLR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2131 KLKKAAEDEAAKQAKAQKDAERLrkeaeaeaakrAAAEAAALKQKQEADAEMAkhkkEAEQALKQKSQVEKELGLVKLQL 2210
Cdd:COG3096 592 ARIKELAARAPAWLAAQDALERL-----------REQSGEALADSQEVTAAMQ----QLLEREREATVERDELAARKQAL 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2211 DETDKQKAL----MDEELQRVKAQ--------------VNDAV--------KQKAQVENELSKVKMQMDEL--------- 2255
Cdd:COG3096 657 ESQIERLSQpggaEDPRLLALAERlggvllseiyddvtLEDAPyfsalygpARHAIVVPDLSAVKEQLAGLedcpedlyl 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2256 -------------------LKLKVRIEEENLR---------LMQKNKDNTQKLLAEEAEkmkSLAEEAARLSVEAEETAR 2307
Cdd:COG3096 737 iegdpdsfddsvfdaeeleDAVVVKLSDRQWRysrfpevplFGRAAREKRLEELRAERD---ELAEQYAKASFDVQKLQR 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2308 QRKTAEAELAEQRALA-----EKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKK-------------LLEDkQEIQ 2369
Cdd:COG3096 814 LHQAFSQFVGGHLAVAfapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEqlqllnkllpqanLLAD-ETLA 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2370 QRLDKETQGFQKSLEAERkrqlEISAEAEKLKLRVKELSSAQAKAEEEAtRFKKQADEAKVRLQETEKQT--TETVVQKL 2447
Cdd:COG3096 893 DRLEELREELDAAQEAQA----FIQQHGKALAQLEPLVAVLQSDPEQFE-QLQADYLQAKEQQRRLKQQIfaLSEVVQRR 967
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2448 ETqrlQSTREADDLKKAIAEL-EKEREKLkRDAQELQNKSKETASAQQEQMEQQKAMLQQ---TFLTEKELLlkreRDVE 2523
Cdd:COG3096 968 PH---FSYEDAVGLLGENSDLnEKLRARL-EQAEEARREAREQLRQAQAQYSQYNQVLASlksSRDAKQQTL----QELE 1039
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 2524 DEKKKLQKHLEDE-VNKAKALKDE------QQRQQKlmDEEKKKLQAImdeavkkqkeaEAEMKNKQKEMEALEKK 2592
Cdd:COG3096 1040 QELEELGVQADAEaEERARIRRDElheelsQNRSRR--SQLEKQLTRC-----------EAEMDSLQKRLRKAERD 1102
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
153-263 |
2.57e-04 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 43.64 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 153 DIQVNGQSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ-ENLEQAFSVA 231
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPvTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|..
gi 1655220527 232 ERELGVTRLLDPEDVDVAHPDEKSIITYVSSL 263
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQF 109
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1581-1922 |
2.60e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1581 AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRL 1660
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1661 KANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYI 1740
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1741 RLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKM 1820
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1821 KQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQ 1900
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330 340
....*....|....*....|..
gi 1655220527 1901 RKLLEDQAAQHKHDIQEKITQL 1922
Cdd:COG4372 349 GLLDNDVLELLSKGAEAGVADG 370
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3741-3776 |
2.72e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.72e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1655220527 3741 LNLLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPE 3776
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2299-2552 |
2.74e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2299 SVEAEETARQRKTAEAELAEQRALAEKmlkekmqAIQEATKLKAEaeelQKQKNQAQEKAKKLLEDKQEIQQRLDKETQG 2378
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK-------ERAEADRQRLE----QEKQQQLAAISGSQSQLESTDQNALETNGQA 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2379 FQKSLEAERKrqlEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQ-ADEAKVRLQETEKQTTETVVQKLETQRLQSTRE 2457
Cdd:NF012221 1607 QRDAILEESR---AVTKELTTLAQGLDALDSQATYAGESGDQWRNPfAGGLLDRVQEQLDDAKKISGKQLADAKQRHVDN 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2458 ADDLKKAIAELE---KEREKLKRDAQelQNKSKETASAQQEQMEqqkAMLQQTFLTEKEllLKRERDVEDEKKKLQKHLE 2534
Cdd:NF012221 1684 QQKVKDAVAKSEagvAQGEQNQANAE--QDIDDAKADAEKRKDD---ALAKQNEAQQAE--SDANAAANDAQSRGEQDAS 1756
|
250
....*....|....*....
gi 1655220527 2535 DEVNKA-KALKDEQQRQQK 2552
Cdd:NF012221 1757 AAENKAnQAQADAKGAKQD 1775
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1497-1791 |
2.85e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1497 ADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAER 1576
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1577 RLKQAEEEkvrqikvVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELE 1656
Cdd:COG4372 81 ELEELNEQ-------LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1657 TWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAE 1736
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 1737 QEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAL 1791
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEAL 288
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2356-2608 |
2.89e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2356 EKAKKLL-EDKQEIQQRLdketqgfqKSLEAERKRQLEISAEAEKLKlrvkelssaqakaeEEATRFKKQADEAKVRLQE 2434
Cdd:PRK00409 505 EEAKKLIgEDKEKLNELI--------ASLEELERELEQKAEEAEALL--------------KEAEKLKEELEEKKEKLQE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2435 TEKQttetVVQKLEtqrlqstREAddlKKAIAELEKEREKLKRDAQELQnksKETASAQQEQmeqqkamlqqtfltekel 2514
Cdd:PRK00409 563 EEDK----LLEEAE-------KEA---QQAIKEAKKEADEIIKELRQLQ---KGGYASVKAH------------------ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2515 llkrerDVEDEKKKLQKHLEdEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAE-------MKNKQKEME 2587
Cdd:PRK00409 608 ------ELIEARKRLNKANE-KKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVLSIPDDKEAIvqagimkMKVPLSDLE 680
|
250 260
....*....|....*....|.
gi 1655220527 2588 ALEKKRLEQEKLLADENKKLR 2608
Cdd:PRK00409 681 KIQKPKKKKKKKPKTVKPKPR 701
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2410-2598 |
3.10e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2410 AQAKAEEEATRFKKQADEAKVRL-QE----------TEKQTTETVVQKLET----QRLQSTREADDLKKAIAELEKEREK 2474
Cdd:NF012221 1552 KQDDAAQNALADKERAEADRQRLeQEkqqqlaaisgSQSQLESTDQNALETngqaQRDAILEESRAVTKELTTLAQGLDA 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2475 LKRDAQ-------------------ELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDV---EDEKKKLQKH 2532
Cdd:NF012221 1632 LDSQATyagesgdqwrnpfagglldRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVaqgEQNQANAEQD 1711
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 2533 LEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKK--QKEAEAEMKNKQKEMEALEKKRLEQEK 2598
Cdd:NF012221 1712 IDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgeQDASAAENKANQAQADAKGAKQDESDK 1779
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2027-2238 |
3.15e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2027 QRKAAQDEVERLKQKAAEANKlKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLlsQEKLRDEFENAKKLAQ 2106
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEK-QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE--EAKAKQAAEAKAKAEA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2107 AAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQ---AKAQKDAER-----LRKEAEAEAAKRAAaeaaalkqkQEA 2178
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAeaeAKAKAEAEAkakaeEAKAKAEAAKAKAA---------AEA 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 2179 DAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQK------ALMDEELQRVKAQVNDAVKQK 2238
Cdd:TIGR02794 210 AAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAGSEVDKYAAIIQQAIQQN 275
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3116-3147 |
3.16e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.16e-04
10 20 30
....*....|....*....|....*....|..
gi 1655220527 3116 QLLSAERAVSGYKDPYTGKTVSLFEAMNKGLI 3147
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1583-1832 |
3.19e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 45.97 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1583 EEKVRQIKVVeeVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKA 1662
Cdd:pfam17045 9 QELMKQIDIM--VAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYEQQLQKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1663 NEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQK--ENAEKELEKQRTFAEQIAQQKLSAEQEYI 1740
Cdd:pfam17045 87 QEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKslEWEQQRLQYQQQVASLEAQRKALAEQSSL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1741 RLKADF----EHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMD--ALLQMKIQAEKvsqsntEKSKQLLE 1814
Cdd:pfam17045 167 IQSAAYqvqlEGRKQCLEASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSelGDSNRKLLEEQ------QRLLEELR 240
|
250
....*....|....*...
gi 1655220527 1815 TEALKMKQLAEEAARLRS 1832
Cdd:pfam17045 241 MSQRQLQVLQNELMELKA 258
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
2260-2600 |
3.33e-04 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 46.96 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2260 VRIEEENLRLMQKNKDNTQKLLAE-EAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEAT 2338
Cdd:pfam14817 50 VRKIRGNLLWYGGLQDKGKAESRQsAAARRLELQKEIERLRAEISRLDKQLEARELELSREEAERERALDEISDSRHRQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2339 KLKAeaeelqkQKNQAQEKAKKLLEDKQEIQQRLDketqgfqksleaeRKRQLEISAEAEKLKLRVKELSSAQAKAEEEA 2418
Cdd:pfam14817 130 LLEA-------YDQQCEEARKILAEDHQRLQGQLQ-------------QLRDAARKAEKEVVFGDSKGSKSSVIALEPQV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2419 TRFKKQADEAKVR----LQETE-KQTTETVVQKLETQR----LQSTREADDLK-----------------KAIAELEKER 2472
Cdd:pfam14817 190 LRDVREACELRAQflqeLLESSlKAYEGSGIHMNRDQRraviQHWLSAVETLLtshppshllqalehlaaREKTAIQEET 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2473 EKL--KRDAQELQNK---------SKETASAQQEQ---MEQQKAMLQQtFLTEKELLLKRERdvedekkKLQKHLE---D 2535
Cdd:pfam14817 270 ESLdvRADAEALRFRyesnhlldvSSDESSDLPSVrqlLERQWAHVQQ-FLNELAETRSRCQ-------QLQARLQglkD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2536 EVNK-----AKALKDEQQRQQKLMDE-----EKKKLQAIMDE------AVKKQKEAEAEMKNKQKEMEALEKKRLEQEKL 2599
Cdd:pfam14817 342 EAELeslgiGDTSQNDSLLRQVLELElqaagLAASRDTLRSEcqqlnkLARERQEALRSLQKKWQRILDFRQLVSELQEQ 421
|
.
gi 1655220527 2600 L 2600
Cdd:pfam14817 422 I 422
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
20-156 |
3.46e-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: 43.84 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 20 QAYENVREKYKDErdrvQKKTFTKWVNK---------HLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrERDLVRN 90
Cdd:cd21324 12 QSSAGTQHSYSEE----EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTID-ERTINKK 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 91 VRLPrekgrmrFHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 156
Cdd:cd21324 87 KLTP-------FTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2752-2785 |
3.52e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 3.52e-04
10 20 30
....*....|....*....|....*....|....
gi 1655220527 2752 LLEAQAASGYIVDPVKNKLLTVDEAVKEELIGPE 2785
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1279-2656 |
3.65e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.35 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1279 KLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDPiasplkkpkmESASDNIIQEyvTLRTRYSElstlTSQ 1358
Cdd:TIGR01612 755 KILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYND----------QINIDNIKDE--DAKQNYDK----SKE 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1359 YIKFIletqrRLEDDEkaSEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQ------- 1431
Cdd:TIGR01612 819 YIKTI-----SIKEDE--IFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISDDKlndyekk 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1432 ---------GLAVDAEKQKQNIQ--------LELTQLKNLSEQEIRSKNQQLEEaqvsrrKLEEEIHLIRiqlQTTIKQK 1494
Cdd:TIGR01612 892 fndskslinEINKSIEEEYQNINtlkkvdeyIKICENTKESIEKFHNKQNILKE------ILNKNIDTIK---ESNLIEK 962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1495 STADDELQKLRDQAAEAEKVRKAAQEEAERLRKqvNEETQKKKNAEDEL-KRKSEAEKEAARQKQKALDELQKhkmQAEE 1573
Cdd:TIGR01612 963 SYKDKFDNTLIDKINELDKAFKDASLNDYEAKN--NELIKYFNDLKANLgKNKENMLYHQFDEKEKATNDIEQ---KIED 1037
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1574 AERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSfsekttklEESLKKEQGTVLQLQEEAEKLR-------------KQ 1640
Cdd:TIGR01612 1038 ANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLN--------KEILEEAEINITNFNEIKEKLKhynfddfgkeeniKY 1109
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1641 EEEANKAREQAEkeletwrlKANEALRLRLRAEEEAQRKSlaqeeaekqkteaerdakkkakaeeaalkqkENAEKELEK 1720
Cdd:TIGR01612 1110 ADEINKIKDDIK--------NLDQKIDHHIKALEEIKKKS-------------------------------ENYIDEIKA 1150
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1721 QRTFAEQIAQQKLSAE--------QEYIRLKADfehaeqQRGLLDNELQRLKNEVNAAEKQRRQLEdelaKVRS------ 1786
Cdd:TIGR01612 1151 QINDLEDVADKAISNDdpeeiekkIENIVTKID------KKKNIYDEIKKLLNEIAEIEKDKTSLE----EVKGinlsyg 1220
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1787 -EMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRaeaekilKEKLAA 1865
Cdd:TIGR01612 1221 kNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDK-------DHHIIS 1293
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1866 INEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQaaQHKHDIQEKITQLQS-SSVSELDRQKNIVEETLRQK 1944
Cdd:TIGR01612 1294 KKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQ--KHNSDINLYLNEIANiYNILKLNKIKKIIDEVKEYT 1371
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1945 KVVEEEIHIIRINFERAS------KEKSDLE---------VELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRRE 2009
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSEklikkiKDDINLEeckskiestLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNEN 1451
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2010 AEEKVKKIAAAEEEAARQRKAAQD--------EVERLKQKAAEANKLKDKAE---KELEKQVILAKEAAQKSTAAEQKAQ 2078
Cdd:TIGR01612 1452 VLLLFKNIEMADNKSQHILKIKKDnatndhdfNINELKEHIDKSKGCKDEADknaKAIEKNKELFEQYKKDVTELLNKYS 1531
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2079 DVLSKNKEDLLSQ--EKLRDEFENAKKLAQAAETAKekaekeaallRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLrke 2156
Cdd:TIGR01612 1532 ALAIKNKFAKTKKdsEIIIKEIKDAHKKFILEAEKS----------EQKIKEIKKEKFRIEDDAAKNDKSNKAAIDI--- 1598
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2157 aeaeaakraaaeAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDET------DKQKALMD--EELQRVK 2228
Cdd:TIGR01612 1599 ------------QLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTelkengDNLNSLQEflESLKDQK 1666
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2229 AQVNDAVKQKAQVENELSKVKMQMDELLK-LKVRIEEENLRLMQKNK---DNTQKLLAEEAEKMKSLAEEAARLSVEAEE 2304
Cdd:TIGR01612 1667 KNIEDKKKELDELDSEIEKIEIDVDQHKKnYEIGIIEKIKEIAIANKeeiESIKELIEPTIENLISSFNTNDLEGIDPNE 1746
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2305 TARQRKTAEAELAEQ--------RALAEKMLKEKMQAIQ-EATKLKAEAEELqkqKN-QAQEKAKKLLEDKQ-------- 2366
Cdd:TIGR01612 1747 KLEEYNTEIGDIYEEfielyniiAGCLETVSKEPITYDEiKNTRINAQNEFL---KIiEIEKKSKSYLDDIEakefdrii 1823
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2367 -EIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELS---------------------SAQAKAEEEATRFKKQ 2424
Cdd:TIGR01612 1824 nHFKKKLDHVNDKFTKEYSKINEGFDDISKSIENVKNSTDENLlfdilnktkdayagiigkkyySYKDEAEKIFINISKL 1903
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2425 ADEAKVRLQETE-----KQTTETVVQKLETqrlqstrEADDLKKAIAELEKERE---KLKRDAQELQNKSKETASAQQEQ 2496
Cdd:TIGR01612 1904 ANSINIQIQNNSgidlfDNINIAILSSLDS-------EKEDTLKFIPSPEKEPEiytKIRDSYDTLLDIFKKSQDLHKKE 1976
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2497 MEQQKAMLQQTFLTEK------------ELLLKRERDVEDekKKLQKHLEDEVNKAKA----------LKDEQQRQQKLM 2554
Cdd:TIGR01612 1977 QDTLNIIFENQQLYEKiqasnelkdtlsDLKYKKEKILND--VKLLLHKFDELNKLSCdsqnydtileLSKQDKIKEKID 2054
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2555 DEEKKKLQAIMDEAVKKQKEaeaEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDK 2634
Cdd:TIGR01612 2055 NYEKEKEKFGIDFDVKAMEE---KFDNDIKDIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKIIEDK 2131
|
1530 1540 1550
....*....|....*....|....*....|....*...
gi 1655220527 2635 VPEE-----QLVSM----------TTVETTK-KVFNGS 2656
Cdd:TIGR01612 2132 IIEKndlidKLIEMrkecllfsyaTLVETLKsKVINHS 2169
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1915-2371 |
3.69e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1915 IQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLkgiadETQKSKAKAEEEAE 1994
Cdd:COG4717 61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1995 KLKKLAAEEERKRREAEEKVKKIaaaeEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAE 2074
Cdd:COG4717 136 ALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2075 QKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLR 2154
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2155 KEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKL--QLDETDKQKALMDEELQRVKA-QV 2231
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRieELQELLREAEELEEELQLEELeQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2232 NDAVKQKAQVENE--LSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEkmkSLAEEAARLSVEAEETARQR 2309
Cdd:COG4717 372 IAALLAEAGVEDEeeLRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE---ELEEELEELEEELEELEEEL 448
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2310 KTAEAELAEQRALAEKMLKEK--MQAIQEATKLKAEAEELQKQKnQAQEKAKKLLEDKQEIQQR 2371
Cdd:COG4717 449 EELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEW-AALKLALELLEEAREEYRE 511
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2141-2484 |
3.80e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2141 AKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALM 2220
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2221 DEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNkdntQKLLAEEAEKMKSLAEEAARLSV 2300
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI----AELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2301 EAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQ 2380
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2381 KSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADD 2460
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
330 340
....*....|....*....|....
gi 1655220527 2461 LKKAIAELEKEREKLKRDAQELQN 2484
Cdd:COG4372 322 LELAKKLELALAILLAELADLLQL 345
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1677-1896 |
3.81e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1677 QRKSLAQEEAEKQKTEAERdakkkakaeeaalkQKENAEKELEKQRTFaEQIAQQKLSAEQEYirlkadfEHAEQQRGll 1756
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQ--------------AEELQQKQAAEQERL-KQLEKERLAAQEQK-------KQAEEAAK-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1757 dnelQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQllETEALKMKQLAEEAARLRSVAEE 1836
Cdd:PRK09510 126 ----QAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAA--KKAAAEAKKKAEAEAAAKAAAEA 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 1837 AKKQRQLAEDEA---ARQRAEAEKilkeKLAAINEATRLKTEAEVALKAKEAENERLKRQAED 1896
Cdd:PRK09510 200 KKKAEAEAKKKAaaeAKKKAAAEA----KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1652-1894 |
4.00e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 46.51 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1652 EKELETWRLKANEalrlrlRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQ 1731
Cdd:PRK07735 4 EKDLEDLKKEAAR------RAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1732 KLSAEQEYI---RLKADFEHAEQQRGlldnELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEK 1808
Cdd:PRK07735 78 KREGTEEVTeeeKAKAKAKAAAAAKA----KAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1809 SKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAED-------EAARQRAEAEKILKEKLAAI-----------NEAT 1870
Cdd:PRK07735 154 TEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGteevteeEKAKAKAKAAAAAKAKAAALakqkasqgngdSGDE 233
|
250 260
....*....|....*....|....
gi 1655220527 1871 RLKTEAEVALKAKEAENERLKRQA 1894
Cdd:PRK07735 234 DAKAKAIAAAKAKAAAAARAKTKG 257
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2429-2629 |
4.02e-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: 46.43 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2429 KVRLQETEKQTTEtVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQK--AMLQQ 2506
Cdd:pfam07888 33 QNRLEECLQERAE-LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKelSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2507 TFLTEKELLLkrerDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEM 2586
Cdd:pfam07888 112 ELSEEKDALL----AQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1655220527 2587 EALEKKRLEQEKLLADENK---KLREKLESLEVTSKQAASKTKEIE 2629
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTqvlQLQDTITTLTQKLTTAHRKEAENE 233
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1533-1734 |
4.13e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1533 TQKKKNAEDELKR-KSEAEKEAARQKQKALdelqkhkMQAEEAERRLKQAEEEKVRQIKvveevaqktaatqlqamsfsE 1611
Cdd:PRK12704 30 EAKIKEAEEEAKRiLEEAKKEAEAIKKEAL-------LEAKEEIHKLRNEFEKELRERR--------------------N 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1612 KTTKLEESLK-KEQgtvlQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKS-LAQEEAEKQ 1689
Cdd:PRK12704 83 ELQKLEKRLLqKEE----NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgLTAEEAKEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1690 ---KTEAErdakkkAKAEEAALKQ------KENAEKELEK------QRTFAEQIAQQKLS 1734
Cdd:PRK12704 159 lleKVEEE------ARHEAAVLIKeieeeaKEEADKKAKEilaqaiQRCAADHVAETTVS 212
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1456-1566 |
4.14e-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: 43.20 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1456 EQEIRsknQQLEEAQVSRRKLEEeihliriqlqttikQKSTADDELQKLRdqaAEAEKVRKAAQEEAERLRKQVNEETQK 1535
Cdd:cd06503 32 EEKIA---ESLEEAEKAKEEAEE--------------LLAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEILAEAKE 91
|
90 100 110
....*....|....*....|....*....|.
gi 1655220527 1536 KKNaedelKRKSEAEKEAARQKQKALDELQK 1566
Cdd:cd06503 92 EAE-----RILEQAKAEIEQEKEKALAELRK 117
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1510-1854 |
4.22e-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: 46.44 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1510 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDElqkhkmQAEEAERRLKQAEEEKVRQI 1589
Cdd:pfam15964 357 QCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQ------NVAQLEAQVEKVTREKNSLV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1590 KVVEEVAQKTAAtqlQAMSFSEKTTKLEESLKKEQgtvlQLQEEAEK-LRKQEEEANKAREQAEKELETWRLKANEAlrl 1668
Cdd:pfam15964 431 SQLEEAQKQLAS---QEMDVTKVCGEMRYQLNQTK----MKKDEAEKeHREYRTKTGRQLEIKDQEIEKLGLELSES--- 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1669 RLRAEEEAQRKSLAQEEAEKQK---TEAERDAKKKAKaeeaalkqkenaEKElEKQRTFAEQIAQQKLSAEQEYIRLKAD 1745
Cdd:pfam15964 501 KQRLEQAQQDAARAREECLKLTellGESEHQLHLTRL------------EKE-SIQQSFSNEAKAQALQAQQREQELTQK 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1746 FEHAEQQRGLLDNELQRLKNEVNAAEKQRRQ--------LEDELAKVRSEMDALLQ----MKIQAEKVSQSNTEKSKQLL 1813
Cdd:pfam15964 568 MQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEecctlakkLEEITQKSRSEVEQLSQekeyLQDRLEKLQKRNEELEEQCV 647
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 1814 ------ETEALKMKQL-------AEEAARLRSVAEEAKKQRQLAEDEAARQRAE 1854
Cdd:pfam15964 648 qhgrmhERMKQRLRQLdkhcqatAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1434-1587 |
4.23e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.56 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1434 AVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHliriQLQTTIKQKSTADDELQKLRDQAAEAEK 1513
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIK----KLESSIKQVEEELEELKEQNEELEKQYK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1514 VRKA-------AQEEAERLRKQVNEETQKKKNAEDE-------LKRKSEAEKEAARQK----QKALDELQKHKMQAEEAE 1575
Cdd:pfam05667 388 VKKKtldllpdAEENIAKLQALVDASAQRLVELAGQwekhrvpLIEEYRALKEAKSNKedesQRKLEEIKELREKIKEVA 467
|
170
....*....|..
gi 1655220527 1576 RRLKQAEEEKVR 1587
Cdd:pfam05667 468 EEAKQKEELYKQ 479
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4296-4329 |
4.24e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.24e-04
10 20 30
....*....|....*....|....*....|....
gi 1655220527 4296 EESGPVAGILDTDTLEKVSVTEAIHRNLVDNITG 4329
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1660-2074 |
4.42e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1660 LKANEALRLRLRaEEEAQRKSLAQEEAEKQKTEAERDAKKKakaeeaalkQKENAEKELEKQRTF--AEQIAQQKLSAEQ 1737
Cdd:COG4717 70 LKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEA---------ELEELREELEKLEKLlqLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1738 EYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEA 1817
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1818 LKMKQLAEEAARLRSVAEEAKKQRQLAEdEAARQRAEAEKILKEKLAAINEATRLKTEAEVAL-----------KAKEAE 1886
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKE-ARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLvlgllallfllLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1887 NERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKS 1966
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1967 DLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKK-IAAAEEEAARQRKAAQDEVERLKQKAAEA 2045
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeLEEELEELEEELEELEEELEELREELAEL 458
|
410 420
....*....|....*....|....*....
gi 1655220527 2046 NKLKDKAEKELEKQVILAKEAAQKSTAAE 2074
Cdd:COG4717 459 EAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1385-1846 |
4.54e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1385 KKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKlkmkedasqrQGLAVDAEKQKQNIQlELTQLKNLSEQEIRSKNQ 1464
Cdd:PRK10246 425 RQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRN----------AALNEMRQRYKEKTQ-QLADVKTICEQEARIKDL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1465 qleEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKvrKAAQEEAERLRKQVNEETQKKKNAEDELK 1544
Cdd:PRK10246 494 ---EAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALEKEV--KKLGEEGAALRGQLDALTKQLQRDESEAQ 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1545 RKSEAEKEAARQKQKAL----------DELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQlqamSFSEKTT 1614
Cdd:PRK10246 569 SLRQEEQALTQQWQAVCaslnitlqpqDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQ----QIEQRQQ 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1615 KLEESLKKEQGTVLQLQEEAEKLRKQEEEAN--KAREQAEKELETwRLKANEALRLRLRAEEEAQrkslaqEEAEKQKTE 1692
Cdd:PRK10246 645 QLLTALAGYALTLPQEDEEASWLATRQQEAQswQQRQNELTALQN-RIQQLTPLLETLPQSDDLP------HSEETVALD 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1693 AER---DAKKKAKAEEAALKQKENAEKE--LEKQRTFAEQIAQQKLSAEQEYIRLKADfehaEQQRGLLDNELQRLKNEV 1767
Cdd:PRK10246 718 NWRqvhEQCLSLHSQLQTLQQQDVLEAQrlQKAQAQFDTALQASVFDDQQAFLAALLD----EETLTQLEQLKQNLENQR 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1768 NAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEA------LKMKQLAEEAARLRSVAEEAKKQR 1841
Cdd:PRK10246 794 QQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTrqgeirQQLKQDADNRQQQQALMQQIAQAT 873
|
....*
gi 1655220527 1842 QLAED 1846
Cdd:PRK10246 874 QQVED 878
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2457-2567 |
4.57e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.61 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2457 EADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLlkrerdveDEKKKLQKHLEDE 2536
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELI--------EEIQELKEELEQR 483
|
90 100 110
....*....|....*....|....*....|.
gi 1655220527 2537 VNKAKALKDEQQRQQKLMDEEKKKLQAIMDE 2567
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| MAP70 |
pfam07058 |
Microtubule-associated protein 70; This family represents a family of plant ... |
2339-2622 |
4.75e-04 |
|
Microtubule-associated protein 70; This family represents a family of plant microtubule-associated proteins of size 70 kDa. The proteins contain four predicted coiled-coil domains, and truncation studies identify a central domain that targets the proteins to microtubules. It has no predicted trans-membrane domains, and the region between the coils from approximately residues 240-483 is the targetting region.
Pssm-ID: 399798 [Multi-domain] Cd Length: 544 Bit Score: 46.35 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2339 KLKAEAEEL---QKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEIsaeaEKLKLRVKELSSAQAKAE 2415
Cdd:pfam07058 15 EVRDKDRELgeaLAEIKALRLSERLKEKAVEELTDELLKLDEKLKASENLLESKNLEI----KKINDEKKAALAAQFAAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2416 EEATRFKK-QADEAKVRLQETE-KQTTETVVQKLETQRLQSTREADD---LKKAIAELEKEREK--LKRDAQ---ELQNK 2485
Cdd:pfam07058 91 ATLRRVHAaQKDEDMPPIEAILaPLEAELKLARQEINKLQDDNKALDrltKSKEAALLEAERAVqiALAKASlvdDLQNK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2486 S----KETASAQQEQMEQQKAMLQQTFLTEKELLLKRErdvedekkkLQKHLEDEVNKAKALKDEQqRQQKLMDEEKKKL 2561
Cdd:pfam07058 171 NqelmKQIEICQEENKILDKAHRQKVAEVEKLSQTVRE---------LEEAVLAGGAAANAVRDYQ-RKVKEMNEERRTL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 2562 QAIMDEAVKKQKEAEAEMKNKQKE-----MEalEKKRLEQEKLLADENKKLREKLESLEVTSKQAA 2622
Cdd:pfam07058 241 ERELARAKVVANRVATVVANEWKDandkvMP--VKQWLEERRFLQGEMQQLRDKLAISERTAKAEA 304
|
|
| I-BAR_IMD |
cd07605 |
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ... |
2493-2636 |
4.77e-04 |
|
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.
Pssm-ID: 153289 [Multi-domain] Cd Length: 223 Bit Score: 45.05 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2493 QQEQMEQQKAMLQQTFLteKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQR-QQKLMDEEKKKLQAIMDEAVKK 2571
Cdd:cd07605 76 THKSIEASLEQVAKAFH--GELILPLEKKLELDQKVINKFEKDYKKEYKQKREDLDKaRSELKKLQKKSQKSGTGKYQEK 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 2572 QKEAEAEMKNKQKEMEALEKkrLEQEKLLADENKKLREKLESL-EVTSKQAASKTKEIEVQTDKVP 2636
Cdd:cd07605 154 LDQALEELNDKQKELEAFVS--QGLRDALLEERRRYCFLVDKHcSVAKHEIAYHAKAMTLLSTRLP 217
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2325-2612 |
4.91e-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: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2325 KMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQgfqkslEAERKRQLEISAEAEKLKLRV 2404
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEE------EKEEERKEERKRYRQELEEQI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2405 KELSSAQAKAEEEATRFKKQADEAKVRLQETEKQttetvvqKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQN 2484
Cdd:pfam13868 83 EEREQKRQEEYEEKLQEREQMDEIVERIQEEDQA-------EAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2485 KSKETASAQQEQMEQQKAMLQQTFLTEKELL------LKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEK 2558
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKEREIarlraqQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQ 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2559 KKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLE 2612
Cdd:pfam13868 236 ELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL 289
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2173-2521 |
5.06e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.43 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2173 KQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEE------LQRVKAQVNDAVKQKAQVENELS 2246
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDdhnrasMQRDEAIAAIDNEQQTNSKDGEQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2247 KVKMQMDELLKLKVRIEEENLRLMQ-------------KNKDNTQK-------LLAEEAEKMKSLAEEAARLSVEAEETA 2306
Cdd:PLN02939 125 LSDFQLEDLVGMIQNAEKNILLLNQarlqaledlekilTEKEALQGkinilemRLSETDARIKLAAQEKIHVEILEEQLE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2307 RQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLedkqeiqqRLDKETQGFQKSLeae 2386
Cdd:PLN02939 205 KLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVF--------KLEKERSLLDASL--- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2387 rkRQLE---ISAEAEKLKLRVKELSSAQAKAEEEAT---RFKKQADEAKVRLQetEKQTTETVVQKLEtqrlQSTREADD 2460
Cdd:PLN02939 274 --RELEskfIVAQEDVSKLSPLQYDCWWEKVENLQDlldRATNQVEKAALVLD--QNQDLRDKVDKLE----ASLKEANV 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 2461 LKKAIAELEKEREKLKRDAQELQNKSKETASaQQEQMEQQKAMLQQTFLTEKELLLKRERD 2521
Cdd:PLN02939 346 SKFSSYKVELLQQKLKLLEERLQASDHEIHS-YIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1493-1932 |
5.38e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.33 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1493 QKSTADDELQKLRDQAAeaeKVRKAAQEEAERLRKQVNEETqkkknaeDELKRKSEAEKEAARQKQ--KALDELQKHKMQ 1570
Cdd:PRK10246 192 QHKSARTELEKLQAQAS---GVALLTPEQVQSLTASLQVLT-------DEEKQLLTAQQQQQQSLNwlTRLDELQQEASR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1571 AEEAERRLKQAEEEKVRQIKVVEeVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAE---KLRKQEEEANKA 1647
Cdd:PRK10246 262 RQQALQQALAAEEKAQPQLAALS-LAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMAlraRIRHHAAKQSAE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1648 REQAEKELETWrLKANEALRL-------------RLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENA 1714
Cdd:PRK10246 341 LQAQQQSLNTW-LAEHDRFRQwnnelagwraqfsQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQHA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1715 EKELEKQR--TFAEQIA--QQKLS--------AEQEYIRLKADFEHAEQQRGLLDNELQRLKNeVNAAEKQRRQLEDELA 1782
Cdd:PRK10246 420 EQRPLRQRlvALHGQIVpqQKRLAqlqvaiqnVTQEQTQRNAALNEMRQRYKEKTQQLADVKT-ICEQEARIKDLEAQRA 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1783 KVRS----------EMDALLQMkiQAEKVSQSNTEKSKqlLETEalkMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQR 1852
Cdd:PRK10246 499 QLQAgqpcplcgstSHPAVEAY--QALEPGVNQSRLDA--LEKE---VKKLGEEGAALRGQLDALTKQLQRDESEAQSLR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1853 AEaEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAeDEAYQRKLLEDQAAQHKHDI---QEKITQLQSSSVSE 1929
Cdd:PRK10246 572 QE-EQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQL-RLLSQRHELQGQIAAHNQQIiqyQQQIEQRQQQLLTA 649
|
...
gi 1655220527 1930 LDR 1932
Cdd:PRK10246 650 LAG 652
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1387-1560 |
5.58e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1387 RMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQglavDAEKQKQNIQLELTQLknlsEQEIRSKNQQL 1466
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE----DLEKEIKRLELEIEEV----EARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1467 EEAQVSRrkleeEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKrK 1546
Cdd:COG1579 83 GNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE-A 156
|
170
....*....|....
gi 1655220527 1547 SEAEKEAARQKQKA 1560
Cdd:COG1579 157 ELEELEAEREELAA 170
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2288-2629 |
5.70e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.84 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2288 MKSLAEEAARLsveaeETARQRKTAEAELAEqRALAEKMLK--EKMQAIQEATKLKAEAEELQ------KQKNQAQEKAK 2359
Cdd:pfam05622 68 LEQLQEENFRL-----ETARDDYRIKCEELE-KEVLELQHRneELTSLAEEAQALKDEMDILRessdkvKKLEATVETYK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2360 KLLED----KQEIQQRLDKETQGFQK--SLEAERKRQLEISAEAEKLKLRVKELssaQAKAEEEATRFKKQADEAKvRLQ 2433
Cdd:pfam05622 142 KKLEDlgdlRRQVKLLEERNAEYMQRtlQLEEELKKANALRGQLETYKRQVQEL---HGKLSEESKKADKLEFEYK-KLE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2434 ETEKqttetVVQKlETQRLQSTReaDDLKKAIAELE----KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFL 2509
Cdd:pfam05622 218 EKLE-----ALQK-EKERLIIER--DTLRETNEELRcaqlQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQH 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2510 TEKELLLKRERDVEDEKKKLQKHLEDevnkAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMK---NKQKEM 2586
Cdd:pfam05622 290 ENKMLRLGQEGSYRERLTELQQLLED----ANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEdssLLKQKL 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1655220527 2587 EALEKKRLEqeklLADENKKLREKLESLEVT-SKQAASKTKEIE 2629
Cdd:pfam05622 366 EEHLEKLHE----AQSELQKKKEQIEELEPKqDSNLAQKIDELQ 405
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2231-2526 |
5.85e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.90 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2231 VNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRK 2310
Cdd:pfam09731 109 TKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2311 TAEAELAEQRALAEKmlkekmqaIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQ 2390
Cdd:pfam09731 189 EALAEKLKEVINLAK--------QSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQ 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2391 LE--------ISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTRE----- 2457
Cdd:pfam09731 261 QElvsifpdiIPVLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARleevr 340
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2458 ADDLKKAIAELEKEREKLKRDAQ-----ELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEK 2526
Cdd:pfam09731 341 AADEAQLRLEFEREREEIRESYEeklrtELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLK 414
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1684-1981 |
6.07e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1684 EEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRL 1763
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1764 KNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEE-AKKQRQ 1842
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQlESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1843 LAEDEAARQR---AEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKI 1919
Cdd:COG4372 166 LAALEQELQAlseAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 1920 TQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADE 1981
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1636-1891 |
6.32e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1636 KLRKQEEEANKAREQAEKEletwrlkanealrlrlrAEEEAQRKSL-AQEEAEKQKTEAERDAKkkakaeeaalkQKENA 1714
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKE-----------------AEAIKKEALLeAKEEIHKLRNEFEKELR-----------ERRNE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1715 EKELEKqrtfaeqiaqqklsaeqeyiRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEdelaKVRSEMDALLQM 1794
Cdd:PRK12704 84 LQKLEK--------------------RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE----KKEEELEELIEE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1795 KIQA-EKVSQSNTEKSKQLLetealkMKQLAEEAarlrsvAEEAKKQRQLAEDEAarqRAEAEKILKEKLA-AIneaTRL 1872
Cdd:PRK12704 140 QLQElERISGLTAEEAKEIL------LEKVEEEA------RHEAAVLIKEIEEEA---KEEADKKAKEILAqAI---QRC 201
|
250 260
....*....|....*....|.
gi 1655220527 1873 KTE--AEVALKAKEAENERLK 1891
Cdd:PRK12704 202 AADhvAETTVSVVNLPNDEMK 222
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1378-1645 |
6.52e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 46.00 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1378 EKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLeltqLKNLSEQ 1457
Cdd:PLN03229 514 EKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKEKMEA----LKAEVAS 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1458 EIRSKNQQLEEA---QVSRRKLEEEIHLIRIQlqttikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQ 1534
Cdd:PLN03229 590 SGASSGDELDDDlkeKVEKMKKEIELELAGVL------KSMGLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINKKIE 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1535 KKKNAEDeLKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKvveevaQKTAATQLQAMSFSEKTT 1614
Cdd:PLN03229 664 RVIRSSD-LKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELK------EKFEELEAELAAARETAA 736
|
250 260 270
....*....|....*....|....*....|.
gi 1655220527 1615 KLEESLKKEqgtvlQLQEEAEKLRKQEEEAN 1645
Cdd:PLN03229 737 ESNGSLKND-----DDKEEDSKEDGSRVEVN 762
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2125-2390 |
6.89e-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: 46.37 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2125 KAEEAEKLKKAAEDEAAKQA---KAQKDAERlrkeaeaeaakraaaeaAALKQ-KQEADAEMAKHKKEAE----QALKQK 2196
Cdd:NF012221 1541 SQQADAVSKHAKQDDAAQNAladKERAEADR-----------------QRLEQeKQQQLAAISGSQSQLEstdqNALETN 1603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2197 SQVEKELglVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENE-----LSKVKMQMDELlKLKVRIEEENLRlmQ 2271
Cdd:NF012221 1604 GQAQRDA--ILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPfagglLDRVQEQLDDA-KKISGKQLADAK--Q 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2272 KNKDNTQKLlAEEAEKMKSLAEEAARLSVEAEETARQRKTaEAELAEQRALAEKmlkekmqaiQEATKLKAEAEELQKQK 2351
Cdd:NF012221 1679 RHVDNQQKV-KDAVAKSEAGVAQGEQNQANAEQDIDDAKA-DAEKRKDDALAKQ---------NEAQQAESDANAAANDA 1747
|
250 260 270
....*....|....*....|....*....|....*....
gi 1655220527 2352 NQAQEKAKKLLEDKQEIQQrldKETQGFQKSLEAERKRQ 2390
Cdd:NF012221 1748 QSRGEQDASAAENKANQAQ---ADAKGAKQDESDKPNRQ 1783
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1726-2141 |
7.11e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.67 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1726 EQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSN 1805
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1806 TEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEA 1885
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1886 ENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEK 1965
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1966 SDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEA 2045
Cdd:COG5278 353 EAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2046 NKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQK 2125
Cdd:COG5278 433 ALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAA 512
|
410
....*....|....*.
gi 1655220527 2126 AEEAEKLKKAAEDEAA 2141
Cdd:COG5278 513 AEAALAAALAAALASA 528
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1365-1689 |
7.34e-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: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1365 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDasqrqglavdaEKQKQNI 1444
Cdd:pfam15558 51 ERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLE-----------RARQEAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1445 QLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIH---LIRIQLQTTIKQKSTAD----DELQKLRDQAAEAEKVRKA 1517
Cdd:pfam15558 120 QRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHkrqLKEREEQKKVQENNLSEllnhQARKVLVDCQAKAEELLRR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1518 AQEEAERLRKQVNEETQKKKNAEdELKRKSEAEKEAARQKQ----KALDELQKHK-MQAEEAERRLKQAEEekvrqikVV 1592
Cdd:pfam15558 200 LSLEQSLQRSQENYEQLVEERHR-ELREKAQKEEEQFQRAKwraeEKEEERQEHKeALAELADRKIQQARQ-------VA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1593 EEVAQKTAATQLQAMSFSEKTTKLEEsLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRA 1672
Cdd:pfam15558 272 HKTVQDKAQRARELNLEREKNHHILK-LKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEARKTARASFHMREKV 350
|
330
....*....|....*..
gi 1655220527 1673 EEEAQRKSLAQEEAEKQ 1689
Cdd:pfam15558 351 REETNNRTFDKMALEAQ 367
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2411-2631 |
7.53e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.22 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2411 QAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQrlqstreaddlkkaIAELEKEREKLKRDAQELQNKSKETA 2490
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQR--------------AAEQARQKELEQRAAAEKAAKQAEQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2491 SAQQEqmEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQ----KLMDEEKKKlqaimD 2566
Cdd:TIGR02794 111 AKQAE--EKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEeakkKAEAEAKAK-----A 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220527 2567 EAVKKQKEAEAEMKNKQ--KEMEALEKKRLEQEKLLADENKKLReKLESLEVTSKQAASKTKEIEVQ 2631
Cdd:TIGR02794 184 EAEAKAKAEEAKAKAEAakAKAAAEAAAKAEAEAAAAAAAEAER-KADEAELGDIFGLASGSNAEKQ 249
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2270-2502 |
7.62e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 45.36 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2270 MQKNKDnTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEAtklKAEAEELQK 2349
Cdd:PRK07735 1 MDPEKD-LEDLKKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAA---KAKAAALAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2350 QKNQAQEKAKKllEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEeatrFKKQADEAK 2429
Cdd:PRK07735 77 QKREGTEEVTE--EEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAA----LAKQKREGT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 2430 VRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKA 2502
Cdd:PRK07735 151 EEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKA 223
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1270-1585 |
8.04e-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: 45.66 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1270 LKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDY---------EFQILAYRALQDPIASPLKKPKMESASDNIIQ 1340
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelesrvaELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1341 EYVTL-------RTRYSEL----STLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRmaeiqAQLETQKQLAEGHAKSV 1409
Cdd:pfam07888 116 EKDALlaqraahEARIRELeediKTLTQRVLERETELERMKERAKKAGAQRKEEEAER-----KQLQAKLQQTEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1410 AKaelEAQELKLKMKEDASQRQGLAVDAEKQKQNI------QLELTQLK----------NLSEQEIRSKNQQLEEAQVSR 1473
Cdd:pfam07888 191 SK---EFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkEAENEALLeelrslqerlNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1474 RKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQ-AAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKE 1552
Cdd:pfam07888 268 DRTQAELHQARLQAAQLTLQLADASLALREGRARwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
330 340 350
....*....|....*....|....*....|...
gi 1655220527 1553 AARQKQKALDELQKHKMQAEEAERRLKQAEEEK 1585
Cdd:pfam07888 348 LGREKDCNRVQLSESRRELQELKASLRVAQKEK 380
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1629-1948 |
8.15e-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: 44.91 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1629 QLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAAL 1708
Cdd:pfam13868 37 EEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1709 KQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKV---- 1784
Cdd:pfam13868 117 EAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQqeka 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1785 ---RSEMDALLQMKIQAEkvsqsNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQlaEDEAARQRAEAEKILKE 1861
Cdd:pfam13868 197 qdeKAERDELRAKLYQEE-----QERKERQKEREEAEKKARQRQELQQAREEQIELKERRL--AEEAEREEEEFERMLRK 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1862 KlaaineatrlkteAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEEtl 1941
Cdd:pfam13868 270 Q-------------AEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEE-- 334
|
....*..
gi 1655220527 1942 RQKKVVE 1948
Cdd:pfam13868 335 RQKKLKE 341
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
8-143 |
8.68e-04 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 45.70 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 8 PGQRLPEEQHYVQAYENvrekykDERDRVQKKTFTKWVNKHLMKAQrhITDLYEDLRDGhnlISLLEVLSGETLPRERDL 87
Cdd:COG5069 357 PGQEPLEEEEKPEIEEF------DAEGEFEARVFTFWLNSLDVSPE--ITNLFGDLRDQ---LILLQALSKKLMPMTVTH 425
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220527 88 VR-NVRLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNpKLTLGLIW 143
Cdd:COG5069 426 KLvKKQPASGIEENRFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVW 481
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1497-1648 |
8.80e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 45.80 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1497 ADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKhKMQAEEAER 1576
Cdd:PRK10811 625 DNRTRREGRENREENRRNRRQAQQQTAETRESQQAEVTEKARTQDEQQQAPRRERQRRRNDEKRQAQQEA-KALNVEEQS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1577 RLKQAEEEKVRQI-----------KV-VEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEA 1644
Cdd:PRK10811 704 VQETEQEERVQQVqprrkqrqlnqKVrIEQSVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEEN 783
|
....
gi 1655220527 1645 NKAR 1648
Cdd:PRK10811 784 NAEN 787
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2292-2555 |
8.84e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2292 AEEAARLSVEAE-----ETARQRKTAEAElaeqRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKakkLLEDKQ 2366
Cdd:PRK11281 29 AASNGDLPTEADvqaqlDALNKQKLLEAE----DKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAK---LRQAQA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2367 EIQQRLDKETQGFQKSLEAERKRQLEisaeaEKLKLRVKELSSAQAKAEEEAT----------RFKKQADEAKVRLQETE 2436
Cdd:PRK11281 102 ELEALKDDNDEETRETLSTLSLRQLE-----SRLAQTLDQLQNAQNDLAEYNSqlvslqtqpeRAQAALYANSQRLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2437 KQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDA--QELQNKSKETASAQQEQMEQQKAMLQQtfltekel 2514
Cdd:PRK11281 177 NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTqlQDLLQKQRDYLTARIQRLEHQLQLLQE-------- 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1655220527 2515 LLKRERDVEDEKKKLQKHLEDEVNKAKA---LKDEQQRQQKLMD 2555
Cdd:PRK11281 249 AINSKRLTLSEKTVQEAQSQDEAARIQAnplVAQELEINLQLSQ 292
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1505-1693 |
8.87e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1505 RDQAAEAEKVRKAAQEEAErlrkqvnEETQKKKNAEDELKRKSEAEKEAARQKQKALD-------ELQKHKMQAEEAERR 1577
Cdd:PRK05035 464 REKAAREARHKKAAEARAA-------KDKDAVAAALARVKAKKAAATQPIVIKAGARPdnsaviaAREARKAQARARQAE 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1578 LKQAEEEKVRQIKVVEEVAQKTAATQLQAmsfsEKTTKLEESLKKEQGTVLQLQEEAeKLRKQEEEANKAREQAEKELET 1657
Cdd:PRK05035 537 KQAAAAADPKKAAVAAAIARAKAKKAAQQ----AANAEAEEEVDPKKAAVAAAIARA-KAKKAAQQAASAEPEEQVAEVD 611
|
170 180 190
....*....|....*....|....*....|....*.
gi 1655220527 1658 WRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEA 1693
Cdd:PRK05035 612 PKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA 647
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1486-1769 |
9.48e-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: 45.60 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1486 QLQTTIKQKSTADDELQKLRDQA-AEAEKvRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKAL-DE 1563
Cdd:NF012221 1543 QADAVSKHAKQDDAAQNALADKErAEADR-QRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEESRAVtKE 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1564 LQKhKMQAEEAERRLKQAEEEKVRQ---------IKVVEEV---AQKTAATQLQAMS--FSEKTTKLEESLKKEQGTVLQ 1629
Cdd:NF012221 1622 LTT-LAQGLDALDSQATYAGESGDQwrnpfagglLDRVQEQlddAKKISGKQLADAKqrHVDNQQKVKDAVAKSEAGVAQ 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1630 lqeeAEKLRKQEEEA-NKAREQAEKeletwrlKANEALRLRLRAEEEAQRKSLAQEEAEKQ-KTEAERDAKKKAKAEEAA 1707
Cdd:NF012221 1701 ----GEQNQANAEQDiDDAKADAEK-------RKDDALAKQNEAQQAESDANAAANDAQSRgEQDASAAENKANQAQADA 1769
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 1708 LKQKENAEKELEKQRTFAEQIAQQKLSAE---QEYIRLKADFEHAEQQR---GLLDNELQRLKNEVNA 1769
Cdd:NF012221 1770 KGAKQDESDKPNRQGAAGSGLSGKAYSVEgvaEPGSHINPDSPAAADGRfseGLTEQEQEALEGATNA 1837
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2377-2638 |
9.74e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.80 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2377 QGFQKSLEAERKRQLEISAEAEKL----KLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ-----TTETVVQKL 2447
Cdd:pfam15905 27 QRFRKQKAAESQPNLNNSKDASTPatarKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQdkrlqALEEELEKV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2448 ETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAM-LQQTFLTEKELLLKRERDVEDEK 2526
Cdd:pfam15905 107 EAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSSLSMELMkLRNKLEAKMKEVMAKQEGMEGKL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2527 KKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEaEMKNKQKEMEALEKKRLEQEKLLADENKK 2606
Cdd:pfam15905 187 QVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSE-QVEKYKLDIAQLEELLKEKNDEIESLKQS 265
|
250 260 270
....*....|....*....|....*....|..
gi 1655220527 2607 LREKLESLEVTSKQAASKTKEIEVQTDKVPEE 2638
Cdd:pfam15905 266 LEEKEQELSKQIKDLNEKCKLLESEKEELLRE 297
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1360-1589 |
9.87e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1360 IKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEghaksVAKAELEAQELklkmkedasqRQGLAvDAEK 1439
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-----YSWDEIDVASA----------EREIA-ELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1440 QKQNIQLELTQLKNLSEQ------EIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEA-- 1511
Cdd:COG4913 676 ELERLDASSDDLAALEEQleeleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErf 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1512 --EKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRK--------------SEAEKEAARQKQKALDELQKHKM--QAEE 1573
Cdd:COG4913 756 aaALGDAVERELRENLEERIDALRARLNRAEEELERAmrafnrewpaetadLDADLESLPEYLALLDRLEEDGLpeYEER 835
|
250
....*....|....*.
gi 1655220527 1574 AERRLKQAEEEKVRQI 1589
Cdd:COG4913 836 FKELLNENSIEFVADL 851
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2463-2639 |
1.01e-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: 44.75 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2463 KAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELllkreRDVEDEKKKLQKHLedevnkaKA 2542
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----RALEQELAALEAEL-------AE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2543 LKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKkRLEQEKLLADENKK----LREKLESLEVTS 2618
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREqaeeLRADLAELAALR 166
|
170 180
....*....|....*....|.
gi 1655220527 2619 KQAASKTKEIEVQTDKVPEEQ 2639
Cdd:COG4942 167 AELEAERAELEALLAELEEER 187
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2380-2713 |
1.02e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2380 QKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRL--QSTRE 2457
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEleSLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2458 ADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEV 2537
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2538 NKAKalKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVT 2617
Cdd:COG4372 190 KEAN--RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2618 SKQAASKTKEIEVQTDKVPEEQLVSMTTVETTKKVFNGSVEAVKKDGASPLAFEGIRESVPAERLLEIGVLTKKDVDKLK 2697
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
330
....*....|....*.
gi 1655220527 2698 KGKVSAQDLSKADKVK 2713
Cdd:COG4372 348 VGLLDNDVLELLSKGA 363
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2180-2437 |
1.07e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.39 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2180 AEMAKHKKEAEQalKQKSQVEKEL--------GLVKLQLDETDKQKALMDEELQRVKAQV---NDAVKQ-KAQVENE--- 2244
Cdd:NF033838 142 AEATKKVEEAEK--KAKDQKEEDRrnyptntyKTLELEIAESDVEVKKAELELVKEEAKEprdEEKIKQaKAKVESKkae 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2245 ---LSKVKMQMDELL-KLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQR 2320
Cdd:NF033838 220 atrLEKIKTDREKAEeEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGEETLPSPS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2321 ALAEKMLKEKMQAIQEATKlKAEAEELQKQKNQAQEKAKKL-LE------DKQEIQQRLDKETQgfQKSLEAERKRQLEI 2393
Cdd:NF033838 300 LKPEKKVAEAEKKVEEAKK-KAKDQKEEDRRNYPTNTYKTLeLEiaesdvKVKEAELELVKEEA--KEPRNEEKIKQAKA 376
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1655220527 2394 SAEAEKLK-LRVKELSSAQAKAEEEATRfkKQADEAKVRLQETEK 2437
Cdd:NF033838 377 KVESKKAEaTRLEKIKTDRKKAEEEAKR--KAAEEDKVKEKPAEQ 419
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1621-1784 |
1.09e-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: 44.84 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1621 KKEQGTVLQLQEEAEKL---RKQEEE----------ANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLA----- 1682
Cdd:TIGR02794 64 KKEQERQKKLEQQAEEAekqRAAEQArqkeleqraaAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAeaerk 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1683 -QEEAEKQKtEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRglldnelq 1761
Cdd:TIGR02794 144 aKEEAAKQA-EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAE-------- 214
|
170 180
....*....|....*....|...
gi 1655220527 1762 RLKNEVNAAEKQRRQLEDELAKV 1784
Cdd:TIGR02794 215 AEAAAAAAAEAERKADEAELGDI 237
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1512-1669 |
1.10e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1512 EKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQkaldELQKHKMQAEEAERRLKQAEEEKVRQIkv 1591
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKE----ELEEKKEKLQEEEDKLLEEAEKEAQQA-- 578
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 1592 VEEvAQKTAATQLQAMSFSEkttKLEESLKKEQgtvlQLQEEAEKLRKQEEEANKAreQAEKELETWRLKANEALRLR 1669
Cdd:PRK00409 579 IKE-AKKEADEIIKELRQLQ---KGGYASVKAH----ELIEARKRLNKANEKKEKK--KKKQKEKQEELKVGDEVKYL 646
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1516-1910 |
1.16e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.02 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1516 KAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAarqKQKALDELQKHKMQAEEAERRLKQAEEEKvRQIKVVEEV 1595
Cdd:pfam05701 27 KAHRIQTVERRKLVELELEKVQEEIPEYKKQSEAAEAA---KAQVLEELESTKRLIEELKLNLERAQTEE-AQAKQDSEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1596 AQktaaTQLQAMsfsekttklEESLKKEQGTVLQLQEEAEKLRKQE--EEANKAREqaekELETWRLKANEALRLRLRAE 1673
Cdd:pfam05701 103 AK----LRVEEM---------EQGIADEASVAAKAQLEVAKARHAAavAELKSVKE----ELESLRKEYASLVSERDIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1674 EEAQRKSLAQEEAEKQKTEAerdakkkakaeeaalKQKENAEKE-LEKQRTFAEQIAQQKLSA----EQEYIRLKADFEH 1748
Cdd:pfam05701 166 KRAEEAVSASKEIEKTVEEL---------------TIELIATKEsLESAHAAHLEAEEHRIGAalarEQDKLNWEKELKQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1749 AEQqrglldnELQRLKNEVNAAEKQRRQLE---DELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLL-ETEALKMKQLA 1824
Cdd:pfam05701 231 AEE-------ELQRLNQQLLSAKDLKSKLEtasALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIqAALASAKKELE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1825 E----------EAARLRSVAE--EAKKQRQLAEDEAARQRAEAEKILKEKLAAinEATRLKTEAEVALKAKEAENERLKR 1892
Cdd:pfam05701 304 EvkaniekakdEVNCLRVAAAslRSELEKEKAELASLRQREGMASIAVSSLEA--ELNRTKSEIALVQAKEKEAREKMVE 381
|
410 420
....*....|....*....|....
gi 1655220527 1893 ------QAEDEAYQRKLLEdQAAQ 1910
Cdd:pfam05701 382 lpkqlqQAAQEAEEAKSLA-QAAR 404
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
184-265 |
1.18e-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: 41.52 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 184 RCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQ-AFSVAE--RELGVTRLLDPEdvDVAHPDEKSIITYV 260
Cdd:cd21218 32 RVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKrAEKVLQaaEKLGCKYFLTPE--DIVSGNPRLNLAFV 109
|
....*
gi 1655220527 261 SSLYD 265
Cdd:cd21218 110 ATLFN 114
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2026-2204 |
1.23e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.86 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2026 RQRKAAQDEVERLKQKA-AEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKL 2104
Cdd:COG2268 199 RDARIAEAEAERETEIAiAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAERE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2105 AQAAETAKEKAEKEaallrqKAEEAEKLKKAAEDEAAKQAKAQKDAERlrkeaeaeaakraaaeaAALKQKQEADAEMAK 2184
Cdd:COG2268 279 VQRQLEIAEREREI------ELQEKEAEREEAELEADVRKPAEAEKQA-----------------AEAEAEAEAEAIRAK 335
|
170 180
....*....|....*....|
gi 1655220527 2185 HKKEAEqALKQKSQVEKELG 2204
Cdd:COG2268 336 GLAEAE-GKRALAEAWNKLG 354
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2261-2445 |
1.23e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.94 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2261 RIEEENLRLMQKNKDNTQKLLAEEAEKMKslaEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKL 2340
Cdd:pfam15709 347 RLEVERKRREQEEQRRLQQEQLERAEKMR---EELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2341 KAEA---EELQKQKNQAQEKAKKLLEDKqeiQQRLDKETQgfqksLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEE 2417
Cdd:pfam15709 424 QQEEfrrKLQELQRKKQQEEAERAEAEK---QRQKELEMQ-----LAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAE 495
|
170 180
....*....|....*....|....*...
gi 1655220527 2418 ATRfKKQADEAKVRLQETEKQTTETVVQ 2445
Cdd:pfam15709 496 ERR-QKEEEAARLALEEAMKQAQEQARQ 522
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
23-146 |
1.31e-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: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 23 ENVREKYKDErdrvQKKTFTKWVN---------KHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrERDLVRnvrl 93
Cdd:cd21292 15 EGTTHSYSEE----EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTID-ERAINK---- 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 94 preKGRMRFHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 146
Cdd:cd21292 86 ---KKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1278-1868 |
1.33e-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: 45.43 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1278 KKLLEEIEKNKDQIENCQKDAKAYIDSLKDyefQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTS 1357
Cdd:TIGR01612 1121 KNLDQKIDHHIKALEEIKKKSENYIDEIKA---QINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLN 1197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1358 QyIKFILETQRRLEDDEKASEKLKEDEKKRMAEiqaQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQrQGLAVDA 1437
Cdd:TIGR01612 1198 E-IAEIEKDKTSLEEVKGINLSYGKNLGKLFLE---KIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENE-MGIEMDI 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1438 EKQKQNIQLE---------LTQLKNLSEQEIRSKNQQLEEAQVSrrklEEEIHLIRIQLQTTIKQKSTADDELQKLRDQA 1508
Cdd:TIGR01612 1273 KAEMETFNIShdddkdhhiISKKHDENISDIREKSLKIIEDFSE----ESDINDIKKELQKNLLDAQKHNSDINLYLNEI 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1509 AEAEKVRK--AAQEEAERLRKQVNEETQKKKNAEDELkrkSEAEKEAARQKQKALDELQKHKMQA-------EEAERRLK 1579
Cdd:TIGR01612 1349 ANIYNILKlnKIKKIIDEVKEYTKEIEENNKNIKDEL---DKSEKLIKKIKDDINLEECKSKIEStlddkdiDECIKKIK 1425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1580 Q------AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGT------VLQLQEEAEKLRKQEEEANKA 1647
Cdd:TIGR01612 1426 ElknhilSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATndhdfnINELKEHIDKSKGCKDEADKN 1505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1648 REQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQkteaerdakkkakaeeaalkQKENAEKELEKQRTFAEQ 1727
Cdd:TIGR01612 1506 AKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSE--------------------IIIKEIKDAHKKFILEAE 1565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1728 IAQQKLSA-EQEYIRLKADF-EHAEQQRGLLDNE--LQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQ 1803
Cdd:TIGR01612 1566 KSEQKIKEiKKEKFRIEDDAaKNDKSNKAAIDIQlsLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTEL 1645
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 1804 SNTEKSKQLLET--EALK---------MKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINE 1868
Cdd:TIGR01612 1646 KENGDNLNSLQEflESLKdqkkniedkKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIKE 1721
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1378-1693 |
1.38e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.59 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1378 EKLKEDEKKRMAEiQAQLETQKQLAEGHAKSVAKAELEAQElklkmKEDASQRQGlAVDAEKQKQniqleltqlknlseq 1457
Cdd:PRK07735 4 EKDLEDLKKEAAR-RAKEEARKRLVAKHGAEISKLEEENRE-----KEKALPKND-DMTIEEAKR--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1458 eiRSKNQQLEEAQVSRRKLEEEIhliriqlqttikqKSTADDELQKLRDQAAEAEKVRKAAqeeaerLRKQVNEETQKKK 1537
Cdd:PRK07735 62 --RAAAAAKAKAAALAKQKREGT-------------EEVTEEEKAKAKAKAAAAAKAKAAA------LAKQKREGTEEVT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1538 naEDELKRKSEAEKEAARQKQKALDElqkhkmQAEEAERRLKQAEEEKvrqikvVEEVAQKTAATQLQAMSFSEKTTKLE 1617
Cdd:PRK07735 121 --EEEKAAAKAKAAAAAKAKAAALAK------QKREGTEEVTEEEEET------DKEKAKAKAAAAAKAKAAALAKQKAA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1618 ESlkkEQGTVLQLQEEAEKLRKQEEEANKAREQA-----------EKELETWRLKANEALRLRLRAEEEAQRKSLAQEEA 1686
Cdd:PRK07735 187 EA---GEGTEEVTEEEKAKAKAKAAAAAKAKAAAlakqkasqgngDSGDEDAKAKAIAAAKAKAAAAARAKTKGAEGKKE 263
|
....*..
gi 1655220527 1687 EKQKTEA 1693
Cdd:PRK07735 264 EEPKQEE 270
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1380-1585 |
1.39e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 43.94 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1380 LKEDEKKRMAEIQ-AQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQE 1458
Cdd:pfam06008 33 SPENAHKIQIEILeKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGEND 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1459 IRSKNQQLEEAQVSRRKLEEEIhliriQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNeetQKKKN 1538
Cdd:pfam06008 113 FALPSSDLSRMLAEAQRMLGEI-----RSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANALR---DSLAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1655220527 1539 AEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEK 1585
Cdd:pfam06008 185 YEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQK 231
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1545-1898 |
1.41e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.85 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1545 RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQ-AEEEKVRQIKvvEEVAQKTAATqLQAMSFSEKTTKLEESLKK- 1622
Cdd:PLN03229 422 KKREAVKTPVRELEGEVEKLKEQILKAKESSSKPSElALNEMIEKLK--KEIDLEYTEA-VIAMGLQERLENLREEFSKa 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1623 ---EQGTVLQLQEEAEKLrKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKK 1699
Cdd:PLN03229 499 nsqDQLMHPVLMEKIEKL-KDEFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIK 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1700 kakaeeaalkqkenaekelEKQRTFAEQIAQQKLSAEQEyirlkadfehaeqqrglLDNELqrlkneVNAAEKQRRQLED 1779
Cdd:PLN03229 578 -------------------EKMEALKAEVASSGASSGDE-----------------LDDDL------KEKVEKMKKEIEL 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1780 ELAKVRSEMDallqmkIQAEKVSQSNTEKSKQLLETE-ALKMKQLAEE----------AARLRSVAEEAKKQRQLA---E 1845
Cdd:PLN03229 616 ELAGVLKSMG------LEVIGVTKKNKDTAEQTPPPNlQEKIESLNEEinkkiervirSSDLKSKIELLKLEVAKAsktP 689
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220527 1846 DEAARQRAEA-EKILKEKLAAINEATRLKT-----EAEVALKAK--EAENERLKRQAEDEA 1898
Cdd:PLN03229 690 DVTEKEKIEAlEQQIKQKIAEALNSSELKEkfeelEAELAAAREtaAESNGSLKNDDDKEE 750
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
2281-2408 |
1.43e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2281 LAEEAEKMKSLAEEAARLSVEAEETARQRKtaEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKK 2360
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEE--EEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1655220527 2361 LLEDKQEIqQRLDKETQGFQKSLEAERKRQLEISAEAEKLK-LRVKELS 2408
Cdd:COG2433 460 EIRKDREI-SRLDREIERLERELEEERERIEELKRKLERLKeLWKLEHS 507
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2281-2394 |
1.44e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.94 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2281 LAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAE---KMLKEKMQAIQEATkLKAEAEELQKQKNQAQEK 2357
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEekqQELEAQLEQLQEKA-AETSQERKQKRKEITDQA 225
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1655220527 2358 AKKLLEDKQE----IQQRL-------DKETQGFQKSLEAERKRQLEIS 2394
Cdd:PRK11448 226 AKRLELSEEEtrilIDQQLrkagweaDSKTLRFSKGARPEKGRNLAIA 273
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1417-1581 |
1.44e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1417 QELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKnlsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKST 1496
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ---EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1497 AD------DELQKLRDQAAEAEKVRKAAQEEAERLR----------KQVNEETQKKKNAE--------------DELKRK 1546
Cdd:PRK00409 603 SVkaheliEARKRLNKANEKKEKKKKKQKEKQEELKvgdevkylslGQKGEVLSIPDDKEaivqagimkmkvplSDLEKI 682
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1655220527 1547 SEAEKEAARQKQKALDELQK-------HKMQAEEAERRLKQA 1581
Cdd:PRK00409 683 QKPKKKKKKKPKTVKPKPRTvsleldlRGMRYEEALERLDKY 724
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2327-2633 |
1.46e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.81 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2327 LKEKMQAI-QEATKLKAEAEELQ---KQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEA-ERK---RQLEISAEAE 2398
Cdd:pfam10174 329 LKESLTAKeQRAAILQTEVDALRlrlEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVkERKinvLQKKIENLQE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2399 KLKLRVKELSSAQAKAEEEATRfKKQADEAKVRLQE--TEKqttETVVQKLETQRLQSTR----EADDLKKAIAELEKER 2472
Cdd:pfam10174 409 QLRDKDKQLAGLKERVKSLQTD-SSNTDTALTTLEEalSEK---ERIIERLKEQREREDRerleELESLKKENKDLKEKV 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2473 EKLKRDAQELQ---NKSKETASAQQEQMEQQKAMLQQTfltEKELLLKRER--DVEDEKKKLQKHLEDE------VNKAK 2541
Cdd:pfam10174 485 SALQPELTEKEsslIDLKEHASSLASSGLKKDSKLKSL---EIAVEQKKEEcsKLENQLKKAHNAEEAVrtnpeiNDRIR 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2542 ALKDEQQRQQklmdEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKllaDENKKLREKLESLEVTSKQA 2621
Cdd:pfam10174 562 LLEQEVARYK----EESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMK---EQNKKVANIKHGQQEMKKKG 634
|
330
....*....|..
gi 1655220527 2622 ASKTKEIEVQTD 2633
Cdd:pfam10174 635 AQLLEEARRRED 646
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
2389-2506 |
1.62e-03 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 44.68 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2389 RQLEISAEAEKLKlrvKELSSAQAKAEEEATRFKKQADEAKVrLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAEL 2468
Cdd:PTZ00186 537 RDSEQHAEADRVK---RELVEVRNNAETQLTTAERQLGEWKY-VSDAEKENVKTLVAELRKAMENPNVAKDDLAAATDKL 612
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1655220527 2469 EKE-----REKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQ 2506
Cdd:PTZ00186 613 QKAvmecgRTEYQQAAAANSGSSSNSGEQQQQQQQQQQQNSEE 655
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
2265-2638 |
1.63e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 44.67 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2265 ENLRLMQKNKDNTQKLLAEEA----EKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQA----IQE 2336
Cdd:pfam15070 4 ESLKQLQTERDQYAENLKEEGavwqQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPpagpSEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2337 ATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQqRLDKETQgfQKSLEAERkrQLEISAEAEKLKLRVkeLSSAQAkaeE 2416
Cdd:pfam15070 84 EQRLQEEAEQLQKELEALAGQLQAQVQDNEQLS-RLNQEQE--QRLLELER--AAERWGEQAEDRKQI--LEDMQS---D 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2417 EAT--RFKKQADEAKVRLQETEKQTTETVVQKLE-TQRLQSTREA-DDLKKAIAELEKEREKLKrdaQELQNKSKEtASA 2492
Cdd:pfam15070 154 RATisRALSQNRELKEQLAELQNGFVKLTNENMElTSALQSEQHVkKELAKKLGQLQEELGELK---ETLELKSQE-AQS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2493 QQEQMEQQKAMLQQ------TFLTEKELLLKRERDVEDEKKKLQ-KHLEDEVNKAKALKDEQQRQQKL--MDEEKKKLQA 2563
Cdd:pfam15070 230 LQEQRDQYLAHLQQyvaayqQLASEKEELHKQYLLQTQLMDRLQhEEVQGKVAAEMARQELQETQERLeaLTQQNQQLQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2564 -----------------IMDEAVKKQKEAEAEMKNKQKEMEA--------LEKKRLEQEKLLADENKKLREKLESLEVTS 2618
Cdd:pfam15070 310 qlsllanpgegdgleseEEEEEAPRPSLSIPEDFESREAMVAffnsalaqAEEERAELRRQLKEQKRRCRRLAQQAAPAQ 389
|
410 420
....*....|....*....|
gi 1655220527 2619 KQAASKTKEIEVQTDKVPEE 2638
Cdd:pfam15070 390 EEPEHEAHAPGTGGDSVPVE 409
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1758-1921 |
1.63e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.48 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1758 NELQRlKNEVNAAEKQRRQledELAKVRSEMDalLQMKIQAEkvSQSNTEKSKQLLETEALKMKQLAEEAARLRSV---- 1833
Cdd:COG2268 206 AEAER-ETEIAIAQANREA---EEAELEQERE--IETARIAE--AEAELAKKKAEERREAETARAEAEAAYEIAEAnaer 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1834 -----AEEAKKQRQ--LAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEV-ALKAK---EAENERLKRQAEdEAYQRK 1902
Cdd:COG2268 278 evqrqLEIAEREREieLQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAeAIRAKglaEAEGKRALAEAW-NKLGDA 356
|
170
....*....|....*....
gi 1655220527 1903 LLEDQAAQHKHDIQEKITQ 1921
Cdd:COG2268 357 AILLMLIEKLPEIAEAAAK 375
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1047-1638 |
1.65e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1047 QKTAEQMKVQSELEGLKKDLNSITEKTEEILASPQqsssapmlrseldvtlkkmdhvyglssvyldKLKTIDIVIRNTKD 1126
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEG-------------------------------SKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1127 AEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQL 1206
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1207 AGSLLERWQAVFAQIDLRQRELSLLGRhMNSYKQsyewliqwlREARLRQEKIEAAPVWDSKAlKEQLTQEkklLEEIEK 1286
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEE-LERLKK---------RLTGLTPEKLEKELEELEKA-KEEIEEE---ISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1287 NKDQIENCQKDAKAYIDSLK---------------DYEFQILA-YRALQDPIASPLKkpKMESASDNIIQEYVTLRTRYS 1350
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKkakgkcpvcgrelteEHRKELLEeYTAELKRIEKELK--EIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1351 ELSTLTSQY--IKFILETQRRLE--DDEKASEKLKEDE--KKRMAEIQAQLETQKQLAEghaksvakaelEAQELKLKMK 1424
Cdd:PRK03918 491 KESELIKLKelAEQLKELEEKLKkyNLEELEKKAEEYEklKEKLIKLKGEIKSLKKELE-----------KLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1425 EDASQRQglavDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKL 1504
Cdd:PRK03918 560 ELEKKLD----ELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1505 RDQAAEAEKVRKaaqeEAERLRKQVNEETQKKKNAE-----DELKRKSEAEKEAARQKQ---KALDELQKHKMQAEEAER 1576
Cdd:PRK03918 636 AETEKRLEELRK----ELEELEKKYSEEEYEELREEylelsRELAGLRAELEELEKRREeikKTLEKLKEELEEREKAKK 711
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 1577 RLKQAEEEKVRQIKVVEEVAQKTAATQLQAMS-FSEKTTKLEESLKKEQGTVLQLQEEAEKLR 1638
Cdd:PRK03918 712 ELEKLEKALERVEELREKVKKYKALLKERALSkVGEIASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1365-1584 |
1.71e-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: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1365 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQL--AEGHAKSVAKAELEAQELKLKMKEDASQRQglAVDAEKQKQ 1442
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAkqAEQAAKQAEEKQKQAEEAKAKQAAEAKAKA--EAEAERKAK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1443 niqlelTQLKNLSEQEirsknQQLEEAQVSRRKLEEeihliriqlqttIKQKSTADDELQKLRDQAAEAEKvrkaAQEEA 1522
Cdd:TIGR02794 146 ------EEAAKQAEEE-----AKAKAAAEAKKKAEE------------AKKKAEAEAKAKAEAEAKAKAEE----AKAKA 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 1523 ERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE 1584
Cdd:TIGR02794 199 EAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2049-2433 |
1.72e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.75 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2049 KDKAEKELEKQVILAKEAAQKSTAAEQKAQdvlSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAallrQKAEE 2128
Cdd:pfam09731 78 ESKEPKEEKKQVKIPRQSGVSSEVAEEEKE---ATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESAT----AVAKE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2129 AEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEK---ELGL 2205
Cdd:pfam09731 151 AKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKlpeHLDN 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2206 VKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKV-----KMQMDELLKLkvrIEEENLRLMQKNKDNTQKL 2280
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVlkednLLSNDDLNSL---IAHAHREIDQLSKKLAELK 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2281 LAEEAEKMKSLAEEAARLSVEAEETARQrktAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAeELQKQKNQAQEKAKK 2360
Cdd:pfam09731 308 KREEKHIERALEKQKEELDKLAEELSAR---LEEVRAADEAQLRLEFEREREEIRESYEEKLRT-ELERQAEAHEEHLKD 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2361 -LLEDKQEIQQRLDKEtqgFQKSLEAERKRQLEisaEAEKLKLRVKELssaqakaeEEATRFKKQADEAKVRLQ 2433
Cdd:pfam09731 384 vLVEQEIELQREFLQD---IKEKVEEERAGRLL---KLNELLANLKGL--------EKATSSHSEVEDENRKAQ 443
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2359-2598 |
1.76e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2359 KKLLEDKQEIQ--QRLDKetqgFQKSLEAERKRQL-----EISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVR 2431
Cdd:PHA02562 153 RKLVEDLLDISvlSEMDK----LNKDKIRELNQQIqtldmKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2432 LQETEKQTTEtvvqkLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSK-----ETASAQQEQMEQQKAMLQ- 2505
Cdd:PHA02562 229 AKTIKAEIEE-----LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekgGVCPTCTQQISEGPDRITk 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2506 -QTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKD--EQQRQQ-KLMDEEKKKLQAIMDEAVKKQKEAEAEMKN 2581
Cdd:PHA02562 304 iKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNkiSTNKQSlITLVDKAKKVKAAIEELQAEFVDNAEELAK 383
|
250
....*....|....*....
gi 1655220527 2582 KQKEMEALEKKR--LEQEK 2598
Cdd:PHA02562 384 LQDELDKIVKTKseLVKEK 402
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1499-1567 |
1.80e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.08 E-value: 1.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 1499 DELQKLRDQA----AEAEKVRKAAQEEAERLRKQVNEETQK-----KKNAEDELKR-KSEAEKEAARQKQKALDELQKH 1567
Cdd:COG0711 41 AEAERAKEEAeaalAEYEEKLAEARAEAAEIIAEARKEAEAiaeeaKAEAEAEAERiIAQAEAEIEQERAKALAELRAE 119
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1593-1774 |
1.82e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1593 EEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwrlKANEALRLRLRA 1672
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE----ERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1673 E--------------------------------EEAQRKSL-----AQEEAEKQKTEAERDAKKKAKAEEAALKQKENAE 1715
Cdd:COG3883 95 LyrsggsvsyldvllgsesfsdfldrlsalskiADADADLLeelkaDKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 1716 KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQR 1774
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1750-2348 |
1.83e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1750 EQQRGLLDN--------ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLEtealkmk 1821
Cdd:PRK02224 183 SDQRGSLDQlkaqieekEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1822 qLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEklaaiNEATRLKTEAEvalkakEAENERLKRQAEDEAYQR 1901
Cdd:PRK02224 256 -LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE-----RDDLLAEAGLD------DADAEAVEARREELEDRD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1902 KLLEDQAAQHKHDIQEKITQLqsssvseldrqkniveETLRqkkvveEEIHIIRINFERASKEKSDLEVELKKLKGIADE 1981
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEA----------------ESLR------EDADDLEERAEELREEAAELESELEEAREAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1982 TQkskakaeeeaeklkKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVI 2061
Cdd:PRK02224 382 RR--------------EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2062 LAkeAAQKSTAAEQKAQD--VLSKNKEDLLSQEKLRDEFENAKklaqaaetakekaeKEAALLRQKAEEAEKLKKaAEDE 2139
Cdd:PRK02224 448 LL--EAGKCPECGQPVEGspHVETIEEDRERVEELEAELEDLE--------------EEVEEVEERLERAEDLVE-AEDR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2140 AAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEqalKQKSQVEKELGLVKlqldETDKQKAL 2219
Cdd:PRK02224 511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA---EAEEEAEEAREEVA----ELNSKLAE 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2220 MDEELQRvkaqvndavkqkaqveneLSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQK--LLAEEAEKMKSLAEEaar 2297
Cdd:PRK02224 584 LKERIES------------------LERIRTLLAAIADAEDEIERLREKREALAELNDERreRLAEKRERKRELEAE--- 642
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 2298 LSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQ-EATKLKAEAEELQ 2348
Cdd:PRK02224 643 FDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQaEIGAVENELEELE 694
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
43-145 |
1.84e-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: 41.13 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 43 KWVNKHLMKAQR---HITDLYEDLRDGHNLISLLEVLSGETLPR--------ERDLVRNVRlprekgrmrfHKLQNVQiA 111
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKelvlevlsEEDLEKRAE----------KVLQAAE-K 85
|
90 100 110
....*....|....*....|....*....|....
gi 1655220527 112 LDFLKHrqvklvnIRNDDIADGNPKLTLGLIWTI 145
Cdd:cd21218 86 LGCKYF-------LTPEDIVSGNPRLNLAFVATL 112
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
2360-2612 |
1.84e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 43.90 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2360 KLLEDKQEIQQRLDKETQgfqksleaeRKRQLEISAEAEKLKLRVKELSSAQAKA--EEEATRFKKQADEAKVRLQETEK 2437
Cdd:pfam15742 6 KLKYQQQEEVQQLRQNLQ---------RLQILCTSAEKELRYERGKNLDLKQHNSllQEENIKIKAELKQAQQKLLDSTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2438 QTT------ETVVQKLETQRLQSTREADDLKkAIAELEKEREKLKRDAQELQNKSKETasaqQEQMEQ-QKAMLQQTFLT 2510
Cdd:pfam15742 77 MCSsltaewKHCQQKIRELELEVLKQAQSIK-SQNSLQEKLAQEKSRVADAEEKILEL----QQKLEHaHKVCLTDTCIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2511 EKELLLKRERDVEDEKKKLQKHLEdevnkakalkdEQQRQQKLMDEEKKKLQaiMDEAVKKQKEAEAEMKNKQ-----KE 2585
Cdd:pfam15742 152 EKKQLEERIKEASENEAKLKQQYQ-----------EEQQKRKLLDQNVNELQ--QQVRSLQDKEAQLEMTNSQqqlriQQ 218
|
250 260
....*....|....*....|....*..
gi 1655220527 2586 MEALEKKrLEQEKLLADENKKLREKLE 2612
Cdd:pfam15742 219 QEAQLKQ-LENEKRKSDEHLKSNQELS 244
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1492-1566 |
1.87e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 41.53 E-value: 1.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 1492 KQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAedelkRKSEAEKEAARQKQKALDELQK 1566
Cdd:PRK07353 54 EAEKLEAQYEQQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQA-----SKEKARREIEQQKQAALAQLEQ 123
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1848-2088 |
1.90e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1848 AARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSv 1927
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1928 SELDRQKNIVEETLRqkkVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKR 2007
Cdd:COG4942 97 AELEAQKEELAELLR---ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2008 REAEEKVKKIAAAEEEAARQRKAAQDEVERL-KQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKE 2086
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
..
gi 1655220527 2087 DL 2088
Cdd:COG4942 254 KL 255
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2122-2290 |
1.92e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2122 LRQKAEEAEKLKKAAEDEAAKQaKAQKDAERlrkeaeaeaakraaaeaaaLKQKQEADAEMAKHKKEAEQALKQKSQVEK 2201
Cdd:PRK00409 539 AEALLKEAEKLKEELEEKKEKL-QEEEDKLL-------------------EEAEKEAQQAIKEAKKEADEIIKELRQLQK 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2202 ELGL-VKLQlDETDKQKALMD-----EELQRVKAQVNDAVK-----------QKAQVeneLSKVK-----MQMDeLLKLK 2259
Cdd:PRK00409 599 GGYAsVKAH-ELIEARKRLNKanekkEKKKKKQKEKQEELKvgdevkylslgQKGEV---LSIPDdkeaiVQAG-IMKMK 673
|
170 180 190
....*....|....*....|....*....|.
gi 1655220527 2260 VRIEEenLRLMQKNKDNTQKLLAEEAEKMKS 2290
Cdd:PRK00409 674 VPLSD--LEKIQKPKKKKKKKPKTVKPKPRT 702
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
16-150 |
2.01e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 41.52 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 16 QHYVQAYENVREKYKDERDrVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerdlVRNVRLPR 95
Cdd:cd21337 1 RHERDAFDTLFDHAPDKLN-VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVP-----LHSFFLTP 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 96 EKGRmrfHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 150
Cdd:cd21337 75 DSFE---QKVLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1280-1584 |
2.08e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 44.54 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1280 LLEEIEKNKDQIEncqkdakAYIDS-----LKDYEFQILAYrALQDPIASPL---KKPKMESASDNIIQEyvtlRTRYSE 1351
Cdd:PLN03188 991 LLEEIQDLRSQLQ-------YYIDSslpsaRKRNSLLKLTY-SCEPSQAPPLntiPESTDESPEKKLEQE----RLRWTE 1058
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1352 LStltSQYIKFILETQRRLEDDEKASEKLKE--DEKKRMAEiqaQLETQKQLA-EGHAKSVAK-AELEAQELKL-----K 1422
Cdd:PLN03188 1059 AE---SKWISLAEELRTELDASRALAEKQKHelDTEKRCAE---ELKEAMQMAmEGHARMLEQyADLEEKHIQLlarhrR 1132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1423 MKE------DASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEirsknqqleeaqvsRRKLEEEIHLIRIQLQTTIKQKST 1496
Cdd:PLN03188 1133 IQEgiddvkKAAARAGVRGAESKFINALAAEISALKVEREKE--------------RRYLRDENKSLQAQLRDTAEAVQA 1198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1497 ADDELQKLRDQ---AAEAEKVRKAAQEEAERLRKQVNeetQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEE 1573
Cdd:PLN03188 1199 AGELLVRLKEAeeaLTVAQKRAMDAEQEAAEAYKQID---KLKRKHENEISTLNQLVAESRLPKEAIRPACNDDCMAKYD 1275
|
330
....*....|.
gi 1655220527 1574 AERRLKQAEEE 1584
Cdd:PLN03188 1276 AGEPLSEGDQQ 1286
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1268-1653 |
2.20e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1268 KALKEQLTQEKKLLEEIEKNKDQIENCQKDakayidslkdyefqILAYRALQDPIASPLKKpKMESASDNiIQEYVTLrt 1347
Cdd:PRK04778 126 EELQELLESEEKNREEVEQLKDLYRELRKS--------------LLANRFSFGPALDELEK-QLENLEEE-FSQFVEL-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1348 ryselsTLTSQYI---KFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLEtqkQLAEGHAKSVAKA--------ELEA 1416
Cdd:PRK04778 188 ------TESGDYVearEILDQLEEELAALEQIMEEIPELLKELQTELPDQLQ---ELKAGYRELVEEGyhldhldiEKEI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1417 QELKLKMKEDASQRQGLAVD-AEKQKQNIQLELTQLKNLSEQEIRSKN----------QQLEEAQVSRRKLEEEIHLIR- 1484
Cdd:PRK04778 259 QDLKEQIDENLALLEELDLDeAEEKNEEIQERIDQLYDILEREVKARKyveknsdtlpDFLEHAKEQNKELKEEIDRVKq 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1485 --------IQLQTTI-KQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVN--EETQKKKNaeDELK--RKSEAEk 1551
Cdd:PRK04778 339 sytlneseLESVRQLeKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEeiEKEQEKLS--EMLQglRKDELE- 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1552 eaARQKqkaLDELQ------KHKMQA--------------EEAERRLKQAEEEkVRQIKV-VEEVAQKTAATQLQAMSFS 1610
Cdd:PRK04778 416 --AREK---LERYRnklheiKRYLEKsnlpglpedylemfFEVSDEIEALAEE-LEEKPInMEAVNRLLEEATEDVETLE 489
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1655220527 1611 EKTTKLEESlkkeqgTVL--QLQEEAEKLRKQEEEANKAREQAEK 1653
Cdd:PRK04778 490 EETEELVEN------ATLteQLIQYANRYRSDNEEVAEALNEAER 528
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2370-2529 |
2.25e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2370 QRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ----TTETVVQ 2445
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvRNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2446 KLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDE 2525
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
....
gi 1655220527 2526 KKKL 2529
Cdd:COG1579 173 PPEL 176
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1727-1898 |
2.25e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1727 QIAQQKLSAEQEYIRlkadFEhAEQQRgLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAllQMKIQAEKVSQSNT 1806
Cdd:PRK05035 440 AIEQEKKKAEEAKAR----FE-ARQAR-LEREKAAREARHKKAAEARAAKDKDAVAAALARVKA--KKAAATQPIVIKAG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1807 EKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQlAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAE 1886
Cdd:PRK05035 512 ARPDNSAVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAK 590
|
170
....*....|..
gi 1655220527 1887 NERLKRQAEDEA 1898
Cdd:PRK05035 591 AKKAAQQAASAE 602
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1422-1679 |
2.26e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1422 KMKEDASQRQGLAVDAEKQKQNIQLELTqlknlsEQEIRSKNQQLEEAQVSRRKLEEEIHliriQLQTTIKQKSTADDEL 1501
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEE------EEEIRRLEEQVERLEAEVEELEAELE----EKDERIERLERELSEA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1502 QKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQ---KALDELQKhkmqaeEAERRL 1578
Cdd:COG2433 454 RSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELvpvKVVEKFTK------EAIRRL 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1579 KQAEEEKVRQIKVVEEV--AQKTAATQL-----QAMSFSEKT-TKLEESLKKEQGTVL-----QLQEEAEKLRKQEEEAN 1645
Cdd:COG2433 528 EEEYGLKEGDVVYLRDAsgAGRSTAELLaeagpRAVIVPGELsEAADEVLFEEGIPVLpaedvTIQEVDDLAVVDEEELE 607
|
250 260 270
....*....|....*....|....*....|....
gi 1655220527 1646 KAREQAEKELETWRLKANEALRLRLRAEEEAQRK 1679
Cdd:COG2433 608 AAIEDWEERAEERRREKKAEMLERLISEYRAERR 641
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1646-1807 |
2.27e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.84 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1646 KAREQAEKELETWR----LKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERdAKKKAKAEEAALKQKENAEKELEKQ 1721
Cdd:pfam05262 185 ALREDNEKGVNFRRdmtdLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADF-AQDNADKQRDEVRQKQQEAKNLPKP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1722 RTFAEQIAQQKLSAEQEYIRLKADFE---HAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmKIQA 1798
Cdd:pfam05262 264 ADTSSPKEDKQVAENQKREIEKAQIEikkNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQ-KTKP 342
|
....*....
gi 1655220527 1799 EKVSQSNTE 1807
Cdd:pfam05262 343 QVEAQPTSL 351
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1501-1696 |
2.37e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1501 LQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQkkknaeDELKRKSEAEKEAARQKQKALDelqkhkmqaeEAERRLKQ 1580
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK------ELLLRERNQQRQEARREREELQ----------REEERLVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1581 AEEEKVRQIkvveevaqktaatqlqamsfsEKTTKLEEslkkeqgtvlQLQEEAEKLRKQEEEANKAREQAEKEL-ETWR 1659
Cdd:PRK12705 89 KEEQLDARA---------------------EKLDNLEN----------QLEEREKALSARELELEELEKQLDNELyRVAG 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1655220527 1660 LKANEALRL---RLRAEEEAQRKSLAQEEAEKQKTEAERD 1696
Cdd:PRK12705 138 LTPEQARKLllkLLDAELEEEKAQRVKKIEEEADLEAERK 177
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1497-1573 |
2.47e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.88 E-value: 2.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220527 1497 ADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNaedelKRKSEAEKEAARQKQKALDELQKHKMQAEE 1573
Cdd:cd06503 42 AEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKE-----EILAEAKEEAERILEQAKAEIEQEKEKALA 113
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3042-3079 |
2.49e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.46 E-value: 2.49e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1655220527 3042 LQGTPSIAGLLNEPTKEKMSFYQAMKKELLSPEAAVNL 3079
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2282-2601 |
2.51e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2282 AEEAEKMKSlAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKL 2361
Cdd:COG3064 1 AQEALEEKA-AEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2362 LE---DKQEIQQRLDKETQgfQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ 2438
Cdd:COG3064 80 AEaekAAAEAEKKAAAEKA--KAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2439 TTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKR 2518
Cdd:COG3064 158 RAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2519 ERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEK 2598
Cdd:COG3064 238 EATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAV 317
|
...
gi 1655220527 2599 LLA 2601
Cdd:COG3064 318 LAA 320
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1364-1590 |
2.69e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 43.67 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1364 LETQRRLEDDEKASE---KLKEDEKKRMAEIQ---------------AQLETQKQlaEGHAKSVAKAELEAQEL---KLK 1422
Cdd:pfam15066 304 FESLQPLEEDMALNEvlqKLKHTNRKQQMQIQdlqcsnlylekkvkeLQMKITKQ--QVFVDIINKLKENVEELiedKYN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1423 MKEDASqrqglavDAEKQKQNIQLELTQLKNLSEQEIRSKNQ-QLEEAQVsrrkleeEIHLIRIQLQ--TTIKQKStadd 1499
Cdd:pfam15066 382 VILEKN-------DINKTLQNLQEILANTQKHLQESRKEKETlQLELKKI-------KVNYVHLQERyiTEMQQKN---- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1500 elqKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRkseaEKEAARQKQKAL-DELQKHKMQAEEAERRL 1578
Cdd:pfam15066 444 ---KSVSQCLEMDKTLSKKEEEVERLQQLKGELEKATTSALDLLKR----EKETREQEFLSLqEEFQKHEKENLEERQKL 516
|
250
....*....|..
gi 1655220527 1579 KQAEEEKVRQIK 1590
Cdd:pfam15066 517 KSRLEKLVAQVK 528
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
2258-2501 |
2.78e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2258 LKVRIEEENLRLMQKNKDNTQKLLA---EEAEKMKSLAEEAARLSVEAEETARQRktAEAELAEqralAEKMLKEKMQAI 2334
Cdd:PRK05771 36 LKEELSNERLRKLRSLLTKLSEALDklrSYLPKLNPLREEKKKVSVKSLEELIKD--VEEELEK----IEKEIKELEEEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2335 QEatkLKAEAEELQKQKNQAqEKAKKLledkqeiqqrldketqgfqkSLEAERKRQLE--------ISAEAEKLKLRVKE 2406
Cdd:PRK05771 110 SE---LENEIKELEQEIERL-EPWGNF--------------------DLDLSLLLGFKyvsvfvgtVPEDKLEELKLESD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2407 LSSAQAKAEEEATRF------KKQADEAKVRLQETEkqttetvVQKLETQRLQSTREA-DDLKKAIAELEKEREKLKRDA 2479
Cdd:PRK05771 166 VENVEYISTDKGYVYvvvvvlKELSDEVEEELKKLG-------FERLELEEEGTPSELiREIKEELEEIEKERESLLEEL 238
|
250 260
....*....|....*....|..
gi 1655220527 2480 QELQNKSKETASAQQEQMEQQK 2501
Cdd:PRK05771 239 KELAKKYLEELLALYEYLEIEL 260
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1270-1500 |
2.85e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.27 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1270 LKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYidsLKDYEFQILAYRALQdpIASPLKKPKMEsaSDNIIQEYVTLRTRY 1349
Cdd:TIGR01612 1488 LKEHIDKSKGCKDEADKNAKAIEKNKELFEQY---KKDVTELLNKYSALA--IKNKFAKTKKD--SEIIIKEIKDAHKKF 1560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1350 SELSTLTSQYIKFILETQRRLEDDEKASEK-----------LKEDEKK--RMAEIQAQLETQKQLAEGHAKSVAKAELEA 1416
Cdd:TIGR01612 1561 ILEAEKSEQKIKEIKKEKFRIEDDAAKNDKsnkaaidiqlsLENFENKflKISDIKKKINDCLKETESIEKKISSFSIDS 1640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1417 QELKLKMKEDASQR-QGLAVDAEKQKQNIQLELTQLKNLsEQEIRS---------KNQQL-------EEAQVSRRKLEEE 1479
Cdd:TIGR01612 1641 QDTELKENGDNLNSlQEFLESLKDQKKNIEDKKKELDEL-DSEIEKieidvdqhkKNYEIgiiekikEIAIANKEEIESI 1719
|
250 260
....*....|....*....|.
gi 1655220527 1480 IHLIRIQLQTTIKQKSTADDE 1500
Cdd:TIGR01612 1720 KELIEPTIENLISSFNTNDLE 1740
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2187-2563 |
2.90e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 43.90 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2187 KEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVND--AVKQKAQVENELSkvkmQMDELLKLKVRIEE 2264
Cdd:pfam13166 89 EESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDecWKKIKRKKNSALS----EALNGFKYEANFKS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2265 ENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEqrALAEKMLKeKMQAIQEATKLKAEA 2344
Cdd:pfam13166 165 RLLREIEKDNFNAGVLLSDEDRKAALATVFSDNKPEIAPLTFNVIDFDALEKAE--ILIQKVIG-KSSAIEELIKNPDLA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2345 EELQkqknQAQEKAKKLLED----KQEIQQRL--------DKETQGFQKSLEaERKRQLE--ISAEAEKLKLRVKELSSA 2410
Cdd:pfam13166 242 DWVE----QGLELHKAHLDTcpfcGQPLPAERkaaleahfDDEFTEFQNRLQ-KLIEKVEsaISSLLAQLPAVSDLASLL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2411 QAkaeeeatrFKKQADEAKVRLQETEKQTtETVVQKLETQRLQSTREADdLKKAIAELEKEREKLKRdAQELQNKSKETA 2490
Cdd:pfam13166 317 SA--------FELDVEDIESEAEVLNSQL-DGLRRALEAKRKDPFKSIE-LDSVDAKIESINDLVAS-INELIAKHNEIT 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 2491 SAQQEQMEQQKAMLQQTFLTEkellLKRERDVEDEKKKLqkhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQA 2563
Cdd:pfam13166 386 DNFEEEKNKAKKKLRLHLVEE----FKSEIDEYKDKYAG---LEKAINSLEKEIKNLEAEIKKLREEIKELEA 451
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2281-2460 |
2.98e-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: 43.45 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2281 LAEEAEKMKSLAEEAARL-SVEAEETARQRKTAEAElaeqralAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAK 2359
Cdd:pfam05262 186 LREDNEKGVNFRRDMTDLkERESQEDAKRAQQLKEE-------LDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2360 KlLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQT 2439
Cdd:pfam05262 259 N-LPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDL 337
|
170 180
....*....|....*....|.
gi 1655220527 2440 TETVVQKletqRLQSTREADD 2460
Cdd:pfam05262 338 QKTKPQV----EAQPTSLNED 354
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2421-2605 |
2.99e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.36 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2421 FKKQADEAKVRLQETEKQTtETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQME-- 2498
Cdd:pfam04012 9 VRANIHEGLDKAEDPEKML-EQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2499 --QQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKhledevNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAE 2576
Cdd:pfam04012 88 alAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAA------LETKIQQLKAKKNLLKARLKAAKAQEAVQTSLGSLSTSS 161
|
170 180 190
....*....|....*....|....*....|....
gi 1655220527 2577 A-----EMKNKQKEMEALEKKRLEQEKLLADENK 2605
Cdd:pfam04012 162 AtdsfeRIEEKIEEREARADAAAELASAVDLDAK 195
|
|
| PTZ00332 |
PTZ00332 |
paraflagellar rod protein; Provisional |
2287-2507 |
3.04e-03 |
|
paraflagellar rod protein; Provisional
Pssm-ID: 240364 [Multi-domain] Cd Length: 589 Bit Score: 43.80 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2287 KMKSLAEEAARLSVEAEETARQRKTAEAELAE-------QRALA--EKMLKEKMQAIQEATKLK---------AEAEELQ 2348
Cdd:PTZ00332 138 KMEKVEEELRRSQLDATQLAQVPTATLKNIEDimnvtqiQNALAstDDQIKTQLAQLEKTNEIQnvamhdgemQVAEEQM 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2349 KQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEiSAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEA 2428
Cdd:PTZ00332 218 WTKVQLQERLIELVADKFRLIGKCEEENKSFSKIHEVQKQANQE-TSQMKDAKRRLKQRCETDLKHIHDAIQKADLEDAE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2429 KVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKER-EKLKRDAQELQNKSKETASAQQ--EQMEQQKAMLQ 2505
Cdd:PTZ00332 297 AMKRYATNKEKSERFIRENEDRQEEAWNKIQDLERQLQRLGTERfEEVKRRIEENDREEKRRVEYQQflEVAGQHKKLLE 376
|
..
gi 1655220527 2506 QT 2507
Cdd:PTZ00332 377 LT 378
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1508-1972 |
3.06e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1508 AAEAEKVRKAAQEEAERLRKQvneETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVR 1587
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQA---EAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1588 QIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALR 1667
Cdd:COG3064 78 KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1668 LRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFE 1747
Cdd:COG3064 158 RAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1748 HAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEA 1827
Cdd:COG3064 238 EATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1828 ARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQ 1907
Cdd:COG3064 318 LAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 1908 AAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVEL 1972
Cdd:COG3064 398 GGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADAL 462
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2029-2201 |
3.13e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2029 KAAQDEVERLKQKAAEANKLKDKAEKELEKQvilaKEAAQKSTAAEQKAQDVLSKNKEDllsqeklrdefENAKKLAQAA 2108
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQ----AEEAEKQRAAEQARQKELEQRAAA-----------EKAAKQAEQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2109 ETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAErlrkeaeAEAAKRAAAEAAALKQKQEADAEM-AKHKK 2187
Cdd:TIGR02794 111 AKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE-------EEAKAKAAAEAKKKAEEAKKKAEAeAKAKA 183
|
170
....*....|....
gi 1655220527 2188 EAEQALKQKSQVEK 2201
Cdd:TIGR02794 184 EAEAKAKAEEAKAK 197
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
2201-2536 |
3.15e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.88 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2201 KELGLVKLQLDEtdKQKALMDEELQRVKAQVNDAVK-QKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNK--DNT 2277
Cdd:PTZ00108 983 KEFYLVRLDLYK--KRKEYLLGKLERELARLSNKVRfIKHVINGELVITNAKKKDLVKELKKLGYVRFKDIIKKKseKIT 1060
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2278 QKLLAEEAEKMKSLAEEAARLSVEAEE------------TARQRKTAEAELAEQRALAEKMLK----------------- 2328
Cdd:PTZ00108 1061 AEEEEGAEEDDEADDEDDEEELGAAVSydyllsmpiwslTKEKVEKLNAELEKKEKELEKLKNttpkdmwledldkfeea 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2329 -EKMQAIQEATKLKAE---------AEELQKQKNQAQEKAKK-------------------LLEDKQEIQQRLDKETQGF 2379
Cdd:PTZ00108 1141 lEEQEEVEEKEIAKEQrlksktkgkASKLRKPKLKKKEKKKKkssadkskkasvvgnskrvDSDEKRKLDDKPDNKKSNS 1220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2380 QKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREAD 2459
Cdd:PTZ00108 1221 SGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGS 1300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 2460 DLKKAIAELEKEREKLKRDAQELQNKSKETASAQQE--QMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDE 2536
Cdd:PTZ00108 1301 KPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKskTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDE 1379
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2184-2484 |
3.18e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 43.02 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2184 KHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIE 2263
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2264 EENLRLMQKNKdntqKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQralaEKMLKEKMQAIQEATKLKAE 2343
Cdd:pfam09728 81 KQNKKLKEESK----KLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREE----NEELREKLKSLIEQYELREL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2344 -------AEELQKQKNQAqeKAKKLLEDKQEIQQ-----RLDKETQGFQKSLEAERKRQLEISAEAEKLKlrvkELSSAQ 2411
Cdd:pfam09728 153 hfekllkTKELEVQLAEA--KLQQATEEEEKKAQekevaKARELKAQVQTLSETEKELREQLNLYVEKFE----EFQDTL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220527 2412 AKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQR--LQSTREADDLKKAIAELEKEREKLKRDAQELQN 2484
Cdd:pfam09728 227 NKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKalLEMAEERQKLKEELEKLQKKLEKLENLCRALQA 301
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1378-1590 |
3.21e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1378 EKLKEDEKKRmAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAV------DAEKQKQNIQLELTQL 1451
Cdd:COG1340 57 EEAQELREKR-DELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKlrkeieRLEWRQQTEVLSPEEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1452 KNLSEQeIRSKNQQLEEAQVSRrKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE 1531
Cdd:COG1340 136 KELVEK-IKELEKELEKAKKAL-EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADE 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1532 ETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAE-EEKVRQIK 1590
Cdd:COG1340 214 LHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEElEEKAEEIF 273
|
|
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
1426-1568 |
3.28e-03 |
|
Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.
Pssm-ID: 462860 [Multi-domain] Cd Length: 187 Bit Score: 41.82 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1426 DASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKN---QQLEEAQVSRRKLEEEIhliriqlqttikqkstaDDELQ 1502
Cdd:pfam09727 57 DSELLRDQSQDEDVYEAMYEKPLAELEKLVEKQRETQRrmlEQLAAAEKRHRRVIREL-----------------EEEKR 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220527 1503 KLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSE-AEKEAARQKQKALDELQKHK 1568
Cdd:pfam09727 120 KHARDTAQGDDFTYLLEKERERLKQELEQEKAQQKRLEKELKKLLEkLEEELSKQKQIALLLVKERK 186
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2417-2615 |
3.32e-03 |
|
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: 42.05 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2417 EATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETA---SAQ 2493
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2494 QEQMEQQKAMLQQtfltekeLLLKRERDVEDEKKKLQKHLEDEvnkaKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQK 2573
Cdd:cd00176 81 LEELNQRWEELRE-------LAEERRQRLEEALDLQQFFRDAD----DLEQWLEEKEAALASEDLGKDLESVEELLKKHK 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1655220527 2574 EAEAEMKNKQKEMEALEKKRLE-QEKLLADENKKLREKLESLE 2615
Cdd:cd00176 150 ELEEELEAHEPRLKSLNELAEElLEEGHPDADEEIEEKLEELN 192
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2264-2372 |
3.35e-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: 40.29 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2264 EENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAE 2343
Cdd:pfam20492 12 EERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEE 91
|
90 100
....*....|....*....|....*....
gi 1655220527 2344 AEELQKQKNQAQEKAKKLLEDKQEIQQRL 2372
Cdd:pfam20492 92 IARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1146-1304 |
3.41e-03 |
|
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: 42.05 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1146 AEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQlagSLLERWQAVFAQIDLRQ 1225
Cdd:cd00176 23 LSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE---ELNQRWEELRELAEERR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 1226 RELSLLGRHMNSYKQSYEwLIQWLREARLRQEKIEAAPvwDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDS 1304
Cdd:cd00176 100 QRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEE 175
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1416-1901 |
3.51e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1416 AQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQttIKQKS 1495
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAE--AAKKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1496 TADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAE 1575
Cdd:COG3064 80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1576 RRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKEL 1655
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1656 ETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSA 1735
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1736 EQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLET 1815
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1816 EALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAE 1895
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLAD 479
|
....*.
gi 1655220527 1896 DEAYQR 1901
Cdd:COG3064 480 LLLLGG 485
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2174-2338 |
3.51e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2174 QKQEADAEMAKHKKEAEQALKQKSQVEKELglvklQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMD 2253
Cdd:PRK12705 31 LAKEAERILQEAQKEAEEKLEAALLEAKEL-----LLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2254 ELLKLKVRIEEENLRLMQKNKDNTQKLlaEEAEKMKS---LAEEAARLSVEAEETARQRKTAEAELA--EQRALAEKMLK 2328
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNEL--YRVAGLTPeqaRKLLLKLLDAELEEEKAQRVKKIEEEAdlEAERKAQNILA 183
|
170
....*....|
gi 1655220527 2329 EKMQAIQEAT 2338
Cdd:PRK12705 184 QAMQRIASET 193
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
2213-2409 |
3.54e-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: 43.08 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2213 TDKQKALMDEELQrvkaqvndAVKQKAQVENELS--KVKMQMDELLKLKVrieEENLRLMQKNKdntqKLLAEEAEKMKS 2290
Cdd:smart00787 108 SPDVKLLMDKQFQ--------LVKTFARLEAKKMwyEWRMKLLEGLKEGL---DENLEGLKEDY----KLLMKELELLNS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2291 LAEEAARLSVEAEETARQRKTAEAEL-----AEQRALAEKMLKEKMQAIQEATKLkaeaEELQKQKNQAQEKAKKLLEDK 2365
Cdd:smart00787 173 IKPKLRDRKDALEEELRQLKQLEDELedcdpTELDRAKEKLKKLLQEIMIKVKKL----EELEEELQELESKIEDLTNKK 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1655220527 2366 QEIQQRLDKETQGFQKSLEAERKrqleisaEAEKLKLRVKELSS 2409
Cdd:smart00787 249 SELNTEIAEAEKKLEQCRGFTFK-------EIEKLKEQLKLLQS 285
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1672-1789 |
3.59e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.11 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1672 AEEEAQRKSL-AQEEAEKQKTEAERDakkkakaEEAALKQKENAEKELEKQRTFAEQ--IAQQKL-SAEQEYIRLKADFE 1747
Cdd:COG1566 93 AAAEAQLARLeAELGAEAEIAAAEAQ-------LAAAQAQLDLAQRELERYQALYKKgaVSQQELdEARAALDAAQAQLE 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1748 HAEQQRGLL------DNELQRLKNEVNAAEKQRRQLEDELAK--VRSEMD 1789
Cdd:COG1566 166 AAQAQLAQAqaglreEEELAAAQAQVAQAEAALAQAELNLARttIRAPVD 215
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1327-1560 |
3.67e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1327 KKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDekkrMAEIQAQLETQKQLAEGHA 1406
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1407 KSVAKAELEAQELKL----KMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEihl 1482
Cdd:COG3883 93 RALYRSGGSVSYLDVllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA--- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 1483 iRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKA 1560
Cdd:COG3883 170 -KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3153-3190 |
3.80e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.80e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1655220527 3153 IRLLEAQLSTGGIIDPVKSYRVPQEVACKRGYFNEEMA 3190
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1534-1657 |
3.83e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 40.31 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1534 QKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQaeeekvrqikvvEEVAQKTAATQLQamsfsekt 1613
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYER------------ELVLHAEDIKALQ-------- 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655220527 1614 tKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELET 1657
Cdd:pfam07926 61 -ALREELNELKAEIAELKAEAESAKAELEESEESWEEQKKELEK 103
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1333-1575 |
3.83e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1333 SASDNIIQEYVTLRTRYSELSTLTSQyikfILETQRRLEDDEKASEKLKEDEKKRMAEIQaqlETQKQLAEghaksvAKA 1412
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAE------AEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1413 ELEAQELKLKMKEDASQRQGLAVDAEKQ---KQNIQLELTQLKNLSeQEIRSKNQQLEEAQVSRRKLEEeihliriqlqt 1489
Cdd:COG3883 80 EIEERREELGERARALYRSGGSVSYLDVllgSESFSDFLDRLSALS-KIADADADLLEELKADKAELEA----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1490 tikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKM 1569
Cdd:COG3883 148 ---KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
....*.
gi 1655220527 1570 QAEEAE 1575
Cdd:COG3883 225 AAAAAA 230
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3780-3814 |
3.84e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.84e-03
10 20 30
....*....|....*....|....*....|....*
gi 1655220527 3780 KLLSAERAVTGYKDPYSGKVISLFQAMKKGLVPED 3814
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
2439-2620 |
3.84e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.77 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2439 TTETVVQKLETQRLQSTRE-------ADDLKkaiAELEKER---EKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQ-T 2507
Cdd:PLN03188 1041 TDESPEKKLEQERLRWTEAeskwislAEELR---TELDASRalaEKQKHELDTEKRCAEELKEAMQMAMEGHARMLEQyA 1117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2508 FLTEKEL-LLKRERDVE---DEKKKL----------QKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMD---EAVK 2570
Cdd:PLN03188 1118 DLEEKHIqLLARHRRIQegiDDVKKAaaragvrgaeSKFINALAAEISALKVEREKERRYLRDENKSLQAQLRdtaEAVQ 1197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1655220527 2571 KQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENK---KLREKLESLEVTSKQ 2620
Cdd:PLN03188 1198 AAGELLVRLKEAEEALTVAQKRAMDAEQEAAEAYKqidKLKRKHENEISTLNQ 1250
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2362-2556 |
3.97e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.97 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2362 LEDKQEIQQR-LDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTT 2440
Cdd:pfam04012 16 GLDKAEDPEKmLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEKKSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2441 ETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKeTASAqQEQMEQQKAMLQQTFLTEKELLLKRER 2520
Cdd:pfam04012 96 EKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLK-AAKA-QEAVQTSLGSLSTSSATDSFERIEEKI 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1655220527 2521 DVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDE 2556
Cdd:pfam04012 174 EEREARADAAAELASAVDLDAKLEQAGIQMEVSEDV 209
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1613-1737 |
4.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1613 TTKLEESLKKEQGTVLQLQEEAEKLRKQ-----EEEANKAREQAEKELETWRLKANEALRlRLRAEEEAQRKSLaqEEAE 1687
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEalleaKEEIHKLRNEFEKELRERRNELQKLEK-RLLQKEENLDRKL--ELLE 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1688 KQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQqkLSAEQ 1737
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG--LTAEE 154
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1365-1960 |
4.12e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1365 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAK--AELEAQELKLKMKEDASQRQGLAVDAEKQKQ 1442
Cdd:pfam10174 116 ENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKllEMLQSKGLPKKSGEEDWERTRRIAEAEMQLG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1443 NIQLELTQLKnlseqeirSKNQQLEEAQVSRRKLEEEIHLIRiQLQTTIKQKSTADDELQK-LRDQAAEAEKVRKAA--- 1518
Cdd:pfam10174 196 HLEVLLDQKE--------KENIHLREELHRRNQLQPDPAKTK-ALQTVIEMKDTKISSLERnIRDLEDEVQMLKTNGllh 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1519 QEEAERLRKQV---NEETQKKKNAEDELKR---KSEAEKEAARQKQKALD----------ELQKHKMQAEEAERRLKQAE 1582
Cdd:pfam10174 267 TEDREEEIKQMevyKSHSKFMKNKIDQLKQelsKKESELLALQTKLETLTnqnsdckqhiEVLKESLTAKEQRAAILQTE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1583 EEKVRQIKVVEEVAQKTAATQLQAMSfSEKTT------KLEESLKKEQGTVLQLQEEAEKLRKQEEEANKARE---QAEK 1653
Cdd:pfam10174 347 VDALRLRLEEKESFLNKKTKQLQDLT-EEKSTlageirDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAglkERVK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1654 ELETWRLKANEAlrlrLRAEEEAqrksLAQEE--AEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTfaeqiaqQ 1731
Cdd:pfam10174 426 SLQTDSSNTDTA----LTTLEEA----LSEKEriIERLKEQREREDRERLEELESLKKENKDLKEKVSALQP-------E 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1732 KLSAEQEYIRLKadfEHAEQQRGLLDNELQRLKnevnaaekqrrQLEDELAKVRSEMDALlqmkiQAEKVSQSNTEKSKQ 1811
Cdd:pfam10174 491 LTEKESSLIDLK---EHASSLASSGLKKDSKLK-----------SLEIAVEQKKEECSKL-----ENQLKKAHNAEEAVR 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1812 LLETEALKMKQLAEEAARLRSvaEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRL---KTEAEVALKAKEAENE 1888
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKE--ESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLrqmKEQNKKVANIKHGQQE 629
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220527 1889 RLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETlrQKKVVEEEIHIIRINFER 1960
Cdd:pfam10174 630 MKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSST--QQSLAEKDGHLTNLRAER 699
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2440-2640 |
4.35e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2440 TETVVQKLETQRLQ--STREADDLKKAIAElEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLK 2517
Cdd:PRK09510 57 PGAVVEQYNRQQQQqkSAKRAEEQRKKKEQ-QQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2518 RERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAimdEAvKKQKEAEAEMK-----NKQKEMEALEKK 2592
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAA---EA-KKKAEAEAAAKaaaeaKKKAEAEAKKKA 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1655220527 2593 RLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2640
Cdd:PRK09510 212 AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
2469-2590 |
4.41e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.74 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2469 EKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQqTFLTEkelLLKRERDVEDEKKKLQKHLEDEV--NKAKALKDE 2546
Cdd:cd22656 109 DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLT-DFENQ---TEKDQTALETLEKALKDLLTDEGgaIARKEIKDL 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655220527 2547 QQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALE 2590
Cdd:cd22656 185 QKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
533-626 |
4.66e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 39.62 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 533 LRYIQDLLGWVEENQRRVDDGEWGSDLPAVESQLGSHRGLHQSVEEFRSKIERAKADESQI---SPASKAAYRDYLAKLE 609
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*..
gi 1655220527 610 LQYDKLLHDSKARLRYL 626
Cdd:smart00150 84 ERWEELKELAEERRQKL 100
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1821-1920 |
4.72e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1821 KQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKIlkEKLAAineatrlktEAEVALKAKEAENERLKRQAE----D 1896
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVAL--EGLAA---------ELEEKQQELEAQLEQLQEKAAetsqE 213
|
90 100
....*....|....*....|....
gi 1655220527 1897 EAYQRKLLEDQAAQhKHDIQEKIT 1920
Cdd:PRK11448 214 RKQKRKEITDQAAK-RLELSEEET 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1076-1447 |
4.72e-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: 43.52 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1076 ILASPQQSSSAPMLRS-------ELDVTLKKMDHVYGLSSVYLDKLKtidiviRNTKDAEDTVKSYESRLRDVSKVPAEE 1148
Cdd:TIGR02169 666 ILFSRSEPAELQRLRErleglkrELSSLQSELRRIENRLDELSQELS------DASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1149 KEVEAHRSQLKAMRAEAEADQATFDRLQDELKAAtsvsdkmtrLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQREL 1228
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEED---------LHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1229 SLLGRHMNSYKQSYEWLIQWLREARlrQEKIEAAPVWDSKalKEQLTQEKKLLE-EIEKNKDQIENCQKDAKAYIDSLKD 1307
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEI--QELQEQRIDLKEQ--IKSIEKEIENLNgKKEELEEELEELEAALRDLESRLGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1308 YEFQILAYRAlqdpiasplKKPKMESASDNIIQEYVTLRTRYSELST---LTSQYIKFILETQRRLEDDEKAS---EKLK 1381
Cdd:TIGR02169 887 LKKERDELEA---------QLRELERKIEELEAQIEKKRKRLSELKAkleALEEELSEIEDPKGEDEEIPEEElslEDVQ 957
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 1382 EDEKKRMAEIQAqLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLE 1447
Cdd:TIGR02169 958 AELQRVEEEIRA-LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1411-2103 |
5.10e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1411 KAELEAQELKLKMKEDasqrqgLAVDAEKQKQNIQlelTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTT 1490
Cdd:TIGR04523 46 KNELKNKEKELKNLDK------NLNKDEEKINNSN---NKIKIL-EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1491 IKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKkknAEDELKRKSEAEKEaarqkqkaLDELQKHKMQ 1570
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK---YNDLKKQKEELENE--------LNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1571 AEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGtvlQLQEEAEKLRKQEEEANKAREQ 1650
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ---EINEKTTEISNTQTQLNQLKDE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1651 AEKELETWRLKANEAlrlrlraeeEAQRKSLAQEEAEKQKTEAErdakkkakaeeaalKQKENAEKELEKQRTFAEQIAQ 1730
Cdd:TIGR04523 262 QNKIKKQLSEKQKEL---------EQNNKKIKELEKQLNQLKSE--------------ISDLNNQKEQDWNKELKSELKN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1731 QklsaEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDaLLQMKIQAEKVSQSNTEKSK 1810
Cdd:TIGR04523 319 Q----EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE-KLKKENQSYKQEIKNLESQI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1811 QLLETEALKMKQLAEEaarlrsvaeeakKQRQLaedeaarQRAEAEKILKEKlaaineatrlkteaevalkakeaENERL 1890
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQ------------KDEQI-------KKLQQEKELLEK-----------------------EIERL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1891 KRQAEDEAYQRKLLEDQAAQHKHDIQ--EKITQLQSSSVSELDRQKNIVEETLRQKKvveEEIHIIRINFERASKEKSDL 1968
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKnlDNTRESLETQLKVLSRSINKIKQNLEQKQ---KELKSKEKELKKLNEEKKEL 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1969 EVELKKLKgiadetqKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAA--RQRKAAQDEVERLKQkaaEAN 2046
Cdd:TIGR04523 509 EEKVKDLT-------KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQ---TQK 578
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220527 2047 KLKDKAEkelEKQVILAKEAAQKstaaeqkaQDVLSKNKEDLLSQEKLRDEFENAKK 2103
Cdd:TIGR04523 579 SLKKKQE---EKQELIDQKEKEK--------KDLIKEIEEKEKKISSLEKELEKAKK 624
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
186-263 |
5.33e-03 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 39.21 E-value: 5.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 186 DNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSvAERELGVTRLLDPEDVDVAHPDEKSIITYVSSL 263
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2121-2324 |
5.51e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2121 LLRQKAEEAEKLKKAAEDEAAKQAKAQKDaerlrkeaeaeaakraaaeaaalKQKQEADAEMAKHKKEAEQALKQKsqvE 2200
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKK-----------------------EALLEAKEEIHKLRNEFEKELRER---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2201 KELGlvklQLDETDKQK-ALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQK 2279
Cdd:PRK12704 82 NELQ----KLEKRLLQKeENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1655220527 2280 LLAEEAEkmKSLAEEAARLSVEAEETARQRKTAEAE----LAEQRALAE 2324
Cdd:PRK12704 158 ILLEKVE--EEARHEAAVLIKEIEEEAKEEADKKAKeilaQAIQRCAAD 204
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2031-2614 |
5.55e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2031 AQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAqaaet 2110
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL----- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2111 akekaekeaallRQKAEEAEKLKKAAEDEAAKQAKAQKdaERLRKEAEAEAAKRaaaeaaalkQKQEADAEMAKHKKEAE 2190
Cdd:COG4913 322 ------------REELDELEAQIRGNGGDRLEQLEREI--ERLERELEERERRR---------ARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2191 QAlkqksQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVK----------MQMDELLKLKV 2260
Cdd:COG4913 379 AE-----EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksniparlLALRDALAEAL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2261 RIEEENLR----LMQ-KNKD-----------NTQK--LLAEEA--------------------EKMKSLAEEAARLSVEA 2302
Cdd:COG4913 454 GLDEAELPfvgeLIEvRPEEerwrgaiervlGGFAltLLVPPEhyaaalrwvnrlhlrgrlvyERVRTGLPDPERPRLDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2303 EETARQ--------RKTAEAELAEQRALA----EKMLKEKMQAIQEA--TKLKAEAEELQKQKN---------QAQEKAK 2359
Cdd:COG4913 534 DSLAGKldfkphpfRAWLEAELGRRFDYVcvdsPEELRRHPRAITRAgqVKGNGTRHEKDDRRRirsryvlgfDNRAKLA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2360 KLLEDKQEIQQRLDkETQGFQKSLEAERKRQLEISAEAEKL-KLRVKELSSAQAKAE-EEATRFKKQADEAKVRLQETEK 2437
Cdd:COG4913 614 ALEAELAELEEELA-EAEERLEALEAELDALQERREALQRLaEYSWDEIDVASAEREiAELEAELERLDASSDDLAALEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2438 QttetvVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQnksKETASAQQEQMEQQKAMLQQTFltEKELLLK 2517
Cdd:COG4913 693 Q-----LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ---DRLEAAEDLARLELRALLEERF--AAALGDA 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2518 RERDVedekkklqkhledevnkAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMknkQKEMEALEKKRLEQE 2597
Cdd:COG4913 763 VEREL-----------------RENLEERIDALRARLNRAEEELERAMRAFNREWPAETADL---DADLESLPEYLALLD 822
|
650
....*....|....*..
gi 1655220527 2598 KLLADENKKLREKLESL 2614
Cdd:COG4913 823 RLEEDGLPEYEERFKEL 839
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2310-2614 |
5.59e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 42.71 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2310 KTAEAELAEQRALAEKMLkEKMQaiQEATKLKAEAEELQKQKNQAQ---EKAKKLLEdkqEIQQRLDKetqgfqKSLEAE 2386
Cdd:pfam05701 27 KAHRIQTVERRKLVELEL-EKVQ--EEIPEYKKQSEAAEAAKAQVLeelESTKRLIE---ELKLNLER------AQTEEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2387 RKRQleisaEAEKLKLRVKEL-------SSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREAD 2459
Cdd:pfam05701 95 QAKQ-----DSELAKLRVEEMeqgiadeASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2460 DLKKAIAELEKEREKLkrdAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKElLLKRERDVEDEKKKLQKhLEDEVNK 2539
Cdd:pfam05701 170 EAVSASKEIEKTVEEL---TIELIATKESLESAHAAHLEAEEHRIGAALAREQD-KLNWEKELKQAEEELQR-LNQQLLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2540 AKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMK---NKQKEMEALEKKRLEQEKL----LADENKKLREKLE 2612
Cdd:pfam05701 245 AKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKktsTSIQAALASAKKELEEVKAniekAKDEVNCLRVAAA 324
|
..
gi 1655220527 2613 SL 2614
Cdd:pfam05701 325 SL 326
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3447-3483 |
5.86e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.08 E-value: 5.86e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1655220527 3447 KLLSAEKAVTGYKDPYTGNKISLFQAMTKELVLREHA 3483
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2124-2390 |
6.01e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.14 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2124 QKAEEAEKLKKAAEDEAAKQAKAQKDAERlrkEAEAEAAKRAAAEAAALKQKQEADAEmaKHKKEAEQALKQKSQVEKEl 2203
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQ---QAEEAEKQRAAEQARQKELEQRAAAE--KAAKQAEQAAKQAEEKQKQ- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2204 glvklqldetdkqkalmDEELqrvKAQVNDAVKQKAQVENElskvkmqmdellklkvrieeenlrlmQKNKDNTQKllAE 2283
Cdd:TIGR02794 121 -----------------AEEA---KAKQAAEAKAKAEAEAE--------------------------RKAKEEAAK--QA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2284 EAEKMKSLAEEAARLSVEAEETARQRKTAEAElAEQRALAekmlkEKMQAIQEATKLKAEAEelQKQKNQAQEKAKKLLE 2363
Cdd:TIGR02794 153 EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAE-AEAKAKA-----EEAKAKAEAAKAKAAAE--AAAKAEAEAAAAAAAE 224
|
250 260
....*....|....*....|....*..
gi 1655220527 2364 DKQEIQQRLDKETQGFQKSLEAERKRQ 2390
Cdd:TIGR02794 225 AERKADEAELGDIFGLASGSNAEKQGG 251
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
2469-2612 |
6.04e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 41.61 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2469 EKEREKLKRDAQElqnKSKETASAQQEQMEQQKAMLQQtfltEKElllKRERDVEDEKKKLQKHLEDEVNKaKALKDEQQ 2548
Cdd:pfam13904 43 KLEGLKLERQPLE---AYENWLAAKQRQRQKELQAQKE----ERE---KEEQEAELRKRLAKEKYQEWLQR-KARQQTKK 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 2549 RQQKLMDEEKKKLQAIMDEAVKKQKEAEAemKNKQKEMEaLEKKRLEQEKLLADENKKLREKLE 2612
Cdd:pfam13904 112 REESHKQKAAESASKSLAKPERKVSQEEA--KEVLQEWE-RKKLEQQQRKREEEQREQLKKEEE 172
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
38-84 |
6.52e-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: 39.18 E-value: 6.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1655220527 38 KKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRE 84
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVP 49
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
2207-2352 |
6.52e-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: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2207 KLQLDETDkqkALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAE 2286
Cdd:smart00787 146 KEGLDENL---EGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMI 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 2287 KMKSLAE---EAARLSVEAEETARQRKTAEAELAEQRalaEKMLKEKMQAIQEATKLKAEAEELQKQKN 2352
Cdd:smart00787 223 KVKKLEEleeELQELESKIEDLTNKKSELNTEIAEAE---KKLEQCRGFTFKEIEKLKEQLKLLQSLTG 288
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1155-1398 |
6.57e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1155 RSQLKAMRAEAEAdqatfdrLQDELKAATSVSDKMTRLHSERDAELEHYRQLAgsllerwQAVFAQIDLR--QRELSLLG 1232
Cdd:COG4913 609 RAKLAALEAELAE-------LEEELAEAEERLEALEAELDALQERREALQRLA-------EYSWDEIDVAsaEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1233 RHMNSYKQSYEWLIQWLREARLRQEKIEAApvwdSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQI 1312
Cdd:COG4913 675 AELERLDASSDDLAALEEQLEELEAELEEL----EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1313 LAYRaLQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIK-FILETQ----------------RRLEDD-- 1373
Cdd:COG4913 751 LEER-FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNReWPAETAdldadleslpeylallDRLEEDgl 829
|
250 260
....*....|....*....|....*....
gi 1655220527 1374 ----EKASEKLKEDEKKRMAEIQAQLETQ 1398
Cdd:COG4913 830 peyeERFKELLNENSIEFVADLLSKLRRA 858
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
2495-2599 |
6.60e-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: 41.90 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2495 EQMEQQKAMLQQTflTEKELLLkrERDVEDEKKKLQKHLEDEVNKAKAlkdeqQRQQKLMDEE-KKKLQAIMDEA-VKKQ 2572
Cdd:cd03406 169 EAMEAEKTKLLIA--EQHQKVV--EKEAETERKRAVIEAEKDAEVAKI-----QMQQKIMEKEaEKKISEIEDEMhLARE 239
|
90 100
....*....|....*....|....*...
gi 1655220527 2573 KE-AEAEMKNKQKEMEAlEKKRLEQEKL 2599
Cdd:cd03406 240 KArADAEYYRALREAEA-NKLKLTPEYL 266
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1437-1640 |
6.60e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 42.72 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1437 AEKQKQNIQLELTQLKNLSEQEIRS---KNQQLEEAQVSRRkleeeIHLIRIQlqttiKQKSTadDELQKLRDQaaeaek 1513
Cdd:pfam10168 522 ADKLSSPSPQECLQLLSRATQVFREeylKKHDLAREEIQKR-----VKLLKLQ-----KEQQL--QELQSLEEE------ 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1514 vRKAAQEEAERLRKQVNE--ETQKK---------KNAEDELKRKSEAEKEAARqkqkaldELQKHKMQAEEAERRLKQAE 1582
Cdd:pfam10168 584 -RKSLSERAEKLAEKYEEikDKQEKlmrrckkvlQRLNSQLPVLSDAEREMKK-------ELETINEQLKHLANAIKQAK 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220527 1583 EEKVRQIKvveEVAQKTAATQLQAMSFSEKTTK-LEESLKKEQGTVLQLQEEAEKLRKQ 1640
Cdd:pfam10168 656 KKMNYQRY---QIAKSQSIRKKSSLSLSEKQRKtIKEILKQLGSEIDELIKQVKDINKH 711
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1370-1654 |
6.85e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.53 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1370 LEDDEKASEKLKEDEKKRMAEIQAQLET-QKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDA---EKQKQNIQ 1445
Cdd:PLN03229 413 VDPERKVNMKKREAVKTPVRELEGEVEKlKEQILKAKESSSKPSELALNEMIEKLKKEIDLEYTEAVIAmglQERLENLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1446 LELTQLKnlseqeirSKNQQLEEAQVSR-RKLEEEIH--LIRIQLQTTIKQKstaddeLQKLRDqaAEAEKVRKAAQEEA 1522
Cdd:PLN03229 493 EEFSKAN--------SQDQLMHPVLMEKiEKLKDEFNkrLSRAPNYLSLKYK------LDMLNE--FSRAKALSEKKSKA 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1523 ERLRKQVNeetQKKKNAED--ELKRKSEAEK-EAARQKQKALDELQKHkmQAEEAERRLKQAEEEKVRQIKV----VEEV 1595
Cdd:PLN03229 557 EKLKAEIN---KKFKEVMDrpEIKEKMEALKaEVASSGASSGDELDDD--LKEKVEKMKKEIELELAGVLKSmgleVIGV 631
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220527 1596 AQKTAATQLQAM--SFSEKTTKLEESLKKEQGTVLQ---LQEEAEKLRKQEEEANKAREQAEKE 1654
Cdd:PLN03229 632 TKKNKDTAEQTPppNLQEKIESLNEEINKKIERVIRssdLKSKIELLKLEVAKASKTPDVTEKE 695
|
|
| CH_PARVB_rpt2 |
cd21338 |
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ... |
36-153 |
7.09e-03 |
|
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409187 Cd Length: 130 Bit Score: 39.96 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 36 VQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrerdlVRNVRLPREKGRMRFHklqNVQIALDFL 115
Cdd:cd21338 21 VVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVP-----LHNFYLTPESFDQKVH---NVSFAFELM 92
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655220527 116 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 153
Cdd:cd21338 93 QDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1747-1847 |
7.18e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1747 EHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEAlkmKQLAEE 1826
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAA---ETSQER 214
|
90 100
....*....|....*....|.
gi 1655220527 1827 AARLRSVAEEAKKQRQLAEDE 1847
Cdd:PRK11448 215 KQKRKEITDQAAKRLELSEEE 235
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
37-146 |
7.32e-03 |
|
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 39.43 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 37 QKKTFTKWVNKHL---------MKAQRHITDLYEDLRDGHNLISLLEVLSGETLPrERDLVRNVRL-PREKgrmrfhkLQ 106
Cdd:cd21293 2 EKGSYVDHINRYLgddpflkqfLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTID-ERAINTKKVLnPWER-------NE 73
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1655220527 107 NVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 146
Cdd:cd21293 74 NHTLCLNSAKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2026-2329 |
7.50e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2026 RQRKAAQDEVERLKQKAAEAnKLK---DKAEKELEKQvilAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAK 2102
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEA-KARfeaRQARLEREKA---AREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2103 KLAQAAETAKEKAEKEAALLRQKAEEAEKlKKAAEDEAAKQAKAQKDAERlrkeaeaeaakrAAAEAAALKQKQEADAEM 2182
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAE-KQAAAAADPKKAAVAAAIAR------------AKAKKAAQQAANAEAEEE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2183 AKHKKEAEQALKQKSQVEKElglvklqldetdkQKALMDEELQRVKAQVNDavkQKAQVENELSKVKMQMDELLKLKVRI 2262
Cdd:PRK05035 575 VDPKKAAVAAAIARAKAKKA-------------AQQAASAEPEEQVAEVDP---KKAAVAAAIARAKAKKAEQQANAEPE 638
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220527 2263 EEEnlrlmqknkDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAElAEQRALAEKMLKE 2329
Cdd:PRK05035 639 EPV---------DPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAA-AIARAKAKKAAQQ 695
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2026-2356 |
7.53e-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: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2026 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKN--------KEDLLSQEKLRDE 2097
Cdd:COG5185 194 ELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSdkleklveQNTDLRLEKLGEN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2098 FENAKKLAQAAETAKEKAEKEAALLRQKAEEAEklKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQE 2177
Cdd:COG5185 274 AESSKRLNENANNLIKQFENTKEKIAEYTKSID--IKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQES 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2178 ADAEMAKHKKEAEQ--ALKQKSQVEKELGLVKLQLDET----DKQKALMDEELQRVKAQVNDAVK----QKAQVENELSK 2247
Cdd:COG5185 352 LTENLEAIKEEIENivGEVELSKSSEELDSFKDTIESTkeslDEIPQNQRGYAQEILATLEDTLKaadrQIEELQRQIEQ 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2248 VKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMK-SLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKM 2326
Cdd:COG5185 432 ATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ 511
|
330 340 350
....*....|....*....|....*....|
gi 1655220527 2327 LKEKMQAIQEATKLKAEAEELQKQKNQAQE 2356
Cdd:COG5185 512 LEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1419-1654 |
7.54e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1419 LKLKMKEDASQRQGLAVDAEKQKQNIQlelTQLKNLSEQEIRSKN--QQLEEAQVSRRKLEEEIHLIRIQLQTTIK---- 1492
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIK---TYNKNIEEQRKKNGEniARKQNKYDELVEEAKTIKAEIEELTDELLnlvm 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1493 -QKSTADDeLQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKkNAEDELKRKSEAeKEAARQKQKALDELQKHkmQA 1571
Cdd:PHA02562 249 dIEDPSAA-LNKLNTAAAKIKSKIEQFQKVIKMYEKGGVCPTCTQ-QISEGPDRITKI-KDKLKELQHSLEKLDTA--ID 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1572 EEAERrlkqaEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQA 1651
Cdd:PHA02562 324 ELEEI-----MDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 1655220527 1652 EKE 1654
Cdd:PHA02562 399 VKE 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1710-1862 |
7.68e-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: 41.45 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1710 QKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDN--ELQRLKNEVNAAEKQRRQLEDELAKVRSE 1787
Cdd:COG1579 39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMER 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220527 1788 MDALlqmkiqaEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQ-LAEDEAARQRAEAEKILKEK 1862
Cdd:COG1579 119 IEEL-------EEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREeLAAKIPPELLALYERIRKRK 187
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
2454-2645 |
8.25e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 41.26 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2454 STREADDLKKAIAELEKEREKLKRDAQELQNKSkETASAQQEQMEQQKAMLQQ------TFLTEKElllKRERDVEDEKK 2527
Cdd:pfam17078 1 STKVIESLHDQIDALTKTNLQLTVQSQNLLSKL-EIAQQKESKFLENLASLKHendnlsSMLNRKE---RRLKDLEDQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2528 KLQKHLEDEVNKAKALKDE----QQRQQKLMdEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEM-EALEKKRLEQEK---- 2598
Cdd:pfam17078 77 ELKNSYEELTESNKQLKKRlensSASETTLE-AELERLQIQYDALVDSQNEYKDHYQQEINTLqESLEDLKLENEKqlen 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2599 ---LLADENKKLREKLESLEVTSKQaaskTKEIEVQTDKVPEEQLVSMTT 2645
Cdd:pfam17078 156 yqqRISSNDKDIDTKLDSYNNKFKN----LDNIYVNKNNKLLTKLDSLAQ 201
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1148-1694 |
8.28e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1148 EKEVEAHRSQLKAMRAEAEADQATFD-------RLQDELKAAT-------SVSDKM----TRLHSERD---AELEHYRQL 1206
Cdd:pfam01576 516 ERQLSTLQAQLSDMKKKLEEDAGTLEaleegkkRLQRELEALTqqleekaAAYDKLektkNRLQQELDdllVDLDHQRQL 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1207 AgSLLERWQAVFAQIDLRQRELSLlgrhmnsykQSYEWLIQWLREARlrqEKieaapvwDSKALkeQLTQEkklLEEIEK 1286
Cdd:pfam01576 596 V-SNLEKKQKKFDQMLAEEKAISA---------RYAEERDRAEAEAR---EK-------ETRAL--SLARA---LEEALE 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1287 NKDQIENCQKDAKAYIDSL--------KDYEFQILAYRALQDPIASplKKPKMESASDNI-IQEYVTLRTRYSeLSTLTS 1357
Cdd:pfam01576 651 AKEELERTNKQLRAEMEDLvsskddvgKNVHELERSKRALEQQVEE--MKTQLEELEDELqATEDAKLRLEVN-MQALKA 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1358 QYikfiletQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQglavDA 1437
Cdd:pfam01576 728 QF-------ERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGRE----EA 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1438 EKQKQNIQlelTQLKNLSeqeirsknQQLEEAQVSRRKleeeihlIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKA 1517
Cdd:pfam01576 797 VKQLKKLQ---AQMKDLQ--------RELEEARASRDE-------ILAQSKESEKKLKNLEAELLQLQEDLAASERARRQ 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1518 AQEEAERLRKQVNEETQKKKNAEDELKR------KSEAEKEAARQKQKALDE-LQKHKMQAEE------AERRLKQAEEE 1584
Cdd:pfam01576 859 AQQERDELADEIASGASGKSALQDEKRRleariaQLEEELEEEQSNTELLNDrLRKSTLQVEQlttelaAERSTSQKSES 938
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1585 KVRQIkvveEVAQKTAATQLQAMSFSEKtTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANE 1664
Cdd:pfam01576 939 ARQQL----ERQNKELKAKLQEMEGTVK-SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVED 1013
|
570 580 590
....*....|....*....|....*....|
gi 1655220527 1665 ALRLRLRAEEEAQRKSLAQEEAEKQKTEAE 1694
Cdd:pfam01576 1014 ERRHADQYKDQAEKGNSRMKQLKRQLEEAE 1043
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2392-2614 |
8.28e-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: 41.98 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2392 EISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREA--DDLKKAIAELE 2469
Cdd:pfam19220 38 AILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAakEELRIELRDKT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2470 KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERD--VEDEKKKLQKHLEDEVNKA------- 2540
Cdd:pfam19220 118 AQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLalLEQENRRLQALSEEQAAELaeltrrl 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2541 ----KALKDEQQR----QQKLMDE--EKKKLQAIMDEAVKKQKEAEAEMKNKqkeMEALEKKRLEQEKLLADENKKLREK 2610
Cdd:pfam19220 198 aeleTQLDATRARlralEGQLAAEqaERERAEAQLEEAVEAHRAERASLRMK---LEALTARAAATEQLLAEARNQLRDR 274
|
....
gi 1655220527 2611 LESL 2614
Cdd:pfam19220 275 DEAI 278
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1379-1588 |
8.28e-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: 41.98 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1379 KLKEDEKKRMAEIQAQLETQKQLAE---GHAKSVAKAELEAQELK-----LKMKEDASQRQGLAVDaekqKQNIQLElTQ 1450
Cdd:pfam19220 196 RLAELETQLDATRARLRALEGQLAAeqaERERAEAQLEEAVEAHRaerasLRMKLEALTARAAATE----QLLAEAR-NQ 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1451 LKNLSEqEIRSKNQQLEEAQVSRRKLEEEIHliriQLQTtikqkstaddELQKLRDQAAEAEKVRKAAQEEAERLRKQVN 1530
Cdd:pfam19220 271 LRDRDE-AIRAAERRLKEASIERDTLERRLA----GLEA----------DLERRTQQFQEMQRARAELEERAEMLTKALA 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220527 1531 EETQKKKNAE----------DELKRKSEAEKEAARQKQKALDElqkhKMQAEEAERRLKQAEEEKVRQ 1588
Cdd:pfam19220 336 AKDAALERAEeriaslsdriAELTKRFEVERAALEQANRRLKE----ELQRERAERALAQGALEIARE 399
|
|
| LCD1 |
pfam09798 |
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ... |
2340-2460 |
8.31e-03 |
|
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. In Schizosaccharomyces pombe this protein is called Rad26 and in Saccharomyces cerevisiae it is called LCD1.
Pssm-ID: 462906 Cd Length: 615 Bit Score: 42.31 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 2340 LKAEAEELQKQKnqaQEKAKKLLEDKQEIQQRLDKETQGFQKSLEaerkrqleiSAEAEK--LKLRVKELSSAQAKAEEE 2417
Cdd:pfam09798 2 LRDKLELLQQEK---EKELEKLKNSYEELKSSHEEELEKLKQEVQ---------KLEDEKkfLLNELRSLSATSPASSQS 69
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1655220527 2418 ATRFKKQADEAKVRLQETEKQTTETVVQKLetQRLQSTREADD 2460
Cdd:pfam09798 70 HETDTDDSSSVSLKKRKIEESTAESLKQKY--IRLQNNRIVDE 110
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1672-1928 |
8.69e-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: 42.51 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1672 AEEEAQRKSLAQEEAEKQKTEAERdakkkakaeEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIR--LKADFEHA 1749
Cdd:NF012221 1548 SKHAKQDDAAQNALADKERAEADR---------QRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRdaILEESRAV 1618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1750 EQQRGLLDNELQRLKNEVNAAEKQRRQLEDELA-----KVRSEMDallqmkiQAEKVSQSNTEKSKQLLETEALKMKqla 1824
Cdd:NF012221 1619 TKELTTLAQGLDALDSQATYAGESGDQWRNPFAgglldRVQEQLD-------DAKKISGKQLADAKQRHVDNQQKVK--- 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1825 EEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKlL 1904
Cdd:NF012221 1689 DAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ-A 1767
|
250 260
....*....|....*....|....
gi 1655220527 1905 EDQAAQHKHDIQEKITQLQSSSVS 1928
Cdd:NF012221 1768 DAKGAKQDESDKPNRQGAAGSGLS 1791
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4302-4332 |
8.96e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.92 E-value: 8.96e-03
10 20 30
....*....|....*....|....*....|.
gi 1655220527 4302 AGILDTDTLEKVSVTEAIHRNLVDNITGQRL 4332
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1502-1602 |
9.02e-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: 39.77 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1502 QKLRDQAAEAEKVRKAAQEEAERLRKQVNEetqkkknAEDELKR-KSEAEKEAARQKQKALDELQkhkmqaEEAERRLKQ 1580
Cdd:COG0711 34 EKIADGLAEAERAKEEAEAALAEYEEKLAE-------ARAEAAEiIAEARKEAEAIAEEAKAEAE------AEAERIIAQ 100
|
90 100
....*....|....*....|...
gi 1655220527 1581 AEEEKVRQI-KVVEEVAQKTAAT 1602
Cdd:COG0711 101 AEAEIEQERaKALAELRAEVADL 123
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1736-1984 |
9.29e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1736 EQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmKIQAEKVSQSNTEKSKQLLET 1815
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNE-KVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1816 EALKMKQLAEEAARLRsvAEEAKKQRQLAEDEAARQRA----EAEKILkeklaaINEATRLKTEAEVALKAKEAENERLK 1891
Cdd:COG1340 93 ELDELRKELAELNKAG--GSIDKLRKEIERLEWRQQTEvlspEEEKEL------VEKIKELEKELEKAKKALEKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1892 RQAEDEAyqrklLEDQAAQHKHDIQEKITQLQS------SSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEK 1965
Cdd:COG1340 165 LRAELKE-----LRKEAEEIHKKIKELAEEAQElheemiELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
250
....*....|....*....
gi 1655220527 1966 SDLEVELKKLKGIADETQK 1984
Cdd:COG1340 240 RELRKELKKLRKKQRALKR 258
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1599-1856 |
9.72e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1599 TAATQLQAMSfsEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwrlKANEALRlRLRAEEEAQR 1678
Cdd:COG3883 13 FADPQIQAKQ--KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID----KLQAEIA-EAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1679 KSLAQEEAEKQKTEAERDAKKKAKaeeaalkqkeNAE--KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEH----AEQQ 1752
Cdd:COG3883 86 EELGERARALYRSGGSVSYLDVLL----------GSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAkkaeLEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220527 1753 RGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRS 1832
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
250 260
....*....|....*....|....
gi 1655220527 1833 VAEEAKKQRQLAEDEAARQRAEAE 1856
Cdd:COG3883 236 AAAAAAAAASAAGAGAAGAAGAAA 259
|
|
| |
